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Conserved domains on  [gi|489121859|ref|WP_003031680|]
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MULTISPECIES: maltose/maltodextrin ABC transporter substrate-binding protein MalE [Citrobacter]

Protein Classification

maltose/maltodextrin ABC transporter substrate-binding protein( domain architecture ID 11484205)

maltose/maltodextrin ABC transporter substrate-binding protein functions as the primary receptor for the active transport of maltose and higher maltodextrins such as maltotriose

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-396 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 813.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATG 80
Cdd:PRK09474   1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPA 160
Cdd:PRK09474  81 DGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 161 LDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE 240
Cdd:PRK09474 161 LDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 241 AAFNKGDTAMTINGPWAWSNIDKSKINYGVTLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLDEVN 320
Cdd:PRK09474 241 AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVN 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489121859 321 KDKPLGAVALKSFQDQLAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRITK 396
Cdd:PRK09474 321 KDKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-396 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 813.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATG 80
Cdd:PRK09474   1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPA 160
Cdd:PRK09474  81 DGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 161 LDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE 240
Cdd:PRK09474 161 LDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 241 AAFNKGDTAMTINGPWAWSNIDKSKINYGVTLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLDEVN 320
Cdd:PRK09474 241 AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVN 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489121859 321 KDKPLGAVALKSFQDQLAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRITK 396
Cdd:PRK09474 321 KDKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 31-394 0e+00

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 675.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  31 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 110
Cdd:cd13656    1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 111 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 190
Cdd:cd13656   81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 191 GGYAFKFENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKSKINYGV 270
Cdd:cd13656  161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 271 TLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLDEVNKDKPLGAVALKSFQDQLAKDPRIAATMDNA 350
Cdd:cd13656  241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 489121859 351 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd13656  321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-396 1.50e-143

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 413.96  E-value: 1.50e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGArILALSALTTMMFSA---------SALAKIEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTIEHP--DKL 69
Cdd:COG2182    1 MKRRLLA-ALALALALALALAAcgsgssssgSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  70 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVP 149
Cdd:COG2182   79 REKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 150 -NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFENGkyDVKDVGVDNAGAKAGLTFLVDLIKNK 228
Cdd:COG2182  159 aEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 229 HMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKS-KINYGVTLLPTF-KGKASKPFVGVLSAGINAASPNKELAKEFL 306
Cdd:COG2182  237 VLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 307 eNYLLTDQGLDEVNKDKPLgAVALKSFQDQ--LAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 384
Cdd:COG2182  317 -EYLTSPEAQKALFEATGR-IPANKAAAEDaeVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394

                        410
                 ....*....|..
gi 489121859 385 AALKDAQGRITK 396
Cdd:COG2182  395 EALDAAQKQIEA 406
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-341 5.52e-29

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 114.04  E-value: 5.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   48 EVGKKFEKDTGIKVTIEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 123
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  124 RYNGKLIAYPIAVEA-LSLIYNKDLVP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKFEN 199
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  200 GKyDVKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGDTAMTINGPWAWSNIDKSKINYGVTLLPtfkg 278
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPK---- 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489121859  279 kaSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDQGLDEVNKDKPLGAVALKSFQ-DQLAKDP 341
Cdd:pfam13416 218 --DGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-396 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 813.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATG 80
Cdd:PRK09474   1 MKIKKGLRTLALSALATLMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPA 160
Cdd:PRK09474  81 DGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 161 LDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAE 240
Cdd:PRK09474 161 LDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 241 AAFNKGDTAMTINGPWAWSNIDKSKINYGVTLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLDEVN 320
Cdd:PRK09474 241 AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVN 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489121859 321 KDKPLGAVALKSFQDQLAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRITK 396
Cdd:PRK09474 321 KDKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 31-394 0e+00

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 675.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  31 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 110
Cdd:cd13656    1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 111 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 190
Cdd:cd13656   81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 191 GGYAFKFENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKSKINYGV 270
Cdd:cd13656  161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 271 TLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLDEVNKDKPLGAVALKSFQDQLAKDPRIAATMDNA 350
Cdd:cd13656  241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 489121859 351 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd13656  321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-396 1.50e-143

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 413.96  E-value: 1.50e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGArILALSALTTMMFSA---------SALAKIEEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTIEHP--DKL 69
Cdd:COG2182    1 MKRRLLA-ALALALALALALAAcgsgssssgSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  70 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVP 149
Cdd:COG2182   79 REKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 150 -NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFENGkyDVKDVGVDNAGAKAGLTFLVDLIKNK 228
Cdd:COG2182  159 aEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 229 HMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKS-KINYGVTLLPTF-KGKASKPFVGVLSAGINAASPNKELAKEFL 306
Cdd:COG2182  237 VLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 307 eNYLLTDQGLDEVNKDKPLgAVALKSFQDQ--LAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 384
Cdd:COG2182  317 -EYLTSPEAQKALFEATGR-IPANKAAAEDaeVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394

                        410
                 ....*....|..
gi 489121859 385 AALKDAQGRITK 396
Cdd:COG2182  395 EALDAAQKQIEA 406
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 32-394 9.55e-141

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 405.26  E-value: 9.55e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKG-YNGLAEVGKKFEKDT-GIKVTIEHPDK--LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 107
Cdd:cd13522    1 TITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 108 DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 186
Cdd:cd13522   81 YVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 187 IAADGGYAFKFENGKYdvkDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDK-S 264
Cdd:cd13522  161 IGGFGGQVFKANNGKN---NPTLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRQaL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 265 KINYGVTLLPTFKG-KASKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLdeVNKDKPLGAVALKSFQDQLAKDPRI 343
Cdd:cd13522  238 KINLGVAPLPTFSGtKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489121859 344 A--ATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd13522  316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 32-394 1.17e-129

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 377.02  E-value: 1.17e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 109
Cdd:cd13586    1 TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 110 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPALDK--ELKAKGKSALMFNLQEPYFTWPLI 187
Cdd:cd13586   81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfNDKAGGKYGFAYDQTNPYFSYPFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 188 AADGGYAFKfENGKyDVKDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKSKI 266
Cdd:cd13586  161 AAFGGYVFG-ENGG-DPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 267 NYGVTLLPTFKG-KASKPFVGVLSAGINAASPNKELAKEFLEnYLLTDQGlDEVNKDKPLGAVALKSFQDQ--LAKDPRI 343
Cdd:cd13586  239 NFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEA-QLLLFEKTGRIPALKDALNDaaVKNDPLV 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489121859 344 AATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd13586  317 KAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 32-395 8.97e-86

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 265.12  E-value: 8.97e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTIEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 109
Cdd:cd13658    1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 110 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFTWPLI 187
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtkEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 188 AADGGYAFKFENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKSKIN 267
Cdd:cd13658  161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 268 YGVTLLPTF-KGKASKPFVGVLSAGINAASPNKELAKEFLEnYLLTDQGL----DEVNKDKPLGAVALKSfqdQLAKDPR 342
Cdd:cd13658  241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLkkryDETNEIPPRKDVRSDP---EIKNNPL 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489121859 343 IAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRIT 395
Cdd:cd13658  317 TSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIK 369
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 32-394 7.24e-73

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 231.88  E-value: 7.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKGY-NGLAEVGKKFEKDTGI---KVTIEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT- 106
Cdd:cd13657    1 TITIWHALTGAEeDALQQIIDEFEAKYPVpnvKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 107 ---PDKAfqDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPY 181
Cdd:cd13657   81 ylsEDDF--ENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtdPAAGSYGLAYQVSDAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 182 FTWPLIAADGGYAFKFENGKydvkdVGVDNAGAKAGLTFLVDLIKnKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNI 261
Cdd:cd13657  159 FVSAWIFGFGGYYFDDETDK-----PGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 262 DKSKINYGVTLLPTFKG-KASKPFVGVLSAGI--NAASPNKELAKEFLENYLLTDQGLDEVNKDKPLGAVALKSFQDQLA 338
Cdd:cd13657  233 KAAGIDLGVAPLPTVDGtNPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVA 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489121859 339 KDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd13657  313 ADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 32-391 1.02e-53

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 182.60  E-value: 1.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKGY-NGLAEVGKKFEK-DTGIKVTIEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 107
Cdd:cd13585    1 TLTFWDWGQPAEtAALKKLIDAFEKeNPGVKVEVVPVpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 108 ---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDL------VPNPPKTWEEIPALDKELKAKGKS----ALM 174
Cdd:cd13585   81 yieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLfdkagpGPKPPWTWDELLEAAKKLTDKKGGqygfALR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 175 FNLQEPYFTWPLIAADGGYAFKFENGKydvkdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEA--AFNKGDTAMTI 252
Cdd:cd13585  161 GGSGGQTQWYPFLWSNGGDLLDEDDGK-----ATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAMMI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 253 NGPWAWSNIDKSKI--NYGVTLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLEnYLLTDQG---LDEVNKDKPLGA 327
Cdd:cd13585  236 DGPWALGTLKDSKVkfKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENqlkLGGAAGPAALAA 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489121859 328 VALKSFQDQLAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASG--RQTVDAALKDAQ 391
Cdd:cd13585  315 AAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAA 380
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-352 5.45e-53

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 180.24  E-value: 5.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGARILALSALTTMMFSASALAKIEEGK--LVIWINGDKGYNGLAEVGKKFEKDT-GIKVTIEHP--DKLEEKFPQ 75
Cdd:COG1653    1 MRRLALALAAALALALAACGGGGSGAAAAAGKvtLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  76 VAATGDGPDIIFWAHDRFGGYAQSGLLAEITP----DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVP-- 149
Cdd:COG1653   81 ALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEka 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 150 --NPPKTWEEIPALDKELKAK-GKSALMFNLQEPYFTWPLIAADGGYAFKfENGKydvkdVGVDNAGAKAGLTFLVDLIK 226
Cdd:COG1653  161 glDPPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLYD-EDGK-----PAFDSPEAVEALEFLKDLVK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 227 NKHMNAD---TDYSIAEAAFNKGDTAMTINGPWAWSNIDKS--KINYGVTLLPTFK-GKASKPFVGVLSAGINAASPNKE 300
Cdd:COG1653  235 DGYVPPGalgTDWDDARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNPE 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489121859 301 LAKEFLEnYLLTDQgldevnkdkplGAVALKSFQDQLAKDPRIAATMDNAQK 352
Cdd:COG1653  315 AAWKFLK-FLTSPE-----------AQAKWDALQAVLLGQKTPEEALDAAQA 354
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 51-394 9.29e-52

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 177.48  E-value: 9.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  51 KKFEK-DTGIKVTIEHP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP----DKAFQDKLYPFTWDA 122
Cdd:cd14748   21 DEFNKsHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDyidkDGVDDDDFYPAALDA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 123 VRYNGKLIAYPIAVEALSLIYNKDL-------VPNPPKTWEEI----PALDKELKAKGKSALMFNLQEPYFTW-PLIAAD 190
Cdd:cd14748  101 GTYDGKLYGLPFDTSTPVLYYNKDLfeeagldPEKPPKTWDELeeaaKKLKDKGGKTGRYGFALPPGDGGWTFqALLWQN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 191 GGYAFKFENGKydvkdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGDTAMTINGPWAWSNIDK--SKINY 268
Cdd:cd14748  181 GGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIRDkgAGFEY 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 269 GVTLLPTFKGKASKPFVGVLSAGINAASP-NKELAKEFLEnYLLTDQGLDEVNKDK---PLGAVALKSFQDQLAKDPRIA 344
Cdd:cd14748  256 GVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATgylPVRKSAAEDPEEFLAENPNYK 334

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489121859 345 ATMDNAQKG-EIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd14748  335 VAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 41-394 2.14e-37

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 139.35  E-value: 2.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  41 KGYNGLAEVGKKFEKDT-GIKVTIEH----PDKLEEKFPQVAATGD-GPDII----FWAhdrfGGYAQSGLLAEITPD-- 108
Cdd:cd14750   11 QEGELLKKAIAAFEKKHpDIKVEIEElpasSDDQRQQLVTALAAGSsAPDVLgldvIWI----PEFAEAGWLLPLTEYlk 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 109 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVP----NPPKTWEEIPALDKELKAKGKSALMFNLQ----EP 180
Cdd:cd14750   87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVFQgkqyEG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 181 YFT--WPLIAADGGYAFKFENGKydvkdVGVDNAGAKAGLTFLVDLIKNKHM-NADTDYSIAEA--AFNKGDTAMTINGP 255
Cdd:cd14750  167 LVCnfLELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISpKGVLTYGEEEAraAFQAGKAAFMRNWP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 256 WAWSNIDKSKINY----GVTLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLEnYLLTDQGLDEVNKDKPLGAVALK 331
Cdd:cd14750  242 YAYALLQGPESAVagkvGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPPTRRA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489121859 332 SFQDQ--LAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQGRI 394
Cdd:cd14750  321 LYDDPevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEKL 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 32-391 5.47e-36

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 135.59  E-value: 5.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIW--INGDKGYNGLAEVGKKFEK---DTGIKVTIEHPDKLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEI 105
Cdd:cd14749    1 TITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 106 TP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDL-----VPNPPKTWEEIPALDKELKAKGKSALMFNL 177
Cdd:cd14749   81 TDyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLfeeagGVKPPKTWDELIEAAKKDKFKAKGQTGFGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 178 Q---EPYFTW-PLIAADGGYAFKFENGkyDVKDVGVDNAGAKAgLTFLVDLIKNKHMNADT---DYSIAEAAFNKGDTAM 250
Cdd:cd14749  161 LlgaQGGHWYfQYLVRQAGGGPLSDDG--SGKATFNDPAFVQA-LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKAAM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 251 TINGPWAWSNIDKS--KINYGVTLLPTFKGKA--SKPFVGVLSAGINAASPNKELAKEFLeNYLLTDQGLDEVNKDKPLG 326
Cdd:cd14749  238 NIGGSWDLGAIKAGepGGKIGVFPFPTVGKGAqtSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQYLEDVGLL 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489121859 327 AVALKSFQDQLAKDPRIAATMD--NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQ 391
Cdd:cd14749  317 PAKEVVAKDEDPDPVAILGPFAdvLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQ 383
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 32-396 3.50e-35

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 133.21  E-value: 3.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKGYNG-LAEVGKKFEKDT-GIKVTIEH------PDKLEEKfpqvAATGDGPDIIFWAHDRFGGYAQSGLLA 103
Cdd:cd14747    1 TLTVWAMGNSAEAElLKELADEFEKENpGIEVKVQVlpwgdaHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 104 EITP---DKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDL-----VPNPPKTWEEIPALDKELKAKG--KSAL 173
Cdd:cd14747   77 DLTPyleDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLlkkagGDEAPKTWDELEAAAKKIKADGpdVSGF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 174 MF----NLQEPYFTWpLIAADGGYAfkfengKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIA--EAAFNKGD 247
Cdd:cd14747  157 AIpgknDVWHNALPF-VWGAGGDLA------TKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQAFANGK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 248 TAMTINGPWAWSNIDKS----KINYGVTLLPTFKGKASKPFVGVLSAGINAASPNKELAKEFLEnYLLTDQGLDEVNKDK 323
Cdd:cd14747  230 VAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKAT 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489121859 324 PLGAVALKSFQD-QLAKDPRIAATMDNAQKGEIMPNIPQmsafWYAVRTAVINA-----ASGRQTVDAALKDAQGRITK 396
Cdd:cd14747  309 GMLPANTSAWDDpSLANDPLLAVFAEQLKTGKATPATPE----WGEIEAELVLVleevwIGVGADVEDALDKAAAEINE 383
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-341 5.52e-29

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 114.04  E-value: 5.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   48 EVGKKFEKDTGIKVTIEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITPDKAFqDKLYPFTwDAV 123
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL-DDLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  124 RYNGKLIAYPIAVEA-LSLIYNKDLVP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKFEN 199
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  200 GKyDVKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGDTAMTINGPWAWSNIDKSKINYGVTLLPtfkg 278
Cdd:pfam13416 146 GV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPK---- 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489121859  279 kaSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDQGLDEVNKDKPLGAVALKSFQ-DQLAKDP 341
Cdd:pfam13416 218 --DGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 43-315 3.37e-28

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 112.12  E-value: 3.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   43 YNGLAEVGKKFEKD-TGIKVTIE--HPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPf 118
Cdd:pfam01547   7 AAALQALVKEFEKEhPGIKVEVEsvGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  119 twdavrynGKLIAYPIAVEALSLIYNKDLVPN----PPKTWEEIPALDKELKAKGKSALMFNLQEP-----YFTWPLIAA 189
Cdd:pfam01547  86 --------PKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  190 DGGYAFKfENGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKSKI- 266
Cdd:pfam01547 158 LGGPLFD-KDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPgvAGADGREALALFEQGKAAMGIVGPWAALAANKVKLk 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489121859  267 ------------NYGVTLLPTFKGKAskpfVGVLSAGINAASPNKELAKEFLeNYLLTDQG 315
Cdd:pfam01547 237 vafaapapdpkgDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEA 292
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 53-390 4.78e-28

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 113.63  E-value: 4.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  53 FEKDT-GIKVTIE-HP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQD--KLYPFTWDAVRYNG 127
Cdd:cd14751   23 FEKEYpKIKVKAVrVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNRYNG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 128 KLIAYPIAVEALSLIYNKDLVPN----PPKTWEEIPALDKE-LKAKGKSALMFNLQEPYFTWPLIAADGGyafKFENGky 202
Cdd:cd14751  103 HYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLLPFLWSFGG---DLTDE-- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 203 DVKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGDTAMTINGPWAWSNIDKSKI-----NYGVTLLPT 275
Cdd:cd14751  178 KKATGYLNSPESVRALETIVDLYDEGAITpcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdNLGIAPVPA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 276 FKGKASKPfVGVLSAGINAASPNKELAKEFLEnYLLTDQGLDEVNKDK---PLGAVALKSfqDQLAKDPRIAATMDNAQK 352
Cdd:cd14751  258 GPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTAAKLgllPTRTSAYES--PEVANNPMVAAFKPALET 333

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 489121859 353 GEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDA 390
Cdd:cd14751  334 AVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 82-366 3.99e-22

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 96.65  E-value: 3.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  82 GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDK--LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD-LVPNPPKTWEEI 158
Cdd:cd13655   53 AADVFAFANDQLGELVDAGAIYPLTGSAVDKIKntNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSkLTEDDVKSLDTM 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 159 paLDKELKAKGKSAlmFNLQEPYFTWPLIAADGGYAFKfeNGKYDVKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSi 238
Cdd:cd13655  133 --LAKAPDAKGKVS--FDLSNSWYLYAFFFGAGCKLFG--NNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGD- 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 239 AEAAFNKGDTAMTINGPWAWSNIDKS-KINYGVTLLPTFK--GKAS--KPFVGVLSAGINAASPNKELAKEFLEnYLLTD 313
Cdd:cd13655  206 AISGLKDGTLGAGVSGPWDAANLKKAlGDNYAVAKLPTYTlgGKDVqmKSFAGYKAIGVNSNTKNPEAAMALAD-YLTNE 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489121859 314 QG---LDEVNKDKPLGAVALKSfqDQLAKDPRIAATMDNAQKGEI-MPNIPQMSAFW 366
Cdd:cd13655  285 ESqltRFEKRGIGPTNKEAAES--DAVKADPAAKALIAQSNEASVvQPKLPKMSNFW 339
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-361 1.30e-17

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 83.04  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGARILALSALTTMMFSASALAkiEEGKLVIWINGdkGYNGlAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATG 80
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGGAPAAA--AEGTLNVYNWG--GYID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  81 DGPDIIFWAHDRFGGYAQSGLLAEITPDK--AFQDkLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEI 158
Cdd:COG0687   76 SGYDVVVPSDYFVARLIKAGLLQPLDKSKlpNLAN-LDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 159 paLDKELkaKGKSALmfnLQEPYFTWPLIAADGGYAFkfengkYDVKDVGVDNAGAKagltflvdLIKNKHMNA--DTDY 236
Cdd:COG0687  155 --WDPEY--KGKVAL---LDDPREVLGAALLYLGYDP------NSTDPADLDAAFEL--------LIELKPNVRafWSDG 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 237 SIAEAAFNKGDT--AMTINGPWAWSNIDKSKINY-----GVTLlptfkgkaskpFVGVLSagINAASPNKELAKEFLeNY 309
Cdd:COG0687  214 AEYIQLLASGEVdlAVGWSGDALALRAEGPPIAYvipkeGALL-----------WFDNMA--IPKGAPNPDLAYAFI-NF 279

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489121859 310 LLTDQGLDEVNKDKPLGAV---ALKSFQDQLAKDPRIAATMDNAQKGEIMPNIPQ 361
Cdd:COG0687  280 MLSPEVAAALAEYVGYAPPnkaARELLPPELAANPAIYPPEEVLDKLEFWNPLPP 334
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 48-311 2.32e-10

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 61.10  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  48 EVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAVRY 125
Cdd:cd13590   14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNLKNLDPQFLNPPYD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 126 NGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEiPALDKELkaKGKSAlMFNLQEPYFTWPLIAAdgGYAFkfengkYDVK 205
Cdd:cd13590   94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL-DLWDPAL--KGRIA-MLDDAREVLGAALLAL--GYSP------NTTD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 206 DVGVDNAGAKagltflvdLIKNKHMNADTDYSIAEAAFNKGDT--AMTINGPWAWSNIDKSKINY-----GVTLlptfkg 278
Cdd:cd13590  162 PAELAAAAEL--------LIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKFvipkeGGLL------ 227

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489121859 279 kaskpfvGVLSAGINAASPNKELAKEFLeNYLL 311
Cdd:cd13590  228 -------WVDNMAIPKGAPNPELAHAFI-NFLL 252
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 51-315 4.42e-10

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 59.95  E-value: 4.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  51 KKFEKDTGIKVTIEHPDKLEEkFPQVAATGDGP--DIIF-WAHDRFGGYAQSGLLAEITPDKA------FQDKLYpfTWd 121
Cdd:COG1840    3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWsGDADALEQLANEGLLQPYKSPELdaipaeFRDPDG--YW- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 122 avryngkliaYPIAVEALSLIYNKDLVP--NPPKTWEEIpaLDKELKAKgksalmfnlqepyFTWPLIAADG-GYAFkfe 198
Cdd:COG1840   79 ----------FGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYKGK-------------IAMADPSSSGtGYLL--- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 199 ngkydvkdVG--VDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAfNKGDTAMTINGPWAWSNIDKSKINYGVTLlptF 276
Cdd:COG1840  131 --------VAalLQAFGEEKGWEWLKGLAANGARVTGSSSAVAKAV-ASGEVAIGIVNSYYALRAKAKGAPVEVVF---P 198

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489121859 277 KGKAskpFVGVLSAGINAASPNKELAKEFLEnYLLTDQG 315
Cdd:COG1840  199 EDGT---LVNPSGAAILKGAPNPEAAKLFID-FLLSDEG 233
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-323 4.45e-09

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  51 KKFEKDTGIKVTIEH--PDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITPdkaFQDKLYP--------FT 119
Cdd:cd13580   26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTD---YLDKYYPnlkkiieqEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 120 WDAVRYNGKLIAYPIAVEALS---LIYNKDLVPN----PPKTWEEipaLDKELKA--------KGK----SALMFNLQEP 180
Cdd:cd13580  103 WDSASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDE---LYEVAKAftekdpdgNGKkdtyGLTDTKDLIG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 181 YFTWPLIAADGGYA---FKFENGKydVKDVGVDNAgAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGDTAMTING 254
Cdd:cd13580  180 SGFTGLFGAFGAPPnnwWKDEDGK--LVPGSIQPE-MKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGIFVGN 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 255 PWA----------------WSNIDKSKINYGvtllptFKGKASKPFVGVLSAgINAASPNKELAKEFL------ENYLLT 312
Cdd:cd13580  257 WWDpawpqaslkkndpdaeWVAVPIPSGPDG------KYGVWAESGVNGFFV-IPKKSKKPEAILKLLdflsdpEVQKLL 329

                        330
                 ....*....|.
gi 489121859 313 DQGLDEVNKDK 323
Cdd:cd13580  330 DYGIEGVHYTV 340
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 49-315 1.49e-07

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 53.23  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  49 VGKKFEKDTGIKVTIEH--PDKLEEKFPQVAATGDGPDII---FWAhDRFGGYAQSGLLAEITPD-------KAFQDKLY 116
Cdd:cd13521   22 VAKEIEKLTNVKLEIVAvtAATSQQKLNLMLASGDLPDIVgadYLK-DKFIAYGMEGAFLPLSKYidqypnlKAFFKQHP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 117 --PFTWDAVRYNGKLIAY--PIAVEALSLIYNKDLVPN----PPKTWEEIPALDKELKAKGKSAlmfNLQEPyfTWPLIA 188
Cdd:cd13521  101 dvLRASTASDGKIYLIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKDPNG---NGKAD--EIPFID 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 189 ADGGY-AFKFENGKYDVKDVGVDNAG----------------AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGDT 248
Cdd:cd13521  176 RDPLYgAFRLINSWGARSAGGSTDSDwyedngkfkhpfaseeYKDGMKYMNKLYTEGLIDKEsftQKDDQAEQKFSNGKL 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 249 AMTINGPWAWSN-----IDKSKINYGvtLLPTFKGKASKPFVGVLSAG--------INAASPNKELAKEFLeNYLLTDQG 315
Cdd:cd13521  256 GGFTHNWFASDNlftaqLGKEKPMYI--LLPIAPAGNVKGRREEDSPGytgpdgvaISKKAKNPVAALKFF-DWLASEEG 332
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 47-314 2.30e-07

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 51.84  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  47 AEVGKKFEKDTGIKVTIEHPDKLEEKfPQVAATGDGP--DIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYPFTWDAV 123
Cdd:cd13589   17 KAVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYSKiPNAAKDKAPAALKT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 124 RYngkliAYPIAVEALSLIYNKDLVPNPPKTWeeiPALDKELKAK--GKSALmfNLQEPYFTWPLIAADGGyafkfengk 201
Cdd:cd13589   96 GY-----GVGYTLYSTGIAYNTDKFKEPPTSW---WLADFWDVGKfpGPRIL--NTSGLALLEAALLADGV--------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 202 yDVKDVGVDNAGAKagltflVDLIKNkhmNADTDY-SIAEAA--FNKGDTAMTINGPWAWSNIDKSKINYGVTLlptfkg 278
Cdd:cd13589  157 -DPYPLDVDRAFAK------LKELKP---NVVTWWtSGAQLAqlLQSGEVDMAPAWNGRAQALIDAGAPVAFVW------ 220

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489121859 279 KASKPFVGVLSAGINAASPNKELAKEFLeNYLLTDQ 314
Cdd:cd13589  221 PKEGAILGPDTLAIVKGAPNKELAMKFI-NFALSPE 255
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 47-151 2.88e-07

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 51.67  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  47 AEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAAT-GDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVR- 124
Cdd:cd13587   13 EDLLEKFENETGIKVQVTTSNNNEEMISKLRATgGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 489121859 125 ---YNGKLIAYPIAVEALSLIYNKDLVPNP 151
Cdd:cd13587   93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 41-168 4.26e-07

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 51.14  E-value: 4.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  41 KGYnGLAEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK-AFQDKLYP-F 118
Cdd:cd13588    8 PGY-ADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKiPNYANIDPrL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489121859 119 TW-DAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPAlDKELKAK 168
Cdd:cd13588   87 RNlPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLW-DPKYKGR 136
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
126-274 8.44e-06

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 47.49  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 126 NGKLIAYPIAVEALSLIYNKD------LVPN-PPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKFE 198
Cdd:PRK10974 134 TGHLLSQPFNSSTPVLYYNKDafkkagLDPEqPPKTWQDLAAYAAKLRAAGMKCGYASGWQGWIQLENFSAWHGLPFASK 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 199 NGKYDvkdvgvdnaGAKAGLTFLVDLiKNKH------MNADTDYSI------AEAAFNKGDTAMTINGPWAWSNIDK-SK 265
Cdd:PRK10974 214 NNGFD---------GTDAVLEFNKPE-QVKHialleeMNKKGDFTYvgrkdeSTEKFYNGDCAITTASSGSLANIRKyAK 283


                 ....*....
gi 489121859 266 INYGVTLLP 274
Cdd:PRK10974 284 FNYGVGMMP 292
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 32-168 2.54e-05

Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270236 [Multi-domain]  Cd Length: 260  Bit Score: 45.37  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  32 KLVIWINGDKgyNGLAEVGKKFEKDTGIKVTIEHpDKLEEKFPQVAATGDGP--DIiFWAHD--RFGGYAQSGLLAEITP 107
Cdd:cd13518    1 ELVVYTASDR--DFAEPVLKAFEEKTGIKVKAVY-DGTGELANRLIAEKNNPqaDV-FWGGEiiALEALKEEGLLEPYTP 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489121859 108 DkafQDKLYPFTWDAVryNGKLiaYPIAVEALSLIYNKDLVPNP--PKTWEEIpaLDKELKAK 168
Cdd:cd13518   77 K---VIEAIPADYRDP--DGYW--VGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKWKGK 130
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 52-168 6.25e-05

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 44.35  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  52 KFEKDTGIKVTIEHPDKLEEKFPQVAATGDGP-DIIFwahdrFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRY----- 125
Cdd:cd13523   18 PFEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVT-----PSDSYTSRQLGVGLMQPIDKSLLPSWATLDPHLtlaav 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489121859 126 ---NGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPaLDKELKAK 168
Cdd:cd13523   93 ltvPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADL-DDPKYKGR 137
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 48-108 7.00e-05

TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270382 [Multi-domain]  Cd Length: 315  Bit Score: 44.27  E-value: 7.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489121859  48 EVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 108
Cdd:cd13664   14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKS 74
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 51-155 9.88e-05

The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270380  Cd Length: 312  Bit Score: 44.05  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  51 KKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEItpDKAfqdKLYPFTWDAVRYNGKLI 130
Cdd:cd13662   17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKL--DKS---KLPNVKEEKDNLMEASK 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489121859 131 AY--------PIAVEALSLIYNKDLVPNPPKTW 155
Cdd:cd13662   92 IYdpgleysvPYMFGATGIAVNKKIVKNYFRKW 124
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-315 2.61e-04

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 43.11  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  51 KKFEKDTGIKVTIEH--PDKLEEKFPQVAATGDGPDII--FWaHDRFGGYAQSGLLAEITP--DKA--FQDKLYPFTW-- 120
Cdd:cd13583   24 KEIEEKTNVKFKRTPipSSDYETKRSLLIASGDAPDIIpvLY-PGEENEFVASGALLPISDylDYMpnYKKYVEKWGLgk 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 121 --DAVRY-NGKLIAYPIAVEA----LSLIYNKDL-----VPnPPKTWEEIPALDKELKAK----------GKSALMFNLQ 178
Cdd:cd13583  103 elATGRQsDGKYYSLPGLHEDpgvqYSFLYRKDIfekagIK-IPTTWDEFYAALKKLKEKypdsypysdrWNSNALLLIA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 179 EPYFTWPLIAADGGYAFKFENGKYdVKDVGVDNagAKAGLTFLVDLIKNKHMN----ADTDySIAEAAFNKGDTAMTING 254
Cdd:cd13583  182 APAFGTTAGWGFSNYTYDPDTDKF-VYGATTDE--YKDMLQYFNKLYAEGLLDpesfTQTD-DQAKAKFLNGKSFVITTN 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489121859 255 PW-----AWSNIDKSKINYGVTLLPTFKGKASK------PFVGVLSAGINAASPNKELAKEFLeNYLLTDQG 315
Cdd:cd13583  258 PQtvdelQRNLRAADGGNYEVVSITPPAGPAGKaingsrLENGFMISSKAKDSKNFEALLQFL-DWLYSDEG 328
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 1-191 9.52e-04

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 40.82  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859   1 MKIKTGARILALSALTTMMFSASAL---AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTI------EHPDKL-- 69
Cdd:PRK15046   1 MRSTNRAAAAAAMKLAAAAAAAAFGggaAPAWAADAVTVYSADGLEDWYQDVFPAFTKATGIKVNYveagsgEVVNRAak 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  70 EEKFPQVAATGDGPDIIFWAhdrfggyAQSGLLAEITPDKAfqDKLYPFTWDAvryNGKLiaYPIAVEALSLIYNKDLVP 149
Cdd:PRK15046  81 EKSNPQADVLVTLPPFIQQA-------AAEGLLQPYSSVNA--KAVPAIAKDA---DGTY--APFVNNYLSFIYNPKVLK 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489121859 150 NPPKTWEEIpaLDKELKAKgksalmfnLQepYFTwPLIAADG 191
Cdd:PRK15046 147 TAPATWADL--LDPKFKGK--------LQ--YST-PGQAGDG 175
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 47-166 1.55e-03

ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 40.22  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  47 AEVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYA-QSGLLAEITPDKAFQDKLyPFTWDAv 123
Cdd:COG4143   48 PWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPkaDVVLGLDNNLLARAlDTGLFAPHGVDALDALAL-PLAWDP- 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489121859 124 ryNGKLIayPIAVEALSLIYNKDLVPNPPKTWEEIPALDKELK 166
Cdd:COG4143  126 --DDRFV--PYDYGYFAFVYDKTKLLNPPESLEDLVDPEYKDK 164
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 48-325 1.81e-03

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 39.59  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  48 EVGKKFEKDTGIKVTIEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYAQS-GLLAEITPdkafqdKLYPFTWDAVR 124
Cdd:cd13545   19 EVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPraDVVLGLDNNLLSRALKeGLFEPYRS------PALDVVPEVPV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 125 YNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEipaldkelkakgksalmfnLQEPYFTWPLIAADG-----GYAFKFen 199
Cdd:cd13545   93 FDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLED-------------------LTAPEYKGLIVVQDPrtsspGLGFLL-- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 200 gkYDVKDVGVDNAgakagLTFLVDLIKNKHMNADTdYSIAEAAFNKGDTAMTI---NGPwAWSNIDKSKINYGVTLLPTf 276
Cdd:cd13545  152 --WTIAVFGEEGY-----LEYWKKLKANGVTVTPG-WSEAYGLFTTGEAPMVVsyaTSP-AYHVYYEKDLRYTAVIFPE- 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 489121859 277 kGKaskpFVGVLSAGINAASPNKELAKEFLEnYLLTdqglDEVNKDKPL 325
Cdd:cd13545  222 -GH----YRQVEGAGILKGAKNPELAKKFVD-FLLS----PEFQEVIPE 260
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 53-314 2.56e-03

Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270266 [Multi-domain]  Cd Length: 310  Bit Score: 39.47  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859  53 FEKDTGIKV---------TIEHPDKlEEKFPQVAATGDGPDIIFWAHdrfggyaQSGLLAEITPDKAFQDklypftwDAV 123
Cdd:cd13548   21 FTKATGITVnyveagsgeVVERAAK-EKSNPQADVLVTLPPFIQQAA-------QMGLLQPYQSDAAKNP-------AII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 124 RYNGKLIAyPIAVEALSLIYNKDLVPNPPKTWEEI--PALDKEL------KAKGKSALMFNLQEpyftwpLIAADGGYAF 195
Cdd:cd13548   86 KAEDGTYA-PLVNNYFSFIYNSAVLKNAPKTFADLldPKYKGKIqystpgQAGDGMAVLLLTTH------LMGSDAAFAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489121859 196 kfengkydVKDVGVDNAGAKAGLTFLVDLIknkhmnadtdySIAEAAFNKGDTAMTIngpwawSNIDKSKINYGVtLLPT 275
Cdd:cd13548  159 --------LAKLQQNNVGPSASTGKLTALV-----------SKGEISVANGDLQMNL------AQMEHANPNKKI-FWPA 212

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489121859 276 FKGKASKPFVGVLSAGINAASPNKELAKEfLENYLLTDQ 314
Cdd:cd13548  213 KAGGQRSTFALPYGIGLVKGAPNADNGKK-LIDFLLSKE 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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