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Conserved domains on  [gi|1321174614|gb|PLU19868|]
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ABC transporter ATP-binding protein [Sinorhizobium medicae]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
7-357 5.23e-58

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 194.11  E-value: 5.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   7 RRSVLAGGAALLSMSAMARSAL-----AQEARLRVlWWGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQ 81
Cdd:COG1653     3 RLALALAAALALALAACGGGGSgaaaaAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  82 VAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSV-LKVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEEAG 160
Cdd:COG1653    82 LAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 161 VDLPspsTTWEEMAKIGAEITqagKRKGFYGLSDGSAVEPLLENWLRQRGKALFTAEGKIGYDANDAAEWFTMWQNMREA 240
Cdd:COG1653   162 LDPP---KTWDELLAAAKKLK---AKDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 241 KAcVPPDVQALDqYTVETSPLSLGKSAASFAHSNQFVAYQGVSKD-KLALRSHPLISKDSKGGHYRKPSMfFSVAAQTKD 319
Cdd:COG1653   236 GY-VPPGALGTD-WDDARAAFASGKAAMMINGSWALGALKDAAPDfDVGVAPLPGGPGGKKPASVLGGSG-LAIPKGSKN 312
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1321174614 320 PELGAKYVNFFVKDPKAAEILGVERGVPESSAVREALA 357
Cdd:COG1653   313 PEAAWKFLKFLTSPEAQAKWDALQAVLLGQKTPEEALD 350
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
7-357 5.23e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 194.11  E-value: 5.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   7 RRSVLAGGAALLSMSAMARSAL-----AQEARLRVlWWGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQ 81
Cdd:COG1653     3 RLALALAAALALALAACGGGGSgaaaaAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  82 VAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSV-LKVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEEAG 160
Cdd:COG1653    82 LAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 161 VDLPspsTTWEEMAKIGAEITqagKRKGFYGLSDGSAVEPLLENWLRQRGKALFTAEGKIGYDANDAAEWFTMWQNMREA 240
Cdd:COG1653   162 LDPP---KTWDELLAAAKKLK---AKDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 241 KAcVPPDVQALDqYTVETSPLSLGKSAASFAHSNQFVAYQGVSKD-KLALRSHPLISKDSKGGHYRKPSMfFSVAAQTKD 319
Cdd:COG1653   236 GY-VPPGALGTD-WDDARAAFASGKAAMMINGSWALGALKDAAPDfDVGVAPLPGGPGGKKPASVLGGSG-LAIPKGSKN 312
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1321174614 320 PELGAKYVNFFVKDPKAAEILGVERGVPESSAVREALA 357
Cdd:COG1653   313 PEAAWKFLKFLTSPEAQAKWDALQAVLLGQKTPEEALD 350
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
33-421 1.86e-44

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: 159.11  E-value: 1.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  33 RLRVLWWGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDD 112
Cdd:cd13585     1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 113 YLGSVLKVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEEAGvDLPSPSTTWEEMAKIGAEITQAGKRKGFYGL 192
Cdd:cd13585    81 YIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 193 SDGSAVEPLLENWLRQRGKALFTA-EGKIGYDANDAAEWFTMWQNMREAKAcVPPDVQAldQYTVETSPLSLGKSAASFA 271
Cdd:cd13585   160 RGGSGGQTQWYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKDGV-APSSATT--GGDEAVDLFASGKVAMMID 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 272 HSNQFVAY-QGVSKDKLALRSHPLISKDSKGGHYrkPSMFFSVAAQTKDPELGAKYVNFFVKDPKAAEILGVERGVPESS 350
Cdd:cd13585   237 GPWALGTLkDSKVKFKWGVAPLPAGPGGKRASVL--GGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1321174614 351 AVREALAPTLDELGRAMLDYVSGLGPLAGELPPPPPSGAGEAEFALRNVAEQVgfGQLDAKQGGETLVNEV 421
Cdd:cd13585   315 AAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGA--LGKSPEEALKEAAKEI 383
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
55-338 9.98e-20

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 88.62  E-value: 9.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  55 FQEQNaGVAINGEFLGWSDYWPRLATQVAGRNAPDI--IQMDYRYIVEYARRGALAPLDDYLGSvlkvEDFDQVqIKGGS 132
Cdd:pfam13416   6 FEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL----DDLPDA-LDAAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 133 VDGKLYGISLGANSA-AMMVNAAAFEEAGVDLpspsTTWEEMAKIGAEITQAgkrkgfYGLSDGSAveplleNWLRQRGK 211
Cdd:pfam13416  80 YDGKLYGVPYAASTPtVLYYNKDLLKKAGEDP----KTWDELLAAAAKLKGK------TGLTDPAT------GWLLWALL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 212 ALFTAEGKIGYDANDAAEWFTMWQNMREAKACVPPDVQAldqytveTSPLSLGKSAASFAHSNQFVAYQGVSKD--KLAL 289
Cdd:pfam13416 144 ADGVDLTDDGKGVEALDEALAYLKKLKDNGKVYNTGADA-------VQLFANGEVAMTVNGTWAAAAAKKAGKKlgAVVP 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1321174614 290 RSHPLIskdskGGHyrkpsmFFSVAAQTKDPELGA-KYVNFFVKDPKAAE 338
Cdd:pfam13416 217 KDGSFL-----GGK------GLVVPAGAKDPRLAAlDFIKFLTSPENQAA 255
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-186 1.07e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 44.23  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   1 MTHKISRRSVLAGGAALLSMSAMARsalAQEARLrVLWWGSQARADRTNKVNQLFqEQNAGVAINGEFL-GWSDYWPRLA 79
Cdd:PRK09474    3 IKKGLRTLALSALATLMFSASALAK---IEEGKL-VIWINGDKGYNGLAEVGKKF-EKDTGIKVTVEHPdKLEEKFPQVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  80 tqvAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSVLKVEDF--DQVqikggSVDGKLYGISLGANSAAMMVNAAAfe 157
Cdd:PRK09474   78 ---ATGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFtwDAV-----RYNGKLIGYPIAVEALSLIYNKDL-- 147
                         170       180
                  ....*....|....*....|....*....
gi 1321174614 158 eagvdLPSPSTTWEEMAKIGAEITQAGKR 186
Cdd:PRK09474  148 -----VPTPPKTWEEIPALDKELKAKGKS 171
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
7-357 5.23e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 194.11  E-value: 5.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   7 RRSVLAGGAALLSMSAMARSAL-----AQEARLRVlWWGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQ 81
Cdd:COG1653     3 RLALALAAALALALAACGGGGSgaaaaAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  82 VAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSV-LKVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEEAG 160
Cdd:COG1653    82 LAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 161 VDLPspsTTWEEMAKIGAEITqagKRKGFYGLSDGSAVEPLLENWLRQRGKALFTAEGKIGYDANDAAEWFTMWQNMREA 240
Cdd:COG1653   162 LDPP---KTWDELLAAAKKLK---AKDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 241 KAcVPPDVQALDqYTVETSPLSLGKSAASFAHSNQFVAYQGVSKD-KLALRSHPLISKDSKGGHYRKPSMfFSVAAQTKD 319
Cdd:COG1653   236 GY-VPPGALGTD-WDDARAAFASGKAAMMINGSWALGALKDAAPDfDVGVAPLPGGPGGKKPASVLGGSG-LAIPKGSKN 312
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1321174614 320 PELGAKYVNFFVKDPKAAEILGVERGVPESSAVREALA 357
Cdd:COG1653   313 PEAAWKFLKFLTSPEAQAKWDALQAVLLGQKTPEEALD 350
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
33-421 1.86e-44

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: 159.11  E-value: 1.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  33 RLRVLWWGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDD 112
Cdd:cd13585     1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 113 YLGSVLKVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEEAGvDLPSPSTTWEEMAKIGAEITQAGKRKGFYGL 192
Cdd:cd13585    81 YIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 193 SDGSAVEPLLENWLRQRGKALFTA-EGKIGYDANDAAEWFTMWQNMREAKAcVPPDVQAldQYTVETSPLSLGKSAASFA 271
Cdd:cd13585   160 RGGSGGQTQWYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKDGV-APSSATT--GGDEAVDLFASGKVAMMID 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 272 HSNQFVAY-QGVSKDKLALRSHPLISKDSKGGHYrkPSMFFSVAAQTKDPELGAKYVNFFVKDPKAAEILGVERGVPESS 350
Cdd:cd13585   237 GPWALGTLkDSKVKFKWGVAPLPAGPGGKRASVL--GGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1321174614 351 AVREALAPTLDELGRAMLDYVSGLGPLAGELPPPPPSGAGEAEFALRNVAEQVgfGQLDAKQGGETLVNEV 421
Cdd:cd13585   315 AAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGA--LGKSPEEALKEAAKEI 383
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
55-421 7.65e-34

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: 130.10  E-value: 7.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  55 FQEQNAGVAINGEFLGWSDYW-PRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDDYL-GSVLKVEDFDQVQIKGGS 132
Cdd:cd14748    23 FNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIdKDGVDDDDFYPAALDAGT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 133 VDGKLYGISLGANSAAMMVNAAAFEEAGVDLPSPSTTWEEMAKIGAEITQAGKRKGFYGLS-DGSAVEPLLENWLRQRGK 211
Cdd:cd14748   103 YDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTGRYGFAlPPGDGGWTFQALLWQNGG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 212 ALFTAE-GKIGYDANDAAEWFTMWQNMREAKAcvppdVQALDQYTVETSPLSLGKSAASFAHSNQFVAYQGVSKDkLALR 290
Cdd:cd14748   183 DLLDEDgGKVTFNSPEGVEALEFLVDLVGKDG-----VSPLNDWGDAQDAFISGKVAMTINGTWSLAGIRDKGAG-FEYG 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 291 SHPLISKDSK------GGHyrkpsMFFSVAAQTKDPELGAKYVNFFVkDPKAAEILGVERGVPessAVREALAPTLDELG 364
Cdd:cd14748   257 VAPLPAGKGKkgatpaGGA-----SLVIPKGSSKKKEAAWEFIKFLT-SPENQAKWAKATGYL---PVRKSAAEDPEEFL 327
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 365 RAMLDY---VSGLgpLAGELPPPPPSGAGEAEFALRNVAEQVGFGQLDAKQGGETLVNEV 421
Cdd:cd14748   328 AENPNYkvaVDQL--DYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
55-371 1.57e-27

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: 112.86  E-value: 1.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  55 FQEQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQMD-YRYIVEYARRGALAPLDDYLGSVLKVEDFDQVQIKGGSV 133
Cdd:cd14749    24 FEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWpGGWLAEFVKAGLLLPLTDYLDPNGVDKRFLPGLADAVTF 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 134 DGKLYGISLGANSAAMMVNAAAFEEAGVDlpSPSTTWEEMAKIGAEITQAGKRKGFYGLSDGSA-VEPLLENWLRQRG-- 210
Cdd:cd14749   104 NGKVYGIPFAARALALFYNKDLFEEAGGV--KPPKTWDELIEAAKKDKFKAKGQTGFGLLLGAQgGHWYFQYLVRQAGgg 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 211 --KALFTAEGKIGYDANDAAewFTMWQNMREAKAcVPPDVQALDqYTVETSPLSLGKSAASFAHSNQFVAY-QGVSKDKL 287
Cdd:cd14749   182 plSDDGSGKATFNDPAFVQA--LQKLQDLVKAGA-FQEGFEGID-YDDAGQAFAQGKAAMNIGGSWDLGAIkAGEPGGKI 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 288 ALRSHPLISKDSKGGHYRKPSMFFSVAAQTKDPELGAKYVNFFVKDPKAAEILGVERGVPESSAVREALAPTLDELGRAM 367
Cdd:cd14749   258 GVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPF 337

                  ....
gi 1321174614 368 LDYV 371
Cdd:cd14749   338 ADVL 341
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
7-371 4.89e-26

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 108.88  E-value: 4.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   7 RRSVLAGGAALLSMSAMA-----------RSALAQEARLRVlwWGSQARADRTNKVNQLFQEQNaGVAINGEFLGWSDYW 75
Cdd:COG2182     3 RRLLAALALALALALALAacgsgssssgsSSAAGAGGTLTV--WVDDDEAEALEEAAAAFEEEP-GIKVKVVEVPWDDLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  76 PRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSvlkVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAA 155
Cdd:COG2182    80 EKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLAD---KDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 156 FEEagvdlpSPSTTWEEMAKIGAEITQAGKRKGFYGLSDGSAVEPllenWLRQRGKALFTAEG----KIGYDANDAAEWF 231
Cdd:COG2182   157 VKA------EPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYP----FLAAFGGYLFGKDGddpkDVGLNSPGAVAAL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 232 TMWQNMREAKAcVPPDVqaldQYTVETSPLSLGKSAASFAHSNQFVAYQGVSKDKLALRSHPLISkdskGGHYRKP---S 308
Cdd:COG2182   227 EYLKDLIKDGV-LPADA----DYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLA----GGKPAKPfvgV 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1321174614 309 MFFSVAAQTKDPELGAKYVNFFVkDPKAAEILGVERG-VPESSAVREALAPTLDELGRAMLDYV 371
Cdd:COG2182   298 KGFGVSAYSKNKEAAQEFAEYLT-SPEAQKALFEATGrIPANKAAAEDAEVKADPLIAAFAEQA 360
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
40-331 2.41e-23

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: 100.85  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  40 GSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSVLK 119
Cdd:cd14747     8 GNSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLEDLGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 120 VEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEEAGVDlpSPSTTWEEMAKIGAEITQAG-KRKGFYGLSDGSAV 198
Cdd:cd14747    88 DKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGD--EAPKTWDELEAAAKKIKADGpDVSGFAIPGKNDVW 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 199 EPLLEnWLRQRGKALFT-AEGKIGYDANDAAEWFTMWQNMREAKACvpPDVQALDQYTVEtSPLSLGKSAASFAHS---N 274
Cdd:cd14747   166 HNALP-FVWGAGGDLATkDKWKATLDSPEAVAGLEFYTSLYQKGLS--PKSTLENSADVE-QAFANGKVAMIISGPweiG 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1321174614 275 QFVAYQGVSKDKLAlrSHPLISKDSKGGhyrkPSMF----FSVAAQTKDPELGAKYVNFFV 331
Cdd:cd14747   242 AIREAGPDLAGKWG--VAPLPGGPGGGS----PSFAggsnLAVFKGSKNKDLAWKFIEFLS 296
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
55-338 9.98e-20

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 88.62  E-value: 9.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  55 FQEQNaGVAINGEFLGWSDYWPRLATQVAGRNAPDI--IQMDYRYIVEYARRGALAPLDDYLGSvlkvEDFDQVqIKGGS 132
Cdd:pfam13416   6 FEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNL----DDLPDA-LDAAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 133 VDGKLYGISLGANSA-AMMVNAAAFEEAGVDLpspsTTWEEMAKIGAEITQAgkrkgfYGLSDGSAveplleNWLRQRGK 211
Cdd:pfam13416  80 YDGKLYGVPYAASTPtVLYYNKDLLKKAGEDP----KTWDELLAAAAKLKGK------TGLTDPAT------GWLLWALL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 212 ALFTAEGKIGYDANDAAEWFTMWQNMREAKACVPPDVQAldqytveTSPLSLGKSAASFAHSNQFVAYQGVSKD--KLAL 289
Cdd:pfam13416 144 ADGVDLTDDGKGVEALDEALAYLKKLKDNGKVYNTGADA-------VQLFANGEVAMTVNGTWAAAAAKKAGKKlgAVVP 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1321174614 290 RSHPLIskdskGGHyrkpsmFFSVAAQTKDPELGA-KYVNFFVKDPKAAE 338
Cdd:pfam13416 217 KDGSFL-----GGK------GLVVPAGAKDPRLAAlDFIKFLTSPENQAA 255
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
39-333 1.68e-17

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: 82.46  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  39 WGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQV-AGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSV 117
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIaAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 118 LKVedfdqvqikggsVDGKLYGISLGANSAAMMVNAAAFEEAGVDLPspsTTWEEMAKIGAEITQAGKRKGFYGLSDGSA 197
Cdd:pfam01547  81 LVL------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP---KTWDELLEAAKKLKEKGKSPGGAGGGDASG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 198 VEPLLEN-WLRQRGKALFTAEGK--IGYDANDAAEWFTMWQNMREAKACVPPDVQALDQYTVETSPLSLGKSAASFAHSN 274
Cdd:pfam01547 146 TLGYFTLaLLASLGGPLFDKDGGglDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPW 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1321174614 275 Q------------FVAYQGVSKDKLALRSHPLISKDSKGGHYrkpsmfFSVAAQTKDPELGAKYVNFFVKD 333
Cdd:pfam01547 226 AalaankvklkvaFAAPAPDPKGDVGYAPLPAGKGGKGGGYG------LAIPKGSKNKEAAKKFLDFLTSP 290
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
35-190 1.59e-15

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


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 77.81  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  35 RVLWW--GSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDD 112
Cdd:cd14751     1 TITFWhtSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 113 YlgsvlkVEDFDQVQIKGGS-----VDGKLYGISLGANSAAMMVNAAAFEEAGVDLPspsTTWEEMAKIGAEITQAGKRK 187
Cdd:cd14751    81 T------PAFDDIVDYLPGPmetnrYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP---KTMDELVAAAKAIKKKKGRY 151

                  ...
gi 1321174614 188 GFY 190
Cdd:cd14751   152 GLY 154
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
36-369 1.98e-13

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


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 71.29  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  36 VLW-WGSQARADRTNKVNQLFQEQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDDYL 114
Cdd:cd13522     3 TVWhQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 115 GSVLKVEdfdQVQIKGGSVDGKLYGISLGANSAAMMVNAAAFEeagvdlPSPSTTWEEMAKIGaeitQAGKRKGFYGLSD 194
Cdd:cd13522    83 SKSGKYA---PNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVP------KNPPKTWQELIALA----QGLKAKNVWGLVY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 195 GSAVEPLLENWLRQRGKALFTAEG---KIGYDANDAAEWFTMWQNMREAKACVPPDvqalDQYTVETSPLSLGKSAASFA 271
Cdd:cd13522   150 NQNEPYFFAAWIGGFGGQVFKANNgknNPTLDTPGAVEALQFLVDLKSKYKIMPPE----TDYSIADALFKAGKAAMIIN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 272 HSNQFVAYQGVSKDKLALRSHPLISkdskGGHYRKP---SMFFSVAAQTKDPELGAKYVNFFVKDPKAAEILGVERGVPE 348
Cdd:cd13522   226 GPWDLGDYRQALKINLGVAPLPTFS----GTKHAAPfvgGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPA 301
                         330       340
                  ....*....|....*....|.
gi 1321174614 349 SSAVREALAPTLDELGRAMLD 369
Cdd:cd13522   302 NLQAYESPAVQNKPAQKASAE 322
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
77-363 4.63e-12

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: 66.93  E-value: 4.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  77 RLATQVAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSVLKvedFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAaf 156
Cdd:cd13586    43 KFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIK---NLPVALAAVTYNGKLYGVPVSVETIALFYNKD-- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 157 eeagvDLPSPSTTWEEMAKIGAEIT-QAGKRKGF-YGLSDGSAVEPllenWLRQRGKALFTAEGK----IGYDANDAAEW 230
Cdd:cd13586   118 -----LVPEPPKTWEELIALAKKFNdKAGGKYGFaYDQTNPYFSYP----FLAAFGGYVFGENGGdptdIGLNNEGAVKG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 231 FTMWQNMREAKACVPPDvqalDQYTVETSPLSLGKSAASFAHSNQFVAYQgVSKDKLALRSHPLISkdskGGHYRKP--- 307
Cdd:cd13586   189 LKFIKDLKKKYKVLPPD----LDYDIADALFKEGKAAMIINGPWDLADYK-DAGINFGVAPLPTLP----GGKQAAPfvg 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1321174614 308 SMFFSVAAQTKDPELGAKYVNFFVKDPKAAEILGVERGVPESSAVREALAPTLDEL 363
Cdd:cd13586   260 VQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDALNDAAVKNDPL 315
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
55-206 8.07e-12

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


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 66.55  E-value: 8.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  55 FQEQNAGVAINGEFLGWS--DYWPRLATQVAGRN-APDIIQMDYRYIVEYARRGALAPLDDYLGSVlKVEDFDQVQIKGG 131
Cdd:cd14750    23 FEKKHPDIKVEIEELPASsdDQRQQLVTALAAGSsAPDVLGLDVIWIPEFAEAGWLLPLTEYLKEE-EDDDFLPATVEAN 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1321174614 132 SVDGKLYGISLGANSAAMMVNAAAFEEAGVDLPspsTTWEEMAKIGAEITQAGKRKGFYGLSdGSAVEPLLENWL 206
Cdd:cd14750   102 TYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPP---KTWDELLEAAKKRKAGEPGIWGYVFQ-GKQYEGLVCNFL 172
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
49-333 4.40e-09

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


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  49 NKVNQLFQEqNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQ-MDYRYIVEYARRGALAPLDDYL---GSVLKvEDFD 124
Cdd:cd13580    22 NPYTKYLEE-KTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTDYLdkyYPNLK-KIIE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 125 QVQIKGGSVDGKLYGI---SLGANSAAMMVNAAAFEEAGVDLPspsTTWEEMAKIGAEITQA-----GKrKGFYGLSD-- 194
Cdd:cd13580   100 QEGWDSASVDGKIYGIprkRPLIGRNGLWIRKDWLDKLGLEVP---KTLDELYEVAKAFTEKdpdgnGK-KDTYGLTDtk 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 195 ---GSAVEPLLENWLRQRGKALFTAEGKIGYD-----ANDAAEWFtmwQNMREAKAcVPPDVqALDQYTVETSPLSLGKS 266
Cdd:cd13580   176 dliGSGFTGLFGAFGAPPNNWWKDEDGKLVPGsiqpeMKEALKFL---KKLYKEGL-IDPEF-AVNDGTKANEKFISGKA 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1321174614 267 AASFAHSNQFVAYQGVSKDKL---ALRSHPLISKDSKGGHYRKPSM---FFSVAAQTKDPELGAKYVNFFVKD 333
Cdd:cd13580   251 GIFVGNWWDPAWPQASLKKNDpdaEWVAVPIPSGPDGKYGVWAESGvngFFVIPKKSKKPEAILKLLDFLSDP 323
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
5-173 9.86e-09

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 56.46  E-value: 9.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   5 ISRRSVLAGGAALLS-MSAMARSALAQEARLRVLWWGSQARADrtnkVNQLFQEQNaGVAINGEFLGWSDywPRLATQVA 83
Cdd:COG0687     1 MSRRSLLGLAAAALAaALAGGAPAAAAEGTLNVYNWGGYIDPD----VLEPFEKET-GIKVVYDTYDSNE--EMLAKLRA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  84 GRNAPDIIQMDYRYIVEYARRGALAPLD-------DYLGSVLKVEDFDQvqikggsvdGKLYGISLGANSAAMMVNAAAF 156
Cdd:COG0687    74 GGSGYDVVVPSDYFVARLIKAGLLQPLDksklpnlANLDPRFKDPPFDP---------GNVYGVPYTWGTTGIAYNTDKV 144
                         170
                  ....*....|....*..
gi 1321174614 157 EEagvdlpsPSTTWEEM 173
Cdd:COG0687   145 KE-------PPTSWADL 154
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
87-352 8.10e-06

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


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 47.76  E-value: 8.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  87 APDIIQMDYRYIVEYARRGALAPLDDYLgSVLKVEDFDQVQIKGGSVDGKLYGISLGANSAAMMVNAAAfeeagvdLPSP 166
Cdd:cd13657    55 GPDLFIWAHDWIGQFAEAGLLVPISDYL-SEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKAL-------VDQP 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 167 STTWEEMAKIGAEITQAGkrKGFYGLSDGSAVEPLLENWLRQRGKALFTAEG-KIGYDANDAAEWFTMWQNMreAKACVP 245
Cdd:cd13657   127 PETTDELLAIMKDHTDPA--AGSYGLAYQVSDAYFVSAWIFGFGGYYFDDETdKPGLDTPETIKGIQFLKDF--SWPYMP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614 246 PDvqalDQYTVETSPLSLGKsAASFAHSNQFVAYQGVSKDKLALRSHPLISKDskggHYRKP-----SMFFSVAAQTKDP 320
Cdd:cd13657   203 SD----PSYNTQTSLFNEGK-AAMIINGPWFIGGIKAAGIDLGVAPLPTVDGT----NPPRPysgveGIYVTKYAERKNK 273
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1321174614 321 ELGAKYVNFFVkDPKAAEILGVERG-VPESSAV 352
Cdd:cd13657   274 EAALDFAKFFT-TAEASKILADENGyVPAATNA 305
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-186 1.07e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 44.23  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   1 MTHKISRRSVLAGGAALLSMSAMARsalAQEARLrVLWWGSQARADRTNKVNQLFqEQNAGVAINGEFL-GWSDYWPRLA 79
Cdd:PRK09474    3 IKKGLRTLALSALATLMFSASALAK---IEEGKL-VIWINGDKGYNGLAEVGKKF-EKDTGIKVTVEHPdKLEEKFPQVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  80 tqvAGRNAPDIIQMDYRYIVEYARRGALAPLDDYLGSVLKVEDF--DQVqikggSVDGKLYGISLGANSAAMMVNAAAfe 157
Cdd:PRK09474   78 ---ATGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFtwDAV-----RYNGKLIGYPIAVEALSLIYNKDL-- 147
                         170       180
                  ....*....|....*....|....*....
gi 1321174614 158 eagvdLPSPSTTWEEMAKIGAEITQAGKR 186
Cdd:PRK09474  148 -----VPTPPKTWEEIPALDKELKAKGKS 171
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
57-175 2.81e-03

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 40.03  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  57 EQNAGVAINGEFLGWSDYWPRLATQVAGRNAPDIIQ-MDYRYIVEYARRGALAPLDDYL-------GSVLKVEDFDQVQI 128
Cdd:cd13583    27 EEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPvLYPGEENEFVASGALLPISDYLdympnykKYVEKWGLGKELAT 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1321174614 129 KGGSvDGKLY-----GISLGANSAAmMVNAAAFEEAGVDLPspsTTWEEMAK 175
Cdd:cd13583   107 GRQS-DGKYYslpglHEDPGVQYSF-LYRKDIFEKAGIKIP---TTWDEFYA 153
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
4-189 6.71e-03

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 38.63  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614   4 KISRRSVLAGGAALLSMSAMARSALaqearlRVLWWGSQ--ARADRTNKVNQLFQEQNAGVAINGEFLGwsDYWPRLATQ 81
Cdd:PRK10974    2 MKSLRSTALGLALGLALSGNAQAVT------EIPFWHSMegELGKEVDSLAQRFNASQPDYKIVPVYKG--NYEQSLAAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321174614  82 VAGR---NAPDIIQMdyrYIVEYAR---RGALAPLDDylgsVLKV--EDFDQVQ----IKGGSVDGKL-YGISLGANSAA 148
Cdd:PRK10974   74 IAAFrsgNAPAILQV---YEVGTATmmaSKAIKPVYD----VFKDagIPFDESQfvptVAGYYSDAKTgHLLSQPFNSST 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1321174614 149 --MMVNAAAFEEAGVDLPSPSTTWEEMAKIGAEITQAGKRKGF 189
Cdd:PRK10974  147 pvLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAAGMKCGY 189
 
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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