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Conserved domains on  [gi|2238898610|ref|WP_249232392|]
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ABC transporter substrate-binding protein [Brenneria tiliae]

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
PubMed:  26517916|24638992|25750732|26517916
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 ...
 1-362 2.28e-56

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 189.87  E-value: 2.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610   1 MKKAILHTLIASSLALLA------APSFAASQVELRMsWWGGNSRHQQTLKAIESFHQQYPNIKVKAEYTGWDGHLSRLT 74
Cdd:COG1653     1 MRRLALALAAALALALAAcggggsGAAAAAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  75 TQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLN--LVKDSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWK 152
Cdd:COG1653    80 TALAAGNAPDVVQVDSGWLAEFAAAG-ALVPLDdlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 153 KAGLEYPKTWDELLNAGKVFKEKLGDqyYPVVLEHQDSLALLSsyMIQKYNiPAIDEKAQKFSYSDAQWIEFFSLYKKLV 232
Cdd:COG1653   159 KAGLDPPKTWDELLAAAKKLKAKDGV--YGFALGGKDGAAWLD--LLLSAG-GDLYDEDGKPAFDSPEAVEALEFLKDLV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 233 DSHVMPSAKHYASFGKSNmyemKPWISGEWSGTYMWNSTITKYSDNLqPPAKLELGPYPMLPEAKDAGLFFKPAqMLSIG 312
Cdd:COG1653   234 KDGYVPPGALGTDWDDAR----AAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKKPASVLGGS-GLAIP 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2238898610 313 KSTRHPKESALLINFLLNSKEGVQAMGLErgvplsKAAVAQLTADGVIKE 362
Cdd:COG1653   308 KGSKNPEAAWKFLKFLTSPEAQAKWDALQ------AVLLGQKTPEEALDA 351
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-362 2.28e-56

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 189.87  E-value: 2.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610   1 MKKAILHTLIASSLALLA------APSFAASQVELRMsWWGGNSRHQQTLKAIESFHQQYPNIKVKAEYTGWDGHLSRLT 74
Cdd:COG1653     1 MRRLALALAAALALALAAcggggsGAAAAAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  75 TQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLN--LVKDSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWK 152
Cdd:COG1653    80 TALAAGNAPDVVQVDSGWLAEFAAAG-ALVPLDdlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 153 KAGLEYPKTWDELLNAGKVFKEKLGDqyYPVVLEHQDSLALLSsyMIQKYNiPAIDEKAQKFSYSDAQWIEFFSLYKKLV 232
Cdd:COG1653   159 KAGLDPPKTWDELLAAAKKLKAKDGV--YGFALGGKDGAAWLD--LLLSAG-GDLYDEDGKPAFDSPEAVEALEFLKDLV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 233 DSHVMPSAKHYASFGKSNmyemKPWISGEWSGTYMWNSTITKYSDNLqPPAKLELGPYPMLPEAKDAGLFFKPAqMLSIG 312
Cdd:COG1653   234 KDGYVPPGALGTDWDDAR----AAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKKPASVLGGS-GLAIP 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2238898610 313 KSTRHPKESALLINFLLNSKEGVQAMGLErgvplsKAAVAQLTADGVIKE 362
Cdd:COG1653   308 KGSKNPEAAWKFLKFLTSPEAQAKWDALQ------AVLLGQKTPEEALDA 351
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 28-414 1.98e-45

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: 161.42  E-value: 1.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  28 ELRMSWWGGNSRHQQTLKAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLN 107
Cdd:cd13585     1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNG-ALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 108 -LVKDSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWKKAGLEY--PKTWDELLNAGKVFKEKLGDQyYPVV 184
Cdd:cd13585    80 dYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPkpPWTWDELLEAAKKLTDKKGGQ-YGFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 185 LEHQDSLALLSSYMIQKYNIPAIDEKAQKFSYSDAQWIEFFSLYKKLVDSHVMPSAkhyASFGKSNMYEMkpWISGE--- 261
Cdd:cd13585   159 LRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSS---ATTGGDEAVDL--FASGKvam 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 262 -WSGTYMwnstitkYSDNLQPPAKLELG--PYPMLPEAKDAGLFFkpAQMLSIGKSTRHPKESALLINFLLnSKEGVQAM 338
Cdd:cd13585   234 mIDGPWA-------LGTLKDSKVKFKWGvaPLPAGPGGKRASVLG--GWGLAISKNSKHPEAAWKFIKFLT-SKENQLKL 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2238898610 339 GLERGVPLSKAAVAQLTADGVIKEDSPSVAGLNQALNLPHALKTSPYFDDPQIVSLFGDAIQyiDYSQKSVEETAK 414
Cdd:cd13585   304 GGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALL--GALGKSPEEALK 377
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 45-332 1.68e-23

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: 99.80  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQI-AGKTEPDVMQTNWNWLPIFSKNGDgfydlnlvkdSLDLNQFDAKEL 123
Cdd:pfam01547  12 ALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIaAGDGPADVFASDNDWIAELAKAGL----------LLPLDDYVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 124 QgtTVNGKLNGIPISVTARVFYFNNESWKKAGLEYPKTWDELLNAGKVFKEKLGDQYYPVVLEHQDSLALLSSYMIQKYN 203
Cdd:pfam01547  82 V--LGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLASLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 204 IPAIDEKAQKFsySDAQWIEFFSLYKKLVDSHVMPSAKHYASFGKSNMYEMKP---------WISGEWSGTYMWNSTITK 274
Cdd:pfam01547 160 GPLFDKDGGGL--DNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALAlfeqgkaamGIVGPWAALAANKVKLKV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2238898610 275 YSDNLQPPAKLELGpYPMLPEAKDAGlffKPAQMLSIGKSTRHPKESALLINFLLNSK 332
Cdd:pfam01547 238 AFAAPAPDPKGDVG-YAPLPAGKGGK---GGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-362 2.28e-56

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 189.87  E-value: 2.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610   1 MKKAILHTLIASSLALLA------APSFAASQVELRMsWWGGNSRHQQTLKAIESFHQQYPNIKVKAEYTGWDGHLSRLT 74
Cdd:COG1653     1 MRRLALALAAALALALAAcggggsGAAAAAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  75 TQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLN--LVKDSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWK 152
Cdd:COG1653    80 TALAAGNAPDVVQVDSGWLAEFAAAG-ALVPLDdlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 153 KAGLEYPKTWDELLNAGKVFKEKLGDqyYPVVLEHQDSLALLSsyMIQKYNiPAIDEKAQKFSYSDAQWIEFFSLYKKLV 232
Cdd:COG1653   159 KAGLDPPKTWDELLAAAKKLKAKDGV--YGFALGGKDGAAWLD--LLLSAG-GDLYDEDGKPAFDSPEAVEALEFLKDLV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 233 DSHVMPSAKHYASFGKSNmyemKPWISGEWSGTYMWNSTITKYSDNLqPPAKLELGPYPMLPEAKDAGLFFKPAqMLSIG 312
Cdd:COG1653   234 KDGYVPPGALGTDWDDAR----AAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKKPASVLGGS-GLAIP 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2238898610 313 KSTRHPKESALLINFLLNSKEGVQAMGLErgvplsKAAVAQLTADGVIKE 362
Cdd:COG1653   308 KGSKNPEAAWKFLKFLTSPEAQAKWDALQ------AVLLGQKTPEEALDA 351
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 28-414 1.98e-45

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: 161.42  E-value: 1.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  28 ELRMSWWGGNSRHQQTLKAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLN 107
Cdd:cd13585     1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNG-ALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 108 -LVKDSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWKKAGLEY--PKTWDELLNAGKVFKEKLGDQyYPVV 184
Cdd:cd13585    80 dYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPkpPWTWDELLEAAKKLTDKKGGQ-YGFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 185 LEHQDSLALLSSYMIQKYNIPAIDEKAQKFSYSDAQWIEFFSLYKKLVDSHVMPSAkhyASFGKSNMYEMkpWISGE--- 261
Cdd:cd13585   159 LRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSS---ATTGGDEAVDL--FASGKvam 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 262 -WSGTYMwnstitkYSDNLQPPAKLELG--PYPMLPEAKDAGLFFkpAQMLSIGKSTRHPKESALLINFLLnSKEGVQAM 338
Cdd:cd13585   234 mIDGPWA-------LGTLKDSKVKFKWGvaPLPAGPGGKRASVLG--GWGLAISKNSKHPEAAWKFIKFLT-SKENQLKL 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2238898610 339 GLERGVPLSKAAVAQLTADGVIKEDSPSVAGLNQALNLPHALKTSPYFDDPQIVSLFGDAIQyiDYSQKSVEETAK 414
Cdd:cd13585   304 GGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALL--GALGKSPEEALK 377
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 33-414 1.58e-38

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: 143.20  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  33 WWGGNSRHQQTL--KAIESFHQQYPNIKVKAEYTGW-DGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNG-----DGFY 104
Cdd:cd14748     4 FWHGMSGPDGKAleELVDEFNKSHPDIKVKAVYQGSyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGaleplDDYI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 105 DlnlvKDSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWKKAGL---EYPKTWDELLNAG-KVFKEKLGDQY 180
Cdd:cd14748    84 D----KDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAkKLKDKGGKTGR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 181 YPVVLEHQDSLALLSSYMIQ---KYnipaIDEKAQKFSYSDAQWIEFFSLYKKLV-DSHVMPSAkhyasfgkSNMYEMKP 256
Cdd:cd14748   160 YGFALPPGDGGWTFQALLWQnggDL----LDEDGGKVTFNSPEGVEALEFLVDLVgKDGVSPLN--------DWGDAQDA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 257 WISGEWSGTYMWNSTITKYSDNlqpPAKLELG--PYPMLPEAKDAGLFFkpAQMLSIGK-STRHPKESALLINFlLNSKE 333
Cdd:cd14748   228 FISGKVAMTINGTWSLAGIRDK---GAGFEYGvaPLPAGKGKKGATPAG--GASLVIPKgSSKKKEAAWEFIKF-LTSPE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 334 GVQAMGLERG-VPLSKAAVAQLTADgvIKEDSPSVAGLNQALNLPHALKTSPYFddPQIVSLFGDAIQYIDYSQKSVEET 412
Cdd:cd14748   302 NQAKWAKATGyLPVRKSAAEDPEEF--LAENPNYKVAVDQLDYAKPWGPPVPNG--AEIRDELNEALEAALLGKKTPEEA 377


                  ..
gi 2238898610 413 AK 414
Cdd:cd14748   378 LK 379
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 45-414 1.13e-29

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: 118.64  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTN-WNWLPIFSKNGDgFYDLN-LVKDSLDLNQFDAKE 122
Cdd:cd14749    19 ELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWpGGWLAEFVKAGL-LLPLTdYLDPNGVDKRFLPGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 123 LQGTTVNGKLNGIPISVTARVFYFNNESWKKAG-LEYPKTWDELLNAGKVFKEKLGDQY-YPVVLEHQDSLALLSSYMIQ 200
Cdd:cd14749    98 ADAVTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKAKGQTgFGLLLGAQGGHWYFQYLVRQ 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 201 KYNIPAIDEKAQKFSYSDAQWIEFFSLYKKLVDSHVMPSAKHYASF---------GKSNMYEMKPWISGewsgtymwnsT 271
Cdd:cd14749   178 AGGGPLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYddagqafaqGKAAMNIGGSWDLG----------A 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 272 ItkysDNLQPPAKLELGPYPMLPEAKDAGLFFKPAQMLSIGKSTRHPKESALLINFlLNSKEGVQAMGLERGVPLSKAAV 351
Cdd:cd14749   248 I----KAGEPGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKY-LTSPEVMKQYLEDVGLLPAKEVV 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238898610 352 AQLTADGVIKEDSPSVAGLNQALNLPHALKTSPYFDDpqivsLFGDAIQYIDYSQKSVEETAK 414
Cdd:cd14749   323 AKDEDPDPVAILGPFADVLNAAGSTPFLDEYWPAAAQ-----VHKDAVQKLLTGKIDPEQVVK 380
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-425 1.55e-28

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 115.82  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610   1 MKK---AILHTLIASSLALLA---------APSFAASQVELRMswWGGNSRHQQTLKAIESFHQQyPNIKVKAEYTGWDG 68
Cdd:COG2182     1 MKRrllAALALALALALALAAcgsgssssgSSSAAGAGGTLTV--WVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  69 HLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLNLVKDSLDlnQFDAKELQGTTVNGKLNGIPISVTARVFYFNN 148
Cdd:COG2182    78 LREKLTTAAPAGKGPDVFVGAHDWLGELAEAG-LLAPLDDDLADKD--DFLPAALDAVTYDGKLYGVPYAVETLALYYNK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 149 ESWKKaglEYPKTWDELLNAGKVFKEklgDQYYPVVLEHQDS---LALLSSYMIQKYNIPAIDEKaqKFSYSDAQWIEFF 225
Cdd:COG2182   155 DLVKA---EPPKTWDELIAAAKKLTA---AGKYGLAYDAGDAyyfYPFLAAFGGYLFGKDGDDPK--DVGLNSPGAVAAL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 226 SLYKKLVDSHVMPSAKHYAS----F--GKSNMyemkpWISGEWsgtyMWNSTITKYSDNlqppakLELGPYPMLPEAKDA 299
Cdd:COG2182   227 EYLKDLIKDGVLPADADYDAadalFaeGKAAM-----IINGPW----AAADLKKALGID------YGVAPLPTLAGGKPA 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 300 glffKP---AQMLSIGKSTRHPKESALLINFLLnSKEGVQAMGLERG-VPLSKAAV--AQLTADGVIKedsPSVAGLNQA 373
Cdd:COG2182   292 ----KPfvgVKGFGVSAYSKNKEAAQEFAEYLT-SPEAQKALFEATGrIPANKAAAedAEVKADPLIA---AFAEQAEYA 363

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2238898610 374 LNLPhalkTSPYFDdpQIVSLFGDAIQYIDYSQKSVEETAKYFQRQSERILK 425
Cdd:COG2182   364 VPMP----NIPEMG--AVWTPLGTALQAIASGKADPAEALDAAQKQIEAAIA 409
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 33-425 2.49e-27

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: 112.02  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  33 WWGGNSRHQQTLKAIES-FHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLNLVKD 111
Cdd:cd14747     5 WAMGNSAEAELLKELADeFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMG-ALEDLTPYLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 112 SLDLNQFDAKEL-QGTTVNGKLNGIPISVTARVFYFNNESWKKAG-LEYPKTWDELLNAGKVFKEKLGDQYypvvlehqd 189
Cdd:cd14747    84 DLGGDKDLFPGLvDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPKTWDELEAAAKKIKADGPDVS--------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 190 SLALLSSYMIQKYNIPAI--------DEKAQKFSYSDAQWIEFFSLYKKLVDSHVMP------SAKHYASF--GKSNMYe 253
Cdd:cd14747   155 GFAIPGKNDVWHNALPFVwgaggdlaTKDKWKATLDSPEAVAGLEFYTSLYQKGLSPkstlenSADVEQAFanGKVAMI- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 254 mkpwISGEWSgtymwNSTITKYsdnlQPPAKLELGPYPMlPeAKDAGLffKPAQM----LSIGKSTRHPKESALLINFLL 329
Cdd:cd14747   234 ----ISGPWE-----IGAIREA----GPDLAGKWGVAPL-P-GGPGGG--SPSFAggsnLAVFKGSKNKDLAWKFIEFLS 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 330 nSKEGVQAMGLERGV-PLSKAAVaqltADGVIKEDsPSVAGLNQALNLPHALKTSPYFddPQIVSLFGDAIQYI-DYSQK 407
Cdd:cd14747   297 -SPENQAAYAKATGMlPANTSAW----DDPSLAND-PLLAVFAEQLKTGKATPATPEW--GEIEAELVLVLEEVwIGVGA 368

                         410
                  ....*....|....*...
gi 2238898610 408 SVEETAKYFQRQSERILK 425
Cdd:cd14747   369 DVEDALDKAAAEINEILN 386
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 30-414 3.69e-25

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: 105.92  E-value: 3.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  30 RMSWWGGNSRHQQTLKA--IESFHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNG-----DG 102
Cdd:cd14751     1 TITFWHTSSDEEKVLYEklIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGylqplDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 103 FYDLNLVKDSLDlnqfdaKELQGTTVNGKLNGIPISVTARVFYFNNESWKKAGLEYPKTWDELLNAGKVFKEKLGDQYYP 182
Cdd:cd14751    81 TPAFDDIVDYLP------GPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKKKKGRYGLY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 183 VVLEHQDSLA-LLSSY---MiqkynipaIDEKAQKFSYSDAQWIEFFSLYKKLVDSHVmpsAKHYASFGKSNMYemkpwi 258
Cdd:cd14751   155 ISGDGPYWLLpFLWSFggdL--------TDEKKATGYLNSPESVRALETIVDLYDEGA---ITPCASGGYPNMQ------ 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 259 SGEWSGTYM------WNSTITKYSDNLQPPAKLELGPYPmlpeaKDAGLFFKP--AQMLSIGKSTRHPKESALLINFLLN 330
Cdd:cd14751   218 DGFKSGRYAmivngpWAYADILGGKEFKDPDNLGIAPVP-----AGPGGSGSPvgGEDLVIFKGSKNKDAAWKFVKFMSS 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 331 SKEGVQAMGLERGVPLSKAAvaqLTADGVIKEdsPSVAGLNQALNLPHALKTSPYFDDpqIVSLFGDAIQYIDYSQKSVE 410
Cdd:cd14751   293 AEAQALTAAKLGLLPTRTSA---YESPEVANN--PMVAAFKPALETAVPRPPIPEWGE--LFEPLTLAFAKVLRGEKSPR 365


                  ....
gi 2238898610 411 ETAK 414
Cdd:cd14751   366 EALD 369
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 45-332 1.68e-23

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: 99.80  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQI-AGKTEPDVMQTNWNWLPIFSKNGDgfydlnlvkdSLDLNQFDAKEL 123
Cdd:pfam01547  12 ALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIaAGDGPADVFASDNDWIAELAKAGL----------LLPLDDYVANYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 124 QgtTVNGKLNGIPISVTARVFYFNNESWKKAGLEYPKTWDELLNAGKVFKEKLGDQYYPVVLEHQDSLALLSSYMIQKYN 203
Cdd:pfam01547  82 V--LGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLASLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 204 IPAIDEKAQKFsySDAQWIEFFSLYKKLVDSHVMPSAKHYASFGKSNMYEMKP---------WISGEWSGTYMWNSTITK 274
Cdd:pfam01547 160 GPLFDKDGGGL--DNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALAlfeqgkaamGIVGPWAALAANKVKLKV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2238898610 275 YSDNLQPPAKLELGpYPMLPEAKDAGlffKPAQMLSIGKSTRHPKESALLINFLLNSK 332
Cdd:pfam01547 238 AFAAPAPDPKGDVG-YAPLPAGKGGK---GGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 45-419 4.92e-23

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: 100.06  E-value: 4.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYPNIKVKAEYTGW--DGHLSRLTTQ-IAGKTEPDVMQTNWNWLPIFSKNGdgfYDLNLVKD--SLDLNQFD 119
Cdd:cd14750    18 KAIAAFEKKHPDIKVEIEELPAssDDQRQQLVTAlAAGSSAPDVLGLDVIWIPEFAEAG---WLLPLTEYlkEEEDDDFL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 120 AKELQGTTVNGKLNGIPISVTARVFYFNNESWKKAGLEYPKTWDELLNAGKVFKEKL---------GDQYYPVVlehQDS 190
Cdd:cd14750    95 PATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEpgiwgyvfqGKQYEGLV---CNF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 191 LALLSSymiqkYNIPAIDEKAQKFSYSDAQWIEFFSLYKKLVDSHVMPSAKHYASFGKSN--MYEMKPWISGEWsgTYMW 268
Cdd:cd14750   172 LELLWS-----NGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARaaFQAGKAAFMRNW--PYAY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 269 NSTItkySDNLQPPAKLELGPYPMLPEAKDA----GLffkpaqMLSIGKSTRHPKESALLINFLLnSKEGVQAMGLERGV 344
Cdd:cd14750   245 ALLQ---GPESAVAGKVGVAPLPAGPGGGSAstlgGW------NLAISANSKHKEAAWEFVKFLT-SPEVQKRRAINGGL 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2238898610 345 PLSKAAVAQltaDGVIKEDSPSVAGLNQALNLPHALKTSPYFddPQIVSLFGDAIQYIDYSQKSVEETAKYFQRQ 419
Cdd:cd14750   315 PPTRRALYD---DPEVLEAYPFLPALLEALENAVPRPVTPKY--PEVSTAIQIALSAALSGQATPEEALKQAQEK 384
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 45-414 8.76e-19

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: 87.35  E-value: 8.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYpNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLNLVKDSLDLNQFDAkeLQ 124
Cdd:cd13586    17 ELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAG-LLAPIPEYLAVKIKNLPVA--LA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 125 GTTVNGKLNGIPISVTARVFYFNNESWKKAgleyPKTWDELLNAGKVFKEKLGDQY---YPVVlEHQDSLALLSSYMIQ- 200
Cdd:cd13586    93 AVTYNGKLYGVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFNDKAGGKYgfaYDQT-NPYFSYPFLAAFGGYv 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 201 ------KYNIPAIDEKAQKfsysdaQWIEFF-SLYKKLvdsHVMPSAKHY----ASF--GKSNMYemkpwISGEWSgtym 267
Cdd:cd13586   168 fgenggDPTDIGLNNEGAV------KGLKFIkDLKKKY---KVLPPDLDYdiadALFkeGKAAMI-----INGPWD---- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 268 wnstITKYSDnlqppAKLELG--PYPMLPEAKDAGLFFKpAQMLSIGKSTRHPKESALLINFLLnSKEGVQAMGLERG-V 344
Cdd:cd13586   230 ----LADYKD-----AGINFGvaPLPTLPGGKQAAPFVG-VQGAFVSAYSKNKEAAVEFAEYLT-SDEAQLLLFEKTGrI 298

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238898610 345 PLSKAAVaqltADGVIKEDsPSVAGLNQALNLPHALKTSP---YFDDPqivslFGDAIQYIDYSQKSVEETAK 414
Cdd:cd13586   299 PALKDAL----NDAAVKND-PLVKAFAEQAQYGVPMPNIPemaAVWDA-----MGNALNLVASGKATPEEAAK 361
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 34-175 2.17e-12

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: 68.21  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  34 WGGNSRHQQTLKAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGdGFYDLNLVKDSL 113
Cdd:cd13522     7 QYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAG-LLAPLDEYVSKS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2238898610 114 DLNQFDAkeLQGTTVNGKLNGIPISVTARVFYFNNeswKKAGLEYPKTWDELLNAGKVFKEK 175
Cdd:cd13522    86 GKYAPNT--IAAMKLNGKLYGVPVSVGAHLMYYNK---KLVPKNPPKTWQELIALAQGLKAK 142
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-353 2.11e-11

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 64.35  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYpNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWN--WLPIFSKNGdGFYDLNLVKDSLDLNQFdake 122
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWIAadQLATLAEAG-LLADLSDVDNLDDLPDA---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 123 LQGTTVNGKLNGIPISV-TARVFYFNNESWKKAGLEyPKTWDELLNAGKVFKEKlgdqyypvVLEHQDSLALLSSYMIQK 201
Cdd:pfam13416  75 LDAAGYDGKLYGVPYAAsTPTVLYYNKDLLKKAGED-PKTWDELLAAAAKLKGK--------TGLTDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 202 YNIPAIDEKAqkfsysDAQWIEFFSLYKKLVDshvmpSAKHYASFGKSNmyemKPWISGEWSGTYMWNSTITKYSDNLQP 281
Cdd:pfam13416 146 GVDLTDDGKG------VEALDEALAYLKKLKD-----NGKVYNTGADAV----QLFANGEVAMTVNGTWAAAAAKKAGKK 210

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238898610 282 pakLELGPYPMlpeakdaGLFFKPAQMLsIGKSTRHPKESAL-LINFLLnSKEGVQAMGLERGVPLSKAAVAQ 353
Cdd:pfam13416 211 ---LGAVVPKD-------GSFLGGKGLV-VPAGAKDPRLAALdFIKFLT-SPENQAALAEDTGYIPANKSAAL 271
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 52-330 9.49e-11

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: 63.50  E-value: 9.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  52 QQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTN-WNWLPIFSKNGdGFYDLN--LVKDSLDLNQFDAKELQGT-T 127
Cdd:cd13580    29 EEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNdPQLSITLVKQG-ALWDLTdyLDKYYPNLKKIIEQEGWDSaS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 128 VNGKLNGIP--ISVTARVFYFNNESW-KKAGLEYPKTWDELLNAGKVFKEKLGDQYY---------PVVLEHQDSLALLS 195
Cdd:cd13580   108 VDGKIYGIPrkRPLIGRNGLWIRKDWlDKLGLEVPKTLDELYEVAKAFTEKDPDGNGkkdtygltdTKDLIGSGFTGLFG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 196 SYMIqkYNIPAIDEKAQKFSYSDAQ--WIEFFSLYKKLVDSH-------VMPSAKHYASF--GKSNMYemkpwiSGEWSG 264
Cdd:cd13580   188 AFGA--PPNNWWKDEDGKLVPGSIQpeMKEALKFLKKLYKEGlidpefaVNDGTKANEKFisGKAGIF------VGNWWD 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2238898610 265 TYMWNSTITKysdnLQPPAKLELGPYPMLPEAK-DAGLFFKPAQMLSIGKSTRHPKESALLINFLLN 330
Cdd:cd13580   260 PAWPQASLKK----NDPDAEWVAVPIPSGPDGKyGVWAESGVNGFFVIPKKSKKPEAILKLLDFLSD 322
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 45-419 9.96e-10

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: 59.70  E-value: 9.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  45 KAIESFHQQYPNIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMQTNWNWLPIFSKNGDgFYDLNLVKDSLDLNQFDAKELQ 124
Cdd:cd13657    18 QIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGL-LVPISDYLSEDDFENYLPTAVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 125 GTTVNGKLNGIPISVTARVFYFNNESWKKAgleyPKTWDELLNAGKVFKEKLGDQyYPVVLEHQDslALLSSYMIQKYNI 204
Cdd:cd13657    97 AVTYKGKVYGLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHTDPAAGS-YGLAYQVSD--AYFVSAWIFGFGG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 205 PAIDEKAQKFSYSDAQWIEFFSLYKKLVDShVMPSAKHYAS----F--GKSNMyemkpWISGEWSgtymwnstitkYSDN 278
Cdd:cd13657   170 YYFDDETDKPGLDTPETIKGIQFLKDFSWP-YMPSDPSYNTqtslFneGKAAM-----IINGPWF-----------IGGI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 279 LQPPAKLELGPYPMLPEAKDA-------GLFFkpAQMLSIGKstrhpKESALLINFLLNSKEGVQAMGLERG-VPLSKAA 350
Cdd:cd13657   233 KAAGIDLGVAPLPTVDGTNPPrpysgveGIYV--TKYAERKN-----KEAALDFAKFFTTAEASKILADENGyVPAATNA 305

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238898610 351 VAQLTADGvikedSPSVAGLNQALNLPHALKTSPYFDdpQIVSLFGDAIQYIDYSQKSVEETAKYFQRQ 419
Cdd:cd13657   306 YDDAEVAA-----DPVIAAFKAQAEHGVPMPNSPEMA--SVWGPVTLALAAVYQGGQDPQEALAAAQQE 367
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 111-180 2.88e-06

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


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 49.02  E-value: 2.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 111 DSLDLNQFDAKELQGTTVNGKLNGIPISVTARVFYFNNESWKKAgleyPKTWDELLNAGKVFKEKLGDQY 180
Cdd:cd13658    79 SKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLTKEKGKQY 144
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 126-334 2.71e-05

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. 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 includes 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: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 46.28  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 126 TTVNGK---LNGIPISVTARVF--YFNNESW-KKAGLEYPKTWDELLNAGKVFKEK------LGDQyYPVVLEHQDS--- 190
Cdd:cd13584   111 TTDDGNiygFPYLPDGDVAKEArgYFIRKDWlDKLGLKTPSTIDEWYTVLKAFKERdpngngKADE-VPLILTKPGYdet 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 191 LALLSSYMIqkYNIPAIDEKAQKFSYSDAQWIEFFSL----YKK-LVDSHVMPSakhyasfgKSNMYEMKpwISGEWSG- 264
Cdd:cd13584   190 GRLINAWGA--YMDFYQENGKVKYGPLEPGFKDFLKTmnqwYKEgLIDPDFFTR--------KAKAREQN--IMNGNIGg 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238898610 265 -TYMWNSTITKYSDNLQ---PPAKLELGPYPML-----PEAKDAGLFFKPAQMlSIGKSTRHPKESALLINFLLnSKEG 334
Cdd:cd13584   258 fTHDWFASTGTFNLALLknvPDFKLVAVPPPVLnkgqtPYEEDSRQIAKGDGA-AITASNKNPVLAIKWLDYAY-SEEG 334
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 56-175 1.10e-04

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


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 44.37  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  56 NIKVKAEYTGWDGHLSRLTTQIAGKTEPDVMqTNWNWLPIFSKNGD--GFYDLN-LVKDSLDLN----QFDAKELQGTTV 128
Cdd:cd13521    31 NVKLEIVAVTAATSQQKLNLMLASGDLPDIV-GADYLKDKFIAYGMegAFLPLSkYIDQYPNLKaffkQHPDVLRASTAS 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2238898610 129 NGKLNGIP---ISVTARVFYFNNESW-KKAGLEYPKTWDELLNAGKVFKEK 175
Cdd:cd13521   110 DGKIYLIPyepPKDVPNQGYFIRKDWlDKLNLKTPKTLDELYNVLKAFKEK 160
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
2-171 1.22e-04

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 43.75  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610   2 KKAILHTLIASSLALLAAPSFAASQ-VELRMSWWGGNsrHQQTLkaIESFHQQYpNIKVKAE-YTGWDGHLSRLTtqiAG 79
Cdd:COG0687     3 RRSLLGLAAAALAAALAGGAPAAAAeGTLNVYNWGGY--IDPDV--LEPFEKET-GIKVVYDtYDSNEEMLAKLR---AG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610  80 KTEPDVMQTNWNWLPIFSKNGdgfydlnLVKDsLDLNQF------DAKELQGTTVNGKLNGIPISVTARVFYFNNESWKK 153
Cdd:COG0687    75 GSGYDVVVPSDYFVARLIKAG-------LLQP-LDKSKLpnlanlDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKE 146

                         170       180
                  ....*....|....*....|.
gi 2238898610 154 AgleyPKTWDELLN---AGKV 171
Cdd:COG0687   147 P----PTSWADLWDpeyKGKV 163
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 144-336 7.11e-04

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 41.57  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 144 FYFNNESWKKAGLEYPKTWDELLNAGKVFKEKLGDQY-YPVVLEHQDSLALL-SSYM---IQKYNIPAIDEKAQKFSYSD 218
Cdd:cd13583   130 FLYRKDIFEKAGIKIPTTWDEFYAALKKLKEKYPDSYpYSDRWNSNALLLIAaPAFGttaGWGFSNYTYDPDTDKFVYGA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238898610 219 AQ-----WIEFFS-LYK-KLVDSHVM----PSAKHYASFGKSNmyemkpWISGEWSGTymwNSTITKYSDNLQPPAKLEL 287
Cdd:cd13583   210 TTdeykdMLQYFNkLYAeGLLDPESFtqtdDQAKAKFLNGKSF------VITTNPQTV---DELQRNLRAADGGNYEVVS 280

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2238898610 288 GPYPMLPEAK-DAGLFFKPAQMLSiGKSTRHPKESALL--INFLLnSKEGVQ 336
Cdd:cd13583   281 ITPPAGPAGKaINGSRLENGFMIS-SKAKDSKNFEALLqfLDWLY-SDEGQE 330
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 135-167 1.17e-03

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: 40.66  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2238898610 135 IPISVTARVFYFNNESWKKAGLEYPKTWDELLN 167
Cdd:cd13544    94 TGIYLGPLGFGVNTDELKEKGLPVPKSWEDLLN 126
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 148-175 4.79e-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: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 39.23  E-value: 4.79e-03
                          10        20
                  ....*....|....*....|....*....
gi 2238898610 148 NESW-KKAGLEYPKTWDELLNAGKVFKEK 175
Cdd:cd13581   136 NKKWlDKLGLEMPTTTDELYEVLKAFKEQ 164
 
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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