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Conserved domains on  [gi|15830188|ref|NP_308961|]
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putrescine ABC transporter periplasmic binding protein [Escherichia coli O157:H7 str. Sakai]

Protein Classification

polyamine ABC transporter substrate-binding protein( domain architecture ID 10793442)

polyamine ABC transporter substrate-binding protein serves as a primary receptor for the active transport of polyamines such as putrescine and spermidine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
1-370 0e+00

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


:

Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 792.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
Cdd:PRK10682   1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   81 LVVPSASFLERQLTAGVFQPLDKSKLPEWKNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPVDSW 160
Cdd:PRK10682  81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  161 DLILKPENLEKLKSCGVSFLDAPEEVFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  241 AIGWAGDVWQASNRAKEAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKA 320
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15830188  321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQAPKIDRVRTRAWTKVKSGK 370
Cdd:PRK10682 321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
 
Name Accession Description Interval E-value
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
1-370 0e+00

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 792.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
Cdd:PRK10682   1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   81 LVVPSASFLERQLTAGVFQPLDKSKLPEWKNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPVDSW 160
Cdd:PRK10682  81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  161 DLILKPENLEKLKSCGVSFLDAPEEVFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  241 AIGWAGDVWQASNRAKEAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKA 320
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15830188  321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQAPKIDRVRTRAWTKVKSGK 370
Cdd:PRK10682 321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
PBP2_PotF cd13659
The periplasmic substrate-binding component of an ABC putrescine transport system and related ...
31-363 0e+00

The periplasmic substrate-binding component of an ABC putrescine transport system and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic substrate-binding domain that serves as the primary polyamine receptor of ABC-type putrescine-preferential transporter from gram-negative 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: 270377 [Multi-domain]  Cd Length: 331  Bit Score: 561.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWK 110
Cdd:cd13659   1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 111 NLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPvDSWDLILKPENLEKLKSCGVSFLDAPEEVFATV 190
Cdd:cd13659  81 NLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLP-DSWDLVFDPENLSKLKSCGVSVLDSPEEVFPAA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 191 LNYLGKDPNSTKADDYtGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAKNGVNVSFSIPK 270
Cdd:cd13659 160 LNYLGLDPNSTDPEDI-KAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQRAKEAGNGVTLEYVIPK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 271 EGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNPGIYPPADVRAKLFTLKV 350
Cdd:cd13659 239 EGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPP 318
                       330
                ....*....|...
gi 15830188 351 QAPKIDRVRTRAW 363
Cdd:cd13659 319 LSAKVQRALTRAW 331
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
4-367 2.57e-145

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 415.08  E-value: 2.57e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   4 LNKKWLSGLVAGALMAVSVG--TLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDL 81
Cdd:COG0687   1 MSRRSLLGLAAAALAAALAGgaPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  82 VVPSASFLERQLTAGVFQPLDKSKLPEWKNLDPELLKLvaKHDPDNKFAMPYMWATTGIGYNVDKVKavlgenAPVDSWD 161
Cdd:COG0687  81 VVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDP--PFDPGNVYGVPYTWGTTGIAYNTDKVK------EPPTSWA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 162 LILKPENLEKlkscgVSFLDAPEEVFATVLNYLGKDPNSTKADDYTgPATDLLLKLRPNIRYFHSS--QYINDLANGDIC 239
Cdd:COG0687 153 DLWDPEYKGK-----VALLDDPREVLGAALLYLGYDPNSTDPADLD-AAFELLIELKPNVRAFWSDgaEYIQLLASGEVD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 240 VAIGWAGDVWQAsnrakeAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANK 319
Cdd:COG0687 227 LAVGWSGDALAL------RAEGPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNK 300
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15830188 320 AATPLVSAEVRDNPGIYPPADVRAKLFTLKVQAPKIDRVRTRAWTKVK 367
Cdd:COG0687 301 AARELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
46-335 5.54e-22

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 94.39  E-value: 5.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    46 VANFEKETGIKVVYDVFDSNEvLEGKLM----AGSTG-FDLVVPSASFLERQLTAGVFQPLDKskLPEWKNLDPellkLV 120
Cdd:pfam13416   3 AKAFEKKTGVTVEVEPQASND-LQAKLLaaaaAGNAPdLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPD----AL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   121 AKHDPDNKF-AMPYMW-ATTGIGYNVDKVKAvlgENAPVDSWDLILkpENLEKLKSCgVSFLDAPEEVFATVLNYLGKDP 198
Cdd:pfam13416  76 DAAGYDGKLyGVPYAAsTPTVLYYNKDLLKK---AGEDPKTWDELL--AAAAKLKGK-TGLTDPATGWLLWALLADGVDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   199 N-STKADDYTGPATDLLLKLRPNIRYF-HSSQYINDLANGDICVAIGWAGDVwqasnrAKEAKNGVNVSFSIPKEGAMAF 276
Cdd:pfam13416 150 TdDGKGVEALDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAA------AAAKKAGKKLGAVVPKDGSFLG 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   277 FDVFAMPADAKNKDE-AYQFLNYLLRPDVVAHISDHVFYANANKAATPlvSAEVRDNPGI 335
Cdd:pfam13416 224 GKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAAL--SDEVKADPAL 281
 
Name Accession Description Interval E-value
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
1-370 0e+00

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 792.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
Cdd:PRK10682   1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   81 LVVPSASFLERQLTAGVFQPLDKSKLPEWKNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPVDSW 160
Cdd:PRK10682  81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  161 DLILKPENLEKLKSCGVSFLDAPEEVFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  241 AIGWAGDVWQASNRAKEAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKA 320
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15830188  321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQAPKIDRVRTRAWTKVKSGK 370
Cdd:PRK10682 321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
PBP2_PotF cd13659
The periplasmic substrate-binding component of an ABC putrescine transport system and related ...
31-363 0e+00

The periplasmic substrate-binding component of an ABC putrescine transport system and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic substrate-binding domain that serves as the primary polyamine receptor of ABC-type putrescine-preferential transporter from gram-negative 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: 270377 [Multi-domain]  Cd Length: 331  Bit Score: 561.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWK 110
Cdd:cd13659   1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 111 NLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPvDSWDLILKPENLEKLKSCGVSFLDAPEEVFATV 190
Cdd:cd13659  81 NLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLP-DSWDLVFDPENLSKLKSCGVSVLDSPEEVFPAA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 191 LNYLGKDPNSTKADDYtGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAKNGVNVSFSIPK 270
Cdd:cd13659 160 LNYLGLDPNSTDPEDI-KAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQRAKEAGNGVTLEYVIPK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 271 EGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNPGIYPPADVRAKLFTLKV 350
Cdd:cd13659 239 EGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPP 318
                       330
                ....*....|...
gi 15830188 351 QAPKIDRVRTRAW 363
Cdd:cd13659 319 LSAKVQRALTRAW 331
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
4-367 2.57e-145

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 415.08  E-value: 2.57e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   4 LNKKWLSGLVAGALMAVSVG--TLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDL 81
Cdd:COG0687   1 MSRRSLLGLAAAALAAALAGgaPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  82 VVPSASFLERQLTAGVFQPLDKSKLPEWKNLDPELLKLvaKHDPDNKFAMPYMWATTGIGYNVDKVKavlgenAPVDSWD 161
Cdd:COG0687  81 VVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDP--PFDPGNVYGVPYTWGTTGIAYNTDKVK------EPPTSWA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 162 LILKPENLEKlkscgVSFLDAPEEVFATVLNYLGKDPNSTKADDYTgPATDLLLKLRPNIRYFHSS--QYINDLANGDIC 239
Cdd:COG0687 153 DLWDPEYKGK-----VALLDDPREVLGAALLYLGYDPNSTDPADLD-AAFELLIELKPNVRAFWSDgaEYIQLLASGEVD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 240 VAIGWAGDVWQAsnrakeAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANK 319
Cdd:COG0687 227 LAVGWSGDALAL------RAEGPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNK 300
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15830188 320 AATPLVSAEVRDNPGIYPPADVRAKLFTLKVQAPKIDRVRTRAWTKVK 367
Cdd:COG0687 301 AARELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
31-363 1.12e-126

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: 366.56  E-value: 1.12e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGS-TGFDLVVPSASFLERQLTAGVFQPLDKSKLPEW 109
Cdd:cd13590   1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGgSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 110 KNLDPELLKLvaKHDPDNKFAMPYMWATTGIGYNVDKVKAvlgenaPVDSWDLILKPENLeklkSCGVSFLDAPEEVFAT 189
Cdd:cd13590  81 KNLDPQFLNP--PYDPGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPAL----KGRIAMLDDAREVLGA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 190 VLNYLGKDPNSTKADDyTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKeakngvNVSFSIP 269
Cdd:cd13590 149 ALLALGYSPNTTDPAE-LAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENP------NLKFVIP 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 270 KEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNPGIYPPADVRAKLFTLK 349
Cdd:cd13590 222 KEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFK 301
                       330
                ....*....|....
gi 15830188 350 VQAPKIDRVRTRAW 363
Cdd:cd13590 302 DVDGEALELYDRIW 315
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
31-311 5.94e-121

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: 350.20  E-value: 5.94e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMA-GSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEW 109
Cdd:cd13523   1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAgGSGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 110 KNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENapvdswdlilKPENLEKLKSCGVSFLDAPEEVFAT 189
Cdd:cd13523  81 ATLDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDKVKAPPKSY----------AADLDDPKYKGRVSFSDIPRETFAM 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 190 VLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHS--SQYINDLANGDICVAIGWAGDVWQASNRakeaknGVNVSFS 267
Cdd:cd13523 151 ALANLGADGNEELYPDFTDAAAALLKELKPNVKKYWSnaSQPANLLLNGEVVLAMAWLGSGFKLKQA------GAPIEFV 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15830188 268 IPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDH 311
Cdd:cd13523 225 VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAAVAAT 268
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
31-363 1.26e-72

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: 228.78  E-value: 1.26e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWK 110
Cdd:cd13664   1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 111 NLDPELLKLVAkhDPDNKFAMPYMWATTGIGYNVDKVKavlgenAPVDSWDLILKPENLEKLKscgVSFLDAPEEVFATV 190
Cdd:cd13664  81 NIDPRWRKPDF--DPGNEYSIPWQWGTTGFAVDTAVYD------GDIDDYSVIFQPPEELKGK---IAMVDSMNEVVNAA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 191 LNYLGKDPNSTKADDYTgPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGdvwqASNRAKEAKNgvNVSFSIPK 270
Cdd:cd13664 150 IYYLGGPICTTDPKLMR-KVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNG----ASLRARRQNP--SLAYAYPK 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 271 EGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNPGIYPPADVRAKLFTLKV 350
Cdd:cd13664 223 EGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTL 302
                       330
                ....*....|...
gi 15830188 351 QAPKIDRVRTRAW 363
Cdd:cd13664 303 CPPKAEKLQSRIW 315
PBP2_PotD cd13660
The periplasmic substrate-binding component of an active spermidine-preferential transport ...
31-340 6.70e-71

The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative 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: 270378 [Multi-domain]  Cd Length: 315  Bit Score: 224.38  E-value: 6.70e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKL-MAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEW 109
Cdd:cd13660   1 TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVkLYKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKITNF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 110 KNLDPELLKlvAKHDPDNKFAMPYMWATTGIGYNVDKVKAVlgenaPVDSWDLILKPENLEKLkscgvSFLDAPEEVFAT 189
Cdd:cd13660  81 SNIDPDFLN--QPFDPNNDYSIPYIWGATALAVNGDAVDGK-----SVTSWADLWKPEYKGKL-----LLTDDAREVFQM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 190 VLNYLGKDPNSTKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKeakngvNVSFSIP 269
Cdd:cd13660 149 ALRKLGYSGNTKDPEEIEA-AFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANK------PIHVVWP 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830188 270 KEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNPGIYPPAD 340
Cdd:cd13660 222 KEGGIFWMDSFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAE 292
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
6-344 1.54e-70

spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 224.41  E-value: 1.54e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    6 KKWLSGLVAGALMAVSVGTLAA-EQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTG-FDLVV 83
Cdd:PRK09501   2 KKWSRHLLAAGALALGMSAAHAdDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGaYDLVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   84 PSASFLERQLTAGVFQPLDKSKLPEWKNLDPELLKlvAKHDPDNKFAMPYMWATTGIGYNVDKVkavlgENAPVDSWDLI 163
Cdd:PRK09501  82 PSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLN--KPFDPNNDYSIPYIWGATAIGVNSDAI-----DPKSVTSWADL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  164 LKPENLEKLkscgvSFLDAPEEVFATVLNYLGKDPNSTKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIG 243
Cdd:PRK09501 155 WKPEYKGSL-----LLTDDAREVFQMALRKLGYSGNTTDPKEIEA-AYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMI 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  244 WAGDVWQAsnraKEAKNGVNVSFsiPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATP 323
Cdd:PRK09501 229 WNGSAFVA----RQAGTPIDVVW--PKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARK 302
                        330       340
                 ....*....|....*....|.
gi 15830188  324 LVSAEVRDNPGIYPPADVRAK 344
Cdd:PRK09501 303 LLSPEVANDKSLYPDAETIKK 323
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
31-367 2.93e-68

The 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 group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative 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, 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: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 217.54  E-value: 2.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWK 110
Cdd:cd13663   1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 111 ---NLDPELLKLvaKHDPDNKFAMPYMWATTGIGYNVDKVKavlgeNAPVDSWDLILKPENLEKlkscgVSFLDAPEEVF 187
Cdd:cd13663  81 kniNIQPDLLNL--AFDPINEYSVPYFWGTLGIVYNKTKVS-----LEELSWWNILWNKKYKGK-----ILMYDSPRDAF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 188 ATVLNYLGKDPNSTKaDDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKeakngvNVSFS 267
Cdd:cd13663 149 MVALKALGYSLNTTN-PDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEENE------NLDYV 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 268 IPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAE--VRDNPGIYPPADVRAKL 345
Cdd:cd13663 222 IPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEEesIKDDKIFYPDEDIYKKC 301
                       330       340
                ....*....|....*....|..
gi 15830188 346 FTLKVQAPKIDRVRTRAWTKVK 367
Cdd:cd13663 302 EVFKYLGGDAKKEYNDLWLEVK 323
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
31-347 1.27e-60

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: 197.74  E-value: 1.27e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWK 110
Cdd:cd13662   1 VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 111 NLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKavlgeNAPVDsWDLILKpenlEKLKScGVSFLDAPEEVFATV 190
Cdd:cd13662  81 EEKDNLMEASKIYDPGLEYSVPYMFGATGIAVNKKIVK-----NYFRK-WSIFLR----EDLAG-RMTMLDDMREVIGAA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 191 LNYLGKdPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAkngvNVSFSIPK 270
Cdd:cd13662 150 LAYLGY-PVDSKDIEQLEEAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEE----KFDFFIPE 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830188 271 EGA-MAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEvrdnPGIYPPADV-RAKLFT 347
Cdd:cd13662 225 GAAsMMYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKEAEKKSQKK----PIIYAEEDLkNSKLPG 299
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
31-321 9.33e-59

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: 191.74  E-value: 9.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWK 110
Cdd:cd13588   1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 111 NLDPELLKLvAKHDPDNK-FAMPYMWATTGIGYNVDKVKAvlgenAPVDSWDLILKPENLEKlkscgVSFLDAPEEVFAT 189
Cdd:cd13588  81 NIDPRLRNL-PWLTVDGKvYGVPYDWGANGLAYNTKKVKT-----PPTSWLALLWDPKYKGR-----VAARDDPIDAIAD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 190 VLNYLG-KDPNSTKADDYTGpATDLLLKLRPNIR-YFHSS-QYINDLANGDICVAIGWAGDVwqasNRAKeaKNGVNVSF 266
Cdd:cd13588 150 AALYLGqDPPFNLTDEQLDA-VKAKLREQRPLVRkYWSDGaELVQLFANGEVVAATAWSGQV----NALQ--KAGKPVAY 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15830188 267 SIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAA 321
Cdd:cd13588 223 VIPKEGATGWVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEA 277
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
49-315 4.69e-38

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: 137.36  E-value: 4.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  49 FEKETGIKVVYDVFDSNEVLeGKLMA--GSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPewkNLDPELLKLVAKHDpd 126
Cdd:cd13589  23 FEKETGIKVVYDTGTSADRL-AKLQAqaGNPQWDVVDLDDGDAARAIAEGLLEPLDYSKIP---NAAKDKAPAALKTG-- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 127 nkFAMPYMWATTGIGYNVDKVKAvlgenaPVDSWDLiLKPENLEKLKSCGVSFLDAPEEVFAtVLNYLGKDPNSTKADdy 206
Cdd:cd13589  97 --YGVGYTLYSTGIAYNTDKFKE------PPTSWWL-ADFWDVGKFPGPRILNTSGLALLEA-ALLADGVDPYPLDVD-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 207 tgPATDLLLKLRPNIRYFHSS--QYINDLANGDICVAIGWAGDVWQAsnrakeAKNGVNVSFSIPKEGAMAFFDVFAMPA 284
Cdd:cd13589 165 --RAFAKLKELKPNVVTWWTSgaQLAQLLQSGEVDMAPAWNGRAQAL------IDAGAPVAFVWPKEGAILGPDTLAIVK 236
                       250       260       270
                ....*....|....*....|....*....|.
gi 15830188 285 DAKNKDEAYQFLNYLLRPDVVAHISDHVFYA 315
Cdd:cd13589 237 GAPNKELAMKFINFALSPEVQAALAEALGYG 267
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
31-321 9.13e-36

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: 132.17  E-value: 9.13e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMA-GSTGFDLVVPSASFLERQLTAGVFQPLDKSKLpEW 109
Cdd:cd13587   1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRAtGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 110 KNLDPELL---KLVAKHDpDNKFAMPYMWATTGIGYNVDKVKAVLGEnAPVDSWDlilkPENLEKlkscgVSFldAPEEV 186
Cdd:cd13587  80 AQFPPSLLestKLGTTIN-GKRYAVPFDWGTEGLTVNSTKAPDVSGF-SYGDLWA----PEYAGK-----VAY--RLKSP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 187 FATVLNYL---GKDPnSTKADDYTGPAT---------DLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWAGDVWqas 252
Cdd:cd13587 147 LTGLGLYAdatGEDP-FNRYLDYKDEAKyqkildqvlQFLIERKANVKAYwnNADEALAAFRSGGCVIGQTWDSTGL--- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830188 253 nraKEAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAA 321
Cdd:cd13587 223 ---KLNRENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVGA 288
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
45-304 5.12e-23

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 97.31  E-value: 5.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  45 TVANFEKETGIKVVYDVFDSNEVLEgKLMA--GSTGFDLV-VPSASFLERQLTAGVFQPLdksKLPEWKNLDPELlklva 121
Cdd:COG1840   1 LLEAFEKKTGIKVNVVRGGSGELLA-RLKAegGNPPADVVwSGDADALEQLANEGLLQPY---KSPELDAIPAEF----- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 122 kHDPDNKFAMPYMWATtGIGYNVDKVKAvlgENAPvDSWDLILKPENLEKLKSCGVSFLDAPEEVFATVLNYLGKDPnst 201
Cdd:COG1840  72 -RDPDGYWFGFSVRAR-VIVYNTDLLKE---LGVP-KSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEK--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 202 kaddytgpATDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWAGDVwqasnrAKEAKNGVNVSFSIPKEGAMAFFDV 279
Cdd:COG1840 143 --------GWEWLKGLAANGARVtgSSSAVAKAVASGEVAIGIVNSYYA------LRAKAKGAPVEVVFPEDGTLVNPSG 208
                       250       260
                ....*....|....*....|....*
gi 15830188 280 FAMPADAKNKDEAYQFLNYLLRPDV 304
Cdd:COG1840 209 AAILKGAPNPEAAKLFIDFLLSDEG 233
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
46-335 5.54e-22

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 94.39  E-value: 5.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    46 VANFEKETGIKVVYDVFDSNEvLEGKLM----AGSTG-FDLVVPSASFLERQLTAGVFQPLDKskLPEWKNLDPellkLV 120
Cdd:pfam13416   3 AKAFEKKTGVTVEVEPQASND-LQAKLLaaaaAGNAPdLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPD----AL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   121 AKHDPDNKF-AMPYMW-ATTGIGYNVDKVKAvlgENAPVDSWDLILkpENLEKLKSCgVSFLDAPEEVFATVLNYLGKDP 198
Cdd:pfam13416  76 DAAGYDGKLyGVPYAAsTPTVLYYNKDLLKK---AGEDPKTWDELL--AAAAKLKGK-TGLTDPATGWLLWALLADGVDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   199 N-STKADDYTGPATDLLLKLRPNIRYF-HSSQYINDLANGDICVAIGWAGDVwqasnrAKEAKNGVNVSFSIPKEGAMAF 276
Cdd:pfam13416 150 TdDGKGVEALDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAA------AAAKKAGKKLGAVVPKDGSFLG 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   277 FDVFAMPADAKNKDE-AYQFLNYLLRPDVVAHISDHVFYANANKAATPlvSAEVRDNPGI 335
Cdd:pfam13416 224 GKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAAL--SDEVKADPAL 281
PBP2_PotD_PotF_like_1 cd13661
The periplasmic substrate-binding component of an uncharacterized active transport system ...
129-344 1.05e-20

The 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 group represents the periplasmic binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from plants and plant-symbiotic cyanobacteria. 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: 270379 [Multi-domain]  Cd Length: 319  Bit Score: 91.32  E-value: 1.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 129 FAMPYMWATTGIGYNVDKVKAVLGenAPVDsWDLILKPEnlekLKScGVSFLDAPEEVFATVLNYLGKDPNSTkaddyTG 208
Cdd:cd13661  81 WAVPYRWGTTVIAYRKDKLKKLGW--DPID-WSDLWRPE----LAG-RIAMVDSPREVIGLVLKKLGASYNTA-----EV 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 209 PATD-----LLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAsnrakeAKNGVNVSFSIPKEGAMAFFDVFAMP 283
Cdd:cd13661 148 PGGRealeeRLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPL------ARRYSNLAVVIPRSGTSLWADLWVIP 221
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830188 284 ADAKNKDEA-------YQFLNYLLRPDVVAHISDHVFYANA---NKAATPLVSAEVR------DNPGIYPPADVRAK 344
Cdd:cd13661 222 AGSDFGGRVrgpspllSQWIDFCLQPARATQFAQLSFGGASpliLDGPSLTPPEATRklkldtNLVLGLPPDEILAK 298
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
6-304 2.89e-18

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 85.10  E-value: 2.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   6 KKWLSGLVAGALMAVS-------VGTLAAEQKTLHIYNWSDYIAP---DTVANFEKET-GIKVVYDVFDSNEVLEgKL-- 72
Cdd:COG1653   2 RRLALALAAALALALAacggggsGAAAAAGKVTLTVWHTGGGEAAaleALIKEFEAEHpGIKVEVESVPYDDYRT-KLlt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  73 -MAGSTGFDLVVPSASFLERQLTAGVFQPLD---KSKLPEWKNLDPELLKLVAkhdPDNK-FAMPYMWATTGIGYNVDKV 147
Cdd:COG1653  81 aLAAGNAPDVVQVDSGWLAEFAAAGALVPLDdllDDDGLDKDDFLPGALDAGT---YDGKlYGVPFNTDTLGLYYNKDLF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 148 KAvLGENAPvDSWD-LIlkpENLEKLKS----CGVSFLDAPEEVFATVLNYLGKDP-NSTKADDYTGPAT----DLLLKL 217
Cdd:COG1653 158 EK-AGLDPP-KTWDeLL---AAAKKLKAkdgvYGFALGGKDGAAWLDLLLSAGGDLyDEDGKPAFDSPEAvealEFLKDL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 218 R------PNIRYFHSSQYINDLANGDicVAIGWAGDvWQASNrAKEAKNGVNVSFS-IP------KEGAMAFFDVFAMPA 284
Cdd:COG1653 233 VkdgyvpPGALGTDWDDARAAFASGK--AAMMINGS-WALGA-LKDAAPDFDVGVApLPggpggkKPASVLGGSGLAIPK 308
                       330       340
                ....*....|....*....|
gi 15830188 285 DAKNKDEAYQFLNYLLRPDV 304
Cdd:COG1653 309 GSKNPEAAWKFLKFLTSPEA 328
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
80-323 7.52e-16

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 76.24  E-value: 7.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    80 DLVVP------SASFLERQLTAGVFQPLDKSKLPEW-KNLDPELLKlvakhDPDNKFAMpYMWATTGIGYNVDKVKavlG 152
Cdd:pfam13343   5 DIILSagdlffDKRFLEKFIEEGLFQPLDSANLPNVpKDFDDEGLR-----DPDGYYTP-YGVGPLVIAYNKERLG---G 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   153 ENAPVdSWDLILKPEnlekLKSCGVSFLDAPEEVFATVLNYLGKDPNSTkaddytgPATDLLLKLRPNIRYFHSSQYIND 232
Cdd:pfam13343  76 RPVPR-SWADLLDPE----YKGKVALPGPNVGDLFNALLLALYKDFGED-------GVRKLARNLKANLHPAQMVKAAGR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   233 LANGD--ICVAIGWAGDVWQASNRakeakngvNVSFSIPKEGAMAFFDVFAMPADakNKDEAYQFLNYLLRPDVVAHISD 310
Cdd:pfam13343 144 LESGEpaVYLMPYFFADILPRKKK--------NVEVVWPEDGALVSPIFMLVKKG--KKELADPLIDFLLSPEVQAILAK 213
                         250
                  ....*....|....*
gi 15830188   311 H--VFYANANKAATP 323
Cdd:pfam13343 214 AglVFPVVLNPAVDN 228
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
46-342 1.25e-15

Substrate binding domain of a putative ferric iron 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: 270262 [Multi-domain]  Cd Length: 292  Bit Score: 76.49  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  46 VANFEKETGIKVVYdVFDSNEVLEGKLMA--GSTGFDLVV--PSASFLERQLTaGVFQPLDksklPEWKNLDPELLKlva 121
Cdd:cd13544  17 LEAFKKDTGIKVEF-VRLSTGEALARLEAekGNPQADVWFggTADAHIQAKKE-GLLEPYK----SPNADKIPAKFK--- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 122 khDPDNKFAMPYMWaTTGIGYNVDKVKAvlgENAPV-DSWDLILKPEnlekLK---------SCGVSFLdapeeVFATVL 191
Cdd:cd13544  88 --DPDGYWTGIYLG-PLGFGVNTDELKE---KGLPVpKSWEDLLNPE----YKgeivmpnpaSSGTAYT-----FLASLI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 192 NYLGKDpnstKADDYtgpatdlLLKLRPNIRYFHSSQY--INDLANGDICVAIGWAGDVwqasnrAKEAKNGVNVSFSIP 269
Cdd:cd13544 153 QLMGED----EAWEY-------LKKLNKNVGQYTKSGSapAKLVASGEAAIGISFLHDA------LKLKEQGYPIKIIFP 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830188 270 KEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISdhvfyanANKAATPLVSAEVRDNPGIYPPADVR 342
Cdd:cd13544 216 KEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEAQELLA-------KVGSYAIPTNPDAKPPEIAPDLKKDK 281
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
46-306 1.42e-12

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: 67.44  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188    46 VANFEKE-TGIKVVYDVFDSNEV---LEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPEWKNLDPELlklva 121
Cdd:pfam01547  14 VKEFEKEhPGIKVEVESVGSGSLaqkLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPKL----- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   122 khdpdnkFAMPYMWATTGIGYNVDKVKAVlgENAPVDSWDLILKPenLEKLKSCGVSFLDAP------------EEVFAT 189
Cdd:pfam01547  89 -------YGVPLAAETLGLIYNKDLFKKA--GLDPPKTWDELLEA--AKKLKEKGKSPGGAGggdasgtlgyftLALLAS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   190 VLNYLGKDPNSTKADDYTGPATDLLLKLR-----------PNIRYFHSSQYINDLANGDICVAIGWAGDvWQASNRAKEA 258
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLYakvlllkklknPGVAGADGREALALFEQGKAAMGIVGPWA-ALAANKVKLK 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15830188   259 KNGVNVSFSIPKEGAMAFF----------DVFAMPADAKNKDEAYQFLNYLLRPDVVA 306
Cdd:pfam01547 237 VAFAAPAPDPKGDVGYAPLpagkggkgggYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
5-335 2.19e-09

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 58.42  E-value: 2.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188   5 NKKWLSGLVAGALMAVSV------------GTLAAEQKTLHIYNWSDYIAP--DTVANFEKETGIKVVYDVFDSNEVLEG 70
Cdd:COG2182   2 KRRLLAALALALALALALaacgsgssssgsSSAAGAGGTLTVWVDDDEAEAleEAAAAFEEEPGIKVKVVEVPWDDLREK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  71 KLMAGSTGF--DLVVPSASFLERQLTAGVFQPLDKSkLPEWKNLDPELLKLVaKHDpDNKFAMPYMWATTGIGYNVDKVK 148
Cdd:COG2182  82 LTTAAPAGKgpDVFVGAHDWLGELAEAGLLAPLDDD-LADKDDFLPAALDAV-TYD-GKLYGVPYAVETLALYYNKDLVK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 149 AvlgenAPVDSWDLILkpENLEKLKSCGVSFL--DAPEE-VFATVLN-----YLGKDPNSTKADDYTGPAT----DLLLK 216
Cdd:COG2182 159 A-----EPPKTWDELI--AAAKKLTAAGKYGLayDAGDAyYFYPFLAafggyLFGKDGDDPKDVGLNSPGAvaalEYLKD 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 217 LRPNiRYFHSS----QYINDLANGDICVAIGWAgdvWQASNrAKEAKnGVNVSFS-IPK----EGAMAFFDV--FAMPAD 285
Cdd:COG2182 232 LIKD-GVLPADadydAADALFAEGKAAMIINGP---WAAAD-LKKAL-GIDYGVApLPTlaggKPAKPFVGVkgFGVSAY 305
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15830188 286 AKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAAtpLVSAEVRDNPGI 335
Cdd:COG2182 306 SKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAA--AEDAEVKADPLI 353
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
31-303 4.61e-09

Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. 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: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 56.46  E-value: 4.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNwSDY--IAPDTVANFEKE-TGIKVvyDVFDSNEvleGKLM--------AGSTGFDLV-VPSASFLERQLTAGVF 98
Cdd:cd13547   1 KLVVYT-SMPedLANALVEAFEKKyPGVKV--EVFRAGT---GKLMaklaaeaeAGNPQADVLwVADPPTAEALKKEGLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  99 QPLDksklpewknlDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVkavlGENAPVDSWDLiLKPEnleklkscgvs 178
Cdd:cd13547  75 LPYK----------SPEADAIPAPFYDKDGYYYGTRLSAMGIAYNTDKV----PEEAPKSWADL-TKPK----------- 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 179 fldapeevfatvlnYLGK----DPNstkaddYTGPATDLL--LKLRPNIR--YFH------------SSQYINDLANGDI 238
Cdd:cd13547 129 --------------YKGQivmpDPL------YSGAALDLVaaLADKYGLGweYFEklkengvkveggNGQVLDAVASGER 188
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830188 239 CVAIGwagdvwQASNRAKEAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPD 303
Cdd:cd13547 189 PAGVG------VDYNALRAKEKGSPLEVIYPEEGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPE 247
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
31-304 8.82e-09

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: 55.77  E-value: 8.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIYNWSDYIAPDTVAN-FEKETGIKVVYdVFDSNEVLEGKLMA--GSTGFDLVVPSA-SFLERQLTAGVFQPLDkskl 106
Cdd:cd13518   1 ELVVYTASDRDFAEPVLKaFEEKTGIKVKA-VYDGTGELANRLIAekNNPQADVFWGGEiIALEALKEEGLLEPYT---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 107 PEWKNLDPELLKlvakhDPDNKFaMPYMWATTGIGYNVDKVKavlGENAPVDSWDLiLKPENLEKLKSCGVSFLDAPEEV 186
Cdd:cd13518  76 PKVIEAIPADYR-----DPDGYW-VGFAARARVFIYNTDKLK---EPDLPKSWDDL-LDPKWKGKIVYPTPLRSGTGLTH 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 187 FATVLNYLGKDpnstKADDYtgpatdLLLKLRPNIRYFHSSQYINDL-ANGDICVAIGWAGDVwqasnrAKEAKNGVNVS 265
Cdd:cd13518 146 VAALLQLMGEE----KGGWY------LLKLLANNGKPVAGNSDAYDLvAKGEVAVGLTDTYYA------ARAAAKGEPVE 209
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15830188 266 FSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDV 304
Cdd:cd13518 210 IVYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEG 248
PBP2_Fbp_like_3 cd13549
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
37-300 2.10e-08

Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. 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: 270267 [Multi-domain]  Cd Length: 263  Bit Score: 54.77  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  37 WSDYIApdTVANFEKETGIKVVYDVFDSNEVLeGKLMA--GSTGFDLVVPSASFLERQLTAGVFQPLdksKLPEWKNLdP 114
Cdd:cd13549  11 WADWGT--QLKAFKKRTGIQIPYDNKNSGQAL-AALIAerARPVADVAYYGVAFGIQAVAQGVVQPY---KPAHWDEI-P 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 115 ELLKlvakhDPDNK-FAMpymwATTGIGYNVDkVKAVLGENAPvDSWDLILKPENLEKlkscgVSFLDAPE----EVFAT 189
Cdd:cd13549  84 EGLK-----DPDGKwFAI----HSGTLGFIVN-VDALGGKPVP-KSWADLLKPEYKGM-----VGYLDPRSafvgYVGAV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 190 VLNY-LGKDpnstkaDDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWqasnRAKEaKNGVNVSFSI 268
Cdd:cd13549 148 AVNQaMGGS------LDNFGPGIDYFKKLHKNGPIVPKQTAYARVLSGEIPILIDYDFNAY----RAKY-TDKANVAFVI 216
                       250       260       270
                ....*....|....*....|....*....|..
gi 15830188 269 PKEGAMAFFDVFAMPADAKNKDEAYQFLNYLL 300
Cdd:cd13549 217 PKEGSVVVPYVMSLVKNAPNPNNGKKVLDFIM 248
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
46-355 5.38e-08

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: 53.95  E-value: 5.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  46 VANFEKE-TGIKVVYDVFDSNEVLEgKLM---AGSTGFDLVVPSASFLERQLTAGVFQPLDK--SKLPEWKNLDPELLKL 119
Cdd:cd13585  20 IDAFEKEnPGVKVEVVPVPYDDYWT-KLTtaaAAGTAPDVFYVDGPWVPEFASNGALLDLDDyiEKDGLDDDFPPGLLDA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 120 VAKhdpDNK-FAMPYMWATTGIGYNVDKVKAVLGENAPVDSWDLIL---KPENLEKLKSCGVSFlDAPEEVFATVLNYL- 194
Cdd:cd13585  99 GTY---DGKlYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLeaaKKLTDKKGGQYGFAL-RGGSGGQTQWYPFLw 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 195 ---GK--DPNSTKADdYTGPAT--------DLLL-KLRPNIRYFHSSQYINDLANGDicVAIGWAGdVWQASNrAKEAKN 260
Cdd:cd13585 175 sngGDllDEDDGKAT-LNSPEAvealqfyvDLYKdGVAPSSATTGGDEAVDLFASGK--VAMMIDG-PWALGT-LKDSKV 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 261 GVNV------SFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNPG 334
Cdd:cd13585 250 KFKWgvaplpAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALA 329
                       330       340
                ....*....|....*....|.
gi 15830188 335 IYPPADVRAKLFTLKVQAPKI 355
Cdd:cd13585 330 LAAAADALAAAVPPPVPPPWP 350
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
46-338 1.82e-07

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: 52.38  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  46 VANFEKET-GIKVVYDVF---DSNEVLEgKLMAGSTGFDLV-VPSASFLERQLTAGVFQPLDKsKLPEWKNLDPELLKLV 120
Cdd:cd14749  21 IADFEKENpNIKVKVVVFpydNYKTKLK-TAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTD-YLDPNGVDKRFLPGLA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 121 AKHDPDNK-FAMPYMWATTGIGYNVDKVKAVLGENAPvDSWDLILkpENLEKLKS-----CGVSFLDAPEEVFA----TV 190
Cdd:cd14749  99 DAVTFNGKvYGIPFAARALALFYNKDLFEEAGGVKPP-KTWDELI--EAAKKDKFkakgqTGFGLLLGAQGGHWyfqyLV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 191 LNYLG-------------KDPNSTKADDYtgpATDLLLK--LRPNIRYFHSSQYINDLANGDICVAIGWAGDVwqASNRA 255
Cdd:cd14749 176 RQAGGgplsddgsgkatfNDPAFVQALQK---LQDLVKAgaFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDL--GAIKA 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 256 KEAKNGVNVsFSIP--KEGAM-----AFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAhisdhvFYANANKAAT---PLV 325
Cdd:cd14749 251 GEPGGKIGV-FPFPtvGKGAQtstigGSDWAIAISANGKKKEAAVKFLKYLTSPEVMK------QYLEDVGLLPakeVVA 323
                       330
                ....*....|...
gi 15830188 326 SAEVRDNPGIYPP 338
Cdd:cd14749 324 KDEDPDPVAILGP 336
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
46-333 7.17e-07

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: 50.75  E-value: 7.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  46 VANFEKE-TGIKVVYDVFDSNEVLEGKLMA---GSTGFDLVVPSASFLERQLTAGVFQPLDK--SKLPEWKNLDPELLKL 119
Cdd:cd14748  20 VDEFNKShPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQVDASWVAQLADSGALEPLDDyiDKDGVDDDDFYPAALD 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 120 VAKHDpDNKFAMPYMWATTGIGYNVD--KvKAVLGENAPVDSWD------LILKPENLEKLKSCGVSFLDAPEEVFATVL 191
Cdd:cd14748 100 AGTYD-GKLYGLPFDTSTPVLYYNKDlfE-EAGLDPEKPPKTWDeleeaaKKLKDKGGKTGRYGFALPPGDGGWTFQALL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 192 NYLGK---DPNSTKADdYTGPA--------TDLLLKlRPNIRYFHSSQYINDLANGDICVAIGWagdVWQASNrAKEAKN 260
Cdd:cd14748 178 WQNGGdllDEDGGKVT-FNSPEgvealeflVDLVGK-DGVSPLNDWGDAQDAFISGKVAMTING---TWSLAG-IRDKGA 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 261 GVNV------SFSIPKEGAMAFFDVFAMPAD-AKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRDNP 333
Cdd:cd14748 252 GFEYgvaplpAGKGKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEEFLAENP 331
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
46-306 6.97e-05

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: 44.61  E-value: 6.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  46 VANFEKET-GIKVVYDVF---DSNEVLEGKLmAGSTGFDLVvpsasflerQL---------TAGVFQPLDkSKLPEWKNL 112
Cdd:cd14747  20 ADEFEKENpGIEVKVQVLpwgDAHTKITTAA-ASGDGPDVV---------QLgntwvaefaAMGALEDLT-PYLEDLGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 113 DPELLKLVAKHDPDNK-FAMPYMWATTGIGYNVDKVKAVLGENAPVDsWDLILkpENLEKLKSCGVSFL--------DAP 183
Cdd:cd14747  89 KDLFPGLVDTGTVDGKyYGVPWYADTRALFYRTDLLKKAGGDEAPKT-WDELE--AAAKKIKADGPDVSgfaipgknDVW 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 184 EEVFATVL----NYLGKD--------PNSTKA-DDYTGPATDLL-LKLRPNiryfHSSQYINDLANGDICVAIGWAGDVW 249
Cdd:cd14747 166 HNALPFVWgaggDLATKDkwkatldsPEAVAGlEFYTSLYQKGLsPKSTLE----NSADVEQAFANGKVAMIISGPWEIG 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830188 250 QASNRAKEAKNGVNVsFSIP---KEGAMAFF--DVFAMPADAKNKDEAYQFLNYLLRPDVVA 306
Cdd:cd14747 242 AIREAGPDLAGKWGV-APLPggpGGGSPSFAggSNLAVFKGSKNKDLAWKFIEFLSSPENQA 302
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
37-340 3.73e-04

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: 42.28  E-value: 3.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  37 WSDYIAPDTVAN-----FEKETGIKVVYdVFDSNEVLEGKLMA---GSTGFDLVVPSASFLERQLTAGVFQPLDKSKLPE 108
Cdd:cd13586   5 WTDEDGELEYLKelaeeFEKKYGIKVEV-VYVDSGDTREKFITagpAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 109 WKNLDPELLKLVAkhdpDNK-FAMPYMWATTGIGYNVDKVKAVlgenapvdswdlilkPENLEKLKSCGVSFLDAPEEVF 187
Cdd:cd13586  84 IKNLPVALAAVTY----NGKlYGVPVSVETIALFYNKDLVPEP---------------PKTWEELIALAKKFNDKAGGKY 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 188 ATVLNY-----------------LGKDPNSTKADDYTGPAT----DLLLKLRPNIRYFHSSqyindlANGDICVAIGWAG 246
Cdd:cd13586 145 GFAYDQtnpyfsypflaafggyvFGENGGDPTDIGLNNEGAvkglKFIKDLKKKYKVLPPD------LDYDIADALFKEG 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 247 DV-------WQASNrAKEAknGVNVSFS-IPK----EGAMAFFDV--FAMPADAKNKDEAYQFLNYLLRPDVVAHISDHV 312
Cdd:cd13586 219 KAamiingpWDLAD-YKDA--GINFGVApLPTlpggKQAAPFVGVqgAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKT 295
                       330       340
                ....*....|....*....|....*...
gi 15830188 313 FYANANKAAtpLVSAEVRDNPGIYPPAD 340
Cdd:cd13586 296 GRIPALKDA--LNDAAVKNDPLVKAFAE 321
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
38-304 4.06e-04

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: 41.52  E-value: 4.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  38 SDYIAPDTVANFEKETGIKV-VYDVFDSNEVLE-GKLMAGSTGFDLVVP-SASFLERQLTAGVFQPLDKsklpewKNLDP 114
Cdd:cd13545  13 EWGPGPEVKAEFEKETGCKVeFVKPGDAGELLNrLILEKNNPRADVVLGlDNNLLSRALKEGLFEPYRS------PALDV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 115 ellKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKavlgeNAPVDSWDLiLKPEnLEKL--------KSCGVSFLdapeev 186
Cdd:cd13545  87 ---VPEVPVFDPEDRLIPYDYGYLAFNYDKKKFK-----EPPLSLEDL-TAPE-YKGLivvqdprtSSPGLGFL------ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 187 FATVLNYlgkdpnstKADDYtgpatdlllklrpniryfhsSQYINDLANGDICVAIGWaGDVWQ-------------ASN 253
Cdd:cd13545 151 LWTIAVF--------GEEGY--------------------LEYWKKLKANGVTVTPGW-SEAYGlfttgeapmvvsyATS 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15830188 254 RAKEAKNGVNVSFS--IPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDV 304
Cdd:cd13545 202 PAYHVYYEKDLRYTavIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPEF 254
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
31-304 6.28e-03

Substrate binding domain of a putative iron transporter BitB, 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: 270264 [Multi-domain]  Cd Length: 258  Bit Score: 38.01  E-value: 6.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  31 TLHIY--NWSDYIAPdTVANFEKETGIKVvydvfdsnevlegKLMAGSTGfDLvvpsasfLERqLTAGVFQPL------- 101
Cdd:cd13546   1 TLVVYspNSEEIIEP-IIKEFEEKPGIKV-------------EVVTGGTG-EL-------LAR-IKAEADNPQadvmwgg 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 102 DKSKLPEWKNL-----DPELLKL-VAKHDPDNKFAmPYMWATTGIGYNVDkvkaVLGENAPVDSWDLILKPenleKLKsc 175
Cdd:cd13546  58 GIETLEAYKDLfepyeSPEAAAIpDAYKSPEGLWT-GFSVLPVVLMVNTD----LVKNIGAPKGWKDLLDP----KWK-- 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 176 G-VSFLDaPEE---VFATVLNYLgkdpnstkaDDYtGPATDLLLKLRPN--IRYFHSSQYINDLANGDICVAIGWAgdvw 249
Cdd:cd13546 127 GkIAFAD-PNKsgsAYTILYTIL---------KLY-GGAWEYIEKLLDNlgVILSSSSAVYKAVADGEYAVGLTYE---- 191
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15830188 250 qaSNRAKEAKNGVNVSFSIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDV 304
Cdd:cd13546 192 --DAAYKYVAGGAPVKIVYPKEGTTAVPDGVAIVKGAKNPENAKKFIDFLLSKEV 244
PBP2_Fbp_like_6 cd13552
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
44-306 9.66e-03

Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. 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: 270270 [Multi-domain]  Cd Length: 266  Bit Score: 37.43  E-value: 9.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188  44 DTVAN-FEKETGIKVVYDVFDSNEVLE----------GKLMAGStgfdlvvPSASFLERQlTAGVFQPLDksklPEWKNL 112
Cdd:cd13552  14 EYVEDaFEEKTGVEVEWLNMGSQELLDrvraekenpqADVWWGG-------PSQLFMQLK-EEGLLEPTE----PSWAEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 113 DPELLKlvakhDPDNKFAMPYMWATTgIGYNVDKVKAvlgENAPVDsWDLILKPENLEKLKSCGVSFLDAPEEVFATVLN 192
Cdd:cd13552  82 VAAEFK-----DADGYWYGTIQTPEV-IMYNTELLSE---EEAPKD-WDDLLDPKWKDKIIIRNPLASGTMRTIFAALIQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830188 193 YlgkdpnSTKADDYTGPATDLLLKLRPNI-RYFHS-SQYINDLANGDICVAIGWAGDVWQASNrakeaKNGVNVSFSIPK 270
Cdd:cd13552 152 R------ELKGTGSLDAGYAWLKKLDANTkEYAASpTMLYLKIGRGEAAISLWNLNDVLDQRE-----NNKMPFGFIDPA 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15830188 271 EGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVA 306
Cdd:cd13552 221 SGAPVITDGIALIKGAPHPEAAKAFYEFVGSAEIQA 256
 
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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