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Conserved domains on  [gi|518557630|ref|WP_019727837|]
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sugar ABC transporter substrate-binding protein [Bifidobacterium breve]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194401)

ABC transporter substrate-binding protein functions as the initial receptor in the active transport of one or more from a variety of substrates including sugars and contains type 2 periplasmic binding fold

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-435 4.08e-62

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: 206.10  E-value: 4.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFWGWDSGNS---MKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNgAPDVVMLEDPTVTQFAVTDGLVDL 116
Cdd:cd13585    1 TLTFWDWGQPAEtaaLKKLIDAFEKENPGVKVEVVPVPYDD-YWTKLTTAAAAGT-APDVFYVDGPWVPEFASNGALLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 117 -SRFGADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDGESIKTWDDYYEAAKKIR--AIGSYITN 193
Cdd:cd13585   79 dDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTdkKGGQYGFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 194 LAGTSNDYQPFTAQIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLVDTKTPNWSDDWNRELNDGTLASLT 273
Cdd:cd13585  159 LRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLN---SPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 274 IGAWMPINLMTGAPDqaGNWRVAQLPQWEDGKEVSAeDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMADTGTFPSL 353
Cdd:cd13585  236 DGPWALGTLKDSKVK--FKWGVAPLPAGPGGKRASV-LGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAAL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 354 KKILKSDSFTDPTTESNKKTNDYFGGQnvnevlsaaaqrpTEKFQYLPYNPYAQTAYGDEVSKAYSGD--ITLEEALQNY 431
Cdd:cd13585  313 AAAAASAAAPDAKPALALAAAADALAA-------------AVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEA 379


                 ....
gi 518557630 432 AKKL 435
Cdd:cd13585  380 AKEI 383
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-435 4.08e-62

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: 206.10  E-value: 4.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFWGWDSGNS---MKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNgAPDVVMLEDPTVTQFAVTDGLVDL 116
Cdd:cd13585    1 TLTFWDWGQPAEtaaLKKLIDAFEKENPGVKVEVVPVPYDD-YWTKLTTAAAAGT-APDVFYVDGPWVPEFASNGALLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 117 -SRFGADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDGESIKTWDDYYEAAKKIR--AIGSYITN 193
Cdd:cd13585   79 dDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTdkKGGQYGFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 194 LAGTSNDYQPFTAQIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLVDTKTPNWSDDWNRELNDGTLASLT 273
Cdd:cd13585  159 LRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLN---SPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 274 IGAWMPINLMTGAPDqaGNWRVAQLPQWEDGKEVSAeDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMADTGTFPSL 353
Cdd:cd13585  236 DGPWALGTLKDSKVK--FKWGVAPLPAGPGGKRASV-LGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAAL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 354 KKILKSDSFTDPTTESNKKTNDYFGGQnvnevlsaaaqrpTEKFQYLPYNPYAQTAYGDEVSKAYSGD--ITLEEALQNY 431
Cdd:cd13585  313 AAAAASAAAPDAKPALALAAAADALAA-------------AVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEA 379


                 ....
gi 518557630 432 AKKL 435
Cdd:cd13585  380 AKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 17-344 2.05e-61

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 203.74  E-value: 2.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  17 LVGLAACGSSNDNSvnKGDADKAELVFWGWDSGNS--MKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNgAP 94
Cdd:COG1653   13 ALALAACGGGGSGA--AAAAGKVTLTVWHTGGGEAaaLEALIKEFEAEHPGIKVEVESVPYDD-YRTKLLTALAAGN-AP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  95 DVVMLEDPTVTQFAVTDGLVDLSRFGADK--LADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDGEsiK 172
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDDDglDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--K 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 173 TWDDYYEAAKKIRAIGSyITNLAGTSNDYQPFTAQIWQAGAQPWKVDGEnITINmtkDEGMQRYVQFVQKLIDEDLVDTK 252
Cdd:COG1653  167 TWDELLAAAKKLKAKDG-VYGFALGGKDGAAWLDLLLSAGGDLYDEDGK-PAFD---SPEAVEALEFLKDLVKDGYVPPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 253 TPNWS-DDWNRELNDGTLASLTIGAWMPINLMTGAPDQagNWRVAQLPQWEDGKEVSAEDGGSALAVTSQSKNQAAAYKL 331
Cdd:COG1653  242 ALGTDwDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKF 319

                        330
                 ....*....|...
gi 518557630 332 VEYMTHGEGAQTM 344
Cdd:COG1653  320 LKFLTSPEAQAKW 332
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 48-336 1.43e-25

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: 105.96  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630   48 SGNSMKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNGAPDVVMLEDPTVTQFAVTDGLVDLSRFGADKLADD 127
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGS-LAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  128 faagpwnklqyNNKPYALPIDSGPEMFFYNKAVFDKAGVDGesIKTWDDYYEAAKKIRAIGSYITNLAGTS---NDYQPF 204
Cdd:pfam01547  85 -----------VPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDasgTLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  205 TAQIWQAGAQPWKVDGENITinmtkDEGMQRYVQFVQKLIDEDLVDTKTPN---WSDDWNRELND---GTLASLTIGAWM 278
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLD-----NPEAVDAITYYVDLYAKVLLLKKLKNpgvAGADGREALALfeqGKAAMGIVGPWA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518557630  279 PINLMTG---------APDQAGNWRVAQLPQWEDGKevsaeDGGSALAVTSQSKNQAAAYKLVEYMT 336
Cdd:pfam01547 227 ALAANKVklkvafaapAPDPKGDVGYAPLPAGKGGK-----GGGYGLAIPKGSKNKEAAKKFLDFLT 288
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
144-188 8.27e-03

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 38.24  E-value: 8.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518557630 144 ALPIDSGPEMFFYNKAVFDKAGVDGESI-KTWDDYYEAAKKIRAIG 188
Cdd:PRK10974 139 SQPFNSSTPVLYYNKDAFKKAGLDPEQPpKTWQDLAAYAAKLRAAG 184
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-435 4.08e-62

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: 206.10  E-value: 4.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFWGWDSGNS---MKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNgAPDVVMLEDPTVTQFAVTDGLVDL 116
Cdd:cd13585    1 TLTFWDWGQPAEtaaLKKLIDAFEKENPGVKVEVVPVPYDD-YWTKLTTAAAAGT-APDVFYVDGPWVPEFASNGALLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 117 -SRFGADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDGESIKTWDDYYEAAKKIR--AIGSYITN 193
Cdd:cd13585   79 dDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTdkKGGQYGFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 194 LAGTSNDYQPFTAQIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLVDTKTPNWSDDWNRELNDGTLASLT 273
Cdd:cd13585  159 LRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLN---SPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 274 IGAWMPINLMTGAPDqaGNWRVAQLPQWEDGKEVSAeDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMADTGTFPSL 353
Cdd:cd13585  236 DGPWALGTLKDSKVK--FKWGVAPLPAGPGGKRASV-LGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAAL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 354 KKILKSDSFTDPTTESNKKTNDYFGGQnvnevlsaaaqrpTEKFQYLPYNPYAQTAYGDEVSKAYSGD--ITLEEALQNY 431
Cdd:cd13585  313 AAAAASAAAPDAKPALALAAAADALAA-------------AVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEA 379


                 ....
gi 518557630 432 AKKL 435
Cdd:cd13585  380 AKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 17-344 2.05e-61

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 203.74  E-value: 2.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  17 LVGLAACGSSNDNSvnKGDADKAELVFWGWDSGNS--MKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNgAP 94
Cdd:COG1653   13 ALALAACGGGGSGA--AAAAGKVTLTVWHTGGGEAaaLEALIKEFEAEHPGIKVEVESVPYDD-YRTKLLTALAAGN-AP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  95 DVVMLEDPTVTQFAVTDGLVDLSRFGADK--LADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDGEsiK 172
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDDDglDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--K 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 173 TWDDYYEAAKKIRAIGSyITNLAGTSNDYQPFTAQIWQAGAQPWKVDGEnITINmtkDEGMQRYVQFVQKLIDEDLVDTK 252
Cdd:COG1653  167 TWDELLAAAKKLKAKDG-VYGFALGGKDGAAWLDLLLSAGGDLYDEDGK-PAFD---SPEAVEALEFLKDLVKDGYVPPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 253 TPNWS-DDWNRELNDGTLASLTIGAWMPINLMTGAPDQagNWRVAQLPQWEDGKEVSAEDGGSALAVTSQSKNQAAAYKL 331
Cdd:COG1653  242 ALGTDwDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKF 319

                        330
                 ....*....|...
gi 518557630 332 VEYMTHGEGAQTM 344
Cdd:COG1653  320 LKFLTSPEAQAKW 332
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 40-435 2.35e-55

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: 188.27  E-value: 2.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFWGWDSGNS---MKEILADFEKANPGITVKFNNTGTAEKTSTALSNAIAAGNgAPDVVMLEDPTVTQFAVTDGLVDL 116
Cdd:cd14748    1 EITFWHGMSGPDgkaLEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGT-APDVAQVDASWVAQLADSGALEPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 117 SRF--GADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDGES-IKTWDDYYEAAKKIRAIGSYITN 193
Cdd:cd14748   80 DDYidKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKpPKTWDELEEAAKKLKDKGGKTGR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 194 LA---GTSNDYQPFTAQIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLVdtkTPNWSDDWNREL-NDGTL 269
Cdd:cd14748  160 YGfalPPGDGGWTFQALLWQNGGDLLDEDGGKVTFN---SPEGVEALEFLVDLVGKDGV---SPLNDWGDAQDAfISGKV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 270 ASLTIGAWMPINLMTGAPDqaGNWRVAQLPQWEDGKEVSAEdGGSALAVTSQ-SKNQAAAYKLVEYMT-HGEGAQTMADT 347
Cdd:cd14748  234 AMTINGTWSLAGIRDKGAG--FEYGVAPLPAGKGKKGATPA-GGASLVIPKGsSKKKEAAWEFIKFLTsPENQAKWAKAT 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 348 GTFPSLKKILKSDSftdpttesnkktnDYFGGQNVNEVLSAAAQRPTEKFQYLPYNPYAQTAYGDEVSKAYSGDITLEEA 427
Cdd:cd14748  311 GYLPVRKSAAEDPE-------------EFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEA 377


                 ....*...
gi 518557630 428 LQNYAKKL 435
Cdd:cd14748  378 LKEAQEKI 385
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
18-441 5.29e-47

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 167.05  E-value: 5.29e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  18 VGLAACGSSNDNSVNK-GDADKAELVFWGWDS-GNSMKEILADFEKAnPGITVKFNNTGTAEKTsTALSNAIAAGNGaPD 95
Cdd:COG2182   17 LALAACGSGSSSSGSSsAAGAGGTLTVWVDDDeAEALEEAAAAFEEE-PGIKVKVVEVPWDDLR-EKLTTAAPAGKG-PD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  96 VVMLEDPTVTQFAVTDGLVDLSRFGADKlaDDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKagvdgESIKTWD 175
Cdd:COG2182   94 VFVGAHDWLGELAEAGLLAPLDDDLADK--DDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA-----EPPKTWD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 176 DYYEAAKKIRAIGSYITnLAGTSNDYQ--PFtaqIWQAGAQPWKVDGEN---ITINmtkDEGMQRYVQFVQKLIDEDLVD 250
Cdd:COG2182  167 ELIAAAKKLTAAGKYGL-AYDAGDAYYfyPF---LAAFGGYLFGKDGDDpkdVGLN---SPGAVAALEYLKDLIKDGVLP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 251 TKTPNwsDDWNRELNDGTLASLTIGAWMpinlMTGAPDQAG-NWRVAQLPQWEDGKEVSAEDGGSALAVTSQSKNQAAAY 329
Cdd:COG2182  240 ADADY--DAADALFAEGKAAMIINGPWA----AADLKKALGiDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQ 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 330 KLVEYMTHGEGAQTMA-DTGTFPSLKkilksDSFTDPTTESNKKTNDYFggqnvnEVLSAAAQRPTekfqyLPYNPYAQT 408
Cdd:COG2182  314 EFAEYLTSPEAQKALFeATGRIPANK-----AAAEDAEVKADPLIAAFA------EQAEYAVPMPN-----IPEMGAVWT 377

                        410       420       430
                 ....*....|....*....|....*....|...
gi 518557630 409 AYGDEVSKAYSGDITLEEALQNYAKKLAEQGKQ 441
Cdd:COG2182  378 PLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 40-364 3.67e-43

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: 155.93  E-value: 3.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFW---GWDSGNSMKEILADFEKANPGITVKFNNTGTA---EKTSTAlsnaiAAGNGAPDVVMLEDPTVTQFAVTDGL 113
Cdd:cd14747    1 TLTVWamgNSAEAELLKELADEFEKENPGIEVKVQVLPWGdahTKITTA-----AASGDGPDVVQLGNTWVAEFAAMGAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 114 VDLS-RFGADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDgESIKTWDDYYEAAKKIRAIGSYIT 192
Cdd:cd14747   76 EDLTpYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGD-EAPKTWDELEAAAKKIKADGPDVS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 193 NLA--GTSNDYQPFTAQIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLVDTKTPNWSDDWNRELNDGTLA 270
Cdd:cd14747  155 GFAipGKNDVWHNALPFVWGAGGDLATKDKWKATLD---SPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 271 SLTIGAWMPINLMTGAPDQAGNWRVAQLPQwEDGKEVSAEDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMAD-TGT 349
Cdd:cd14747  232 MIISGPWEIGAIREAGPDLAGKWGVAPLPG-GPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKaTGM 310

                        330
                 ....*....|....*
gi 518557630 350 FPSLKKILKSDSFTD 364
Cdd:cd14747  311 LPANTSAWDDPSLAN 325
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 47-435 3.10e-41

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: 150.91  E-value: 3.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  47 DSGNSMKEILADFEKANPGITVKFN-NTGTAEKTSTALSNAIAAGNGAPDVVMLEDPTVTQFAVTDGLVDLSRFGADKLA 125
Cdd:cd14750   11 QEGELLKKAIAAFEKKHPDIKVEIEeLPASSDDQRQQLVTALAAGSSAPDVLGLDVIWIPEFAEAGWLLPLTEYLKEEED 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 126 DDFAAGPWNKLQYNNKPYALP--IDSGpeMFFYNKAVFDKAGVdgESIKTWDDYYEAAKKIRAIGSYITNLAGTSNDYQP 203
Cdd:cd14750   91 DDFLPATVEANTYDGKLYALPwfTDAG--LLYYRKDLLEKYGP--EPPKTWDELLEAAKKRKAGEPGIWGYVFQGKQYEG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 204 FTA----QIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLvdtkTPNWSDDWNRELNDGTLAS---LTIGA 276
Cdd:cd14750  167 LVCnfleLLWSNGGDIFDDDSGKVTVD---SPEALEALQFLRDLIGEGI----SPKGVLTYGEEEARAAFQAgkaAFMRN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 277 WMPINLMTGAPDQA--GNWRVAQLPQWEDGKEVSAEdGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMA-DTGTFPSL 353
Cdd:cd14750  240 WPYAYALLQGPESAvaGKVGVAPLPAGPGGGSASTL-GGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAiNGGLPPTR 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 354 KKIlksdsFTDPTtesNKKTNDYFggQNVNEVLSAAAQRPTekfqyLPYNPYAQTAYGDEVSKAYSGDITLEEALQNYAK 433
Cdd:cd14750  319 RAL-----YDDPE---VLEAYPFL--PALLEALENAVPRPV-----TPKYPEVSTAIQIALSAALSGQATPEEALKQAQE 383


                 ..
gi 518557630 434 KL 435
Cdd:cd14750  384 KL 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 40-437 1.73e-36

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


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 137.90  E-value: 1.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFWGWDSGNSMK----EILADFEKANPGITVKFNNTGTaEKTSTALSNAIAAGNGaPDVVMLEDPTVTQFAVTDGLV- 114
Cdd:cd14749    1 TITYWQYFTGDTKKkymdELIADFEKENPNIKVKVVVFPY-DNYKTKLKTAVAAGEG-PDVFNLWPGGWLAEFVKAGLLl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 115 DLSR-FGADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVDgESIKTWDDYYEAAKKIRAIGSYITN 193
Cdd:cd14749   79 PLTDyLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGV-KPPKTWDELIEAAKKDKFKAKGQTG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 194 --LAGTSNDYQPFTAQI-WQAGAQPWKVDGEN-ITINmtkdegMQRYVQFVQKLIDEDLVDTKTPNWS-----DDWNrEL 264
Cdd:cd14749  158 fgLLLGAQGGHWYFQYLvRQAGGGPLSDDGSGkATFN------DPAFVQALQKLQDLVKAGAFQEGFEgidydDAGQ-AF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 265 NDGTLASLTIGAWMPINLMTGAPdqAGNWRVAQLPQWEDGKEVSAEDGGS-ALAVTSQSKNQAAAYKLVEYMTHGE-GAQ 342
Cdd:cd14749  231 AQGKAAMNIGGSWDLGAIKAGEP--GGKIGVFPFPTVGKGAQTSTIGGSDwAIAISANGKKKEAAVKFLKYLTSPEvMKQ 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 343 TMADTGTFPSLKKILKSDSFTDPTTESnkktndyfggqNVNEVLSAAAQRPTEKFQYLPYNPYAQtaygDEVSKAYSGDI 422
Cdd:cd14749  309 YLEDVGLLPAKEVVAKDEDPDPVAILG-----------PFADVLNAAGSTPFLDEYWPAAAQVHK----DAVQKLLTGKI 373

                        410
                 ....*....|....*
gi 518557630 423 TLEEALQNYAKKLAE 437
Cdd:cd14749  374 DPEQVVKQAQSAAAK 388
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 46-434 1.84e-29

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: 118.25  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  46 WDSGNS-----MKEILADFEKANPGITVKFNNTGTAEKTSTALSNAiaAGNGAPDVVMLEDPTVTQFAVTDGLVDLSRFG 120
Cdd:cd14751    5 WHTSSDeekvlYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAA--AGGQAPDVMRADIAWVPEFAKLGYLQPLDGTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 121 ADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGVdgESIKTWDDYYEAAKKI-RAIGSYITNLAGTSN 199
Cdd:cd14751   83 AFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGT--EVPKTMDELVAAAKAIkKKKGRYGLYISGDGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 200 DY-QPFtaqIWQAGAQPWKVDGENITINmtkDEGMQRYVQFVQKLIDEDLVdtkTPNWSDDWNRELN---DGTLASLTIG 275
Cdd:cd14751  161 YWlLPF---LWSFGGDLTDEKKATGYLN---SPESVRALETIVDLYDEGAI---TPCASGGYPNMQDgfkSGRYAMIVNG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 276 AWMPINLMTGAPDQ-AGNWRVAQLPQWEDGKevSAEDGGSALAVTSQSKNQAAAYKLVEYMTHGEG-AQTMADTGTFPSL 353
Cdd:cd14751  232 PWAYADILGGKEFKdPDNLGIAPVPAGPGGS--GSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAqALTAAKLGLLPTR 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 354 KKILKSDSFTDpttesnkktNDYFggQNVNEVLSAAAQRPTekfqyLP-----YNPYAQTaygdeVSKAYSGDITLEEAL 428
Cdd:cd14751  310 TSAYESPEVAN---------NPMV--AAFKPALETAVPRPP-----IPewgelFEPLTLA-----FAKVLRGEKSPREAL 368


                 ....*.
gi 518557630 429 QNYAKK 434
Cdd:cd14751  369 DEAAKQ 374
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 48-336 1.43e-25

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: 105.96  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630   48 SGNSMKEILADFEKANPGITVKFNNTGTAEkTSTALSNAIAAGNGAPDVVMLEDPTVTQFAVTDGLVDLSRFGADKLADD 127
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGS-LAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  128 faagpwnklqyNNKPYALPIDSGPEMFFYNKAVFDKAGVDGesIKTWDDYYEAAKKIRAIGSYITNLAGTS---NDYQPF 204
Cdd:pfam01547  85 -----------VPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDasgTLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  205 TAQIWQAGAQPWKVDGENITinmtkDEGMQRYVQFVQKLIDEDLVDTKTPN---WSDDWNRELND---GTLASLTIGAWM 278
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLD-----NPEAVDAITYYVDLYAKVLLLKKLKNpgvAGADGREALALfeqGKAAMGIVGPWA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518557630  279 PINLMTG---------APDQAGNWRVAQLPQWEDGKevsaeDGGSALAVTSQSKNQAAAYKLVEYMT 336
Cdd:pfam01547 227 ALAANKVklkvafaapAPDPKGDVGYAPLPAGKGGK-----GGGYGLAIPKGSKNKEAAKKFLDFLT 288
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 54-364 4.86e-21

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 92.47  E-value: 4.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630   54 EILADFEKANpGITVKFNNTGTAEKTSTALSnAIAAGNG-APDVVMLEDPTVTQFAVTDGLVDLSRFGADKLADDFAAGp 132
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLA-AAAAGNApDLDVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDA- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  133 wnkLQYNNKPYALPID-SGPEMFFYNKAVFDKAgvdGESIKTWDDYYEAAKKIRaiGSYItnLAGTSNDYQPFTAQIwqa 211
Cdd:pfam13416  78 ---AGYDGKLYGVPYAaSTPTVLYYNKDLLKKA---GEDPKTWDELLAAAAKLK--GKTG--LTDPATGWLLWALLA--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  212 gaqpwkvDGENITINMTKDEGMQRYVQFVQKLIDedlvDTKTPNWSDDWNRELNDGTLASLTIGAWMpinlMTGAPDQAG 291
Cdd:pfam13416 145 -------DGVDLTDDGKGVEALDEALAYLKKLKD----NGKVYNTGADAVQLFANGEVAMTVNGTWA----AAAAKKAGK 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518557630  292 NWRVAQLPQwedgkevSAEDGGSALAVTSQSKN-QAAAYKLVEYMTHGEG-AQTMADTGTFPSLKKILKSDSFTD 364
Cdd:pfam13416 210 KLGAVVPKD-------GSFLGGKGLVVPAGAKDpRLAALDFIKFLTSPENqAALAEDTGYIPANKSAALSDEVKA 277
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 41-429 1.09e-19

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: 90.16  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  41 LVFWGWDSGNS---MKEILADFEKANPGITVKFNNTGTaEKTSTALSNAIAAGNGaPDVVMLEDPTVTQFAVTDGLVDLS 117
Cdd:cd13522    2 ITVWHQYDTGEnqaVNELIAKFEKAYPGITVEVTYQDT-EARRQFFSTAAAGGKG-PDVVFGPSDSLGPFAAAGLLAPLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 118 RFGADKlaDDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKagvdgESIKTWDDYYEAAKKIRAIGSYITNLAGT 197
Cdd:cd13522   80 EYVSKS--GKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPK-----NPPKTWQELIALAQGLKAKNVWGLVYNQN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 198 sndyQPFTAQIWQAGAQPWKVDGENITINMTKD-EGMQRYVQFVQKLIDEDLVDTKTPNWSDDwNRELNDGTLASLTIGA 276
Cdd:cd13522  153 ----EPYFFAAWIGGFGGQVFKANNGKNNPTLDtPGAVEALQFLVDLKSKYKIMPPETDYSIA-DALFKAGKAAMIINGP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 277 WMpinlmTGAPDQA--GNWRVAQLPQWEDGKEVSAEDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMADT-GTFPSL 353
Cdd:cd13522  228 WD-----LGDYRQAlkINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDaGDIPAN 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 354 KKILKSDSFtdpttesnkktndyfggqnvneVLSAAAQRPTEKFQY------LPYNPYAQTAYGDEVSKAYSGDITLEEA 427
Cdd:cd13522  303 LQAYESPAV----------------------QNKPAQKASAEQAAYgvpmpnIPEMRAVWDAFRIAVNSVLAGKVTPEAA 360


                 ..
gi 518557630 428 LQ 429
Cdd:cd13522  361 AK 362
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 40-431 1.35e-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: 89.66  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFWGWDSGNS--MKEILADFEKANpGITVKFNNtGTAEKTSTALSNAIAAGNGaPDVVMLEDPTVTQFAVTDGLVDLS 117
Cdd:cd13586    1 TITVWTDEDGELeyLKELAEEFEKKY-GIKVEVVY-VDSGDTREKFITAGPAGKG-PDVFFGPHDWLGELAAAGLLAPIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 118 RFGADKlaDDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKavfDKAGvdgESIKTWDDYYEAAKKIraiGSYITNLAGT 197
Cdd:cd13586   78 EYLAVK--IKNLPVALAAVTYNGKLYGVPVSVETIALFYNK---DLVP---EPPKTWEELIALAKKF---NDKAGGKYGF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 198 SNDYQ-PFTAQIWQA--GAQPWKVDGENIT-INMTKDEGMQRYvQFVQKLIDEDLVDTKTPNWsDDWNRELNDGTLASLT 273
Cdd:cd13586  147 AYDQTnPYFSYPFLAafGGYVFGENGGDPTdIGLNNEGAVKGL-KFIKDLKKKYKVLPPDLDY-DIADALFKEGKAAMII 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 274 IGAWMpinlmTGAPDQAG-NWRVAQLPQWEDGKEVSAEDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMAD-TGTFP 351
Cdd:cd13586  225 NGPWD-----LADYKDAGiNFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEkTGRIP 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 352 SLKKILKSDSFTDpttesnkktNDYFGGqnVNEVLSAAAQRPTekfqyLPYNPYAQTAYGDEVSKAYSGDITLEEALQNY 431
Cdd:cd13586  300 ALKDALNDAAVKN---------DPLVKA--FAEQAQYGVPMPN-----IPEMAAVWDAMGNALNLVASGKATPEEAAKDA 363
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 40-361 2.52e-16

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: 80.11  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFW-GWDSG--NSMKEILADFEKANP--GITVKFNNTGTaekTSTALSNAIAAGNGaPDVVMLEDPTVTQFAVTDGLV 114
Cdd:cd13657    1 TITIWhALTGAeeDALQQIIDEFEAKYPvpNVKVPFEKKPD---LQNKLLTAIPAGEG-PDLFIWAHDWIGQFAEAGLLV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 115 DLSRFGADKLADDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAGvdgesiKTWDDYYEAAKKI--RAIGSYit 192
Cdd:cd13657   77 PISDYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPP------ETTDELLAIMKDHtdPAAGSY-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 193 NLAGTSNDYQPFTAqiWQAGAQPWKVDGENITINMTKDE---GMQRYVQFVQKLIDEDLVDTKTPNWsddwnreLNDGTL 269
Cdd:cd13657  149 GLAYQVSDAYFVSA--WIFGFGGYYFDDETDKPGLDTPEtikGIQFLKDFSWPYMPSDPSYNTQTSL-------FNEGKA 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 270 ASLTIGAWmpinLMTGAPDQAGNWRVAQLPQWEDGKEVSAEDGGSALAVTS--QSKNQAAAYKLVEYMTHGEGAQTMADT 347
Cdd:cd13657  220 AMIINGPW----FIGGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVTKyaERKNKEAALDFAKFFTTAEASKILADE 295

                        330
                 ....*....|....*
gi 518557630 348 -GTFPSLKKILKSDS 361
Cdd:cd13657  296 nGYVPAATNAYDDAE 310
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 75-442 1.59e-11

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: 65.94  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  75 TAEKTSTALSNAIAAGNgAPDVVMLED--PTVTQFAVTDGLVDLSRFGAD-----KLADDFAAGPWNKLQYNNKPYALPi 147
Cdd:cd13521   40 TAATSQQKLNLMLASGD-LPDIVGADYlkDKFIAYGMEGAFLPLSKYIDQypnlkAFFKQHPDVLRASTASDGKIYLIP- 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 148 dSGPEM------FFYNKAVFDKAGVdgESIKTWDDYYEAAKKIRA-----------IGSYITNLAGTSNDYQPFTAQIWQ 210
Cdd:cd13521  118 -YEPPKdvpnqgYFIRKDWLDKLNL--KTPKTLDELYNVLKAFKEkdpngngkadeIPFIDRDPLYGAFRLINSWGARSA 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 211 AGAQP--WKVDGENITINMTKDEgMQRYVQFVQKLIDEDLVDTKTPNWSDDWNRE-LNDGTLASLTIGAWMPINLMTG-- 285
Cdd:cd13521  195 GGSTDsdWYEDNGKFKHPFASEE-YKDGMKYMNKLYTEGLIDKESFTQKDDQAEQkFSNGKLGGFTHNWFASDNLFTAql 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 286 APDQAGNWRVAQLPQWEDGKEV----SAEDGGSALAVTSQSKNQAAAYKLVEYM---------------TH----GEGAQ 342
Cdd:cd13521  274 GKEKPMYILLPIAPAGNVKGRReedsPGYTGPDGVAISKKAKNPVAALKFFDWLaseegrelanfgiegVHynkdNGKKR 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 343 T------MADTG-----TFPSLKKILKSDSFTDPTTESNKKTND--------YFGGQNVNEVLSAAAQRPTEKFQYLPYN 403
Cdd:cd13521  354 TkdpvkkSDQPGdnqlyDLPAFIKGGFWNEYTYPRPQWGVLTGDsarlpidmYIKPKYSPPKPEGANLTIEEREQVSIDN 433

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 518557630 404 PYAQTaYGDEVSKAY-SGDITLEEALQNYAKKLAEQGKQQ 442
Cdd:cd13521  434 TELKD-IMMEMTQKWiMGTKEKDEEWDAYQEQLKSAGLYQ 472
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 61-378 4.46e-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: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 64.69  E-value: 4.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  61 KANPGITVKFNNTGTAEKTsTALSNAIAAGNgAPDVVM-LEDPTVTQFAVTDGLVDLSRF-----------GADKLADDF 128
Cdd:cd13583   27 EEKTNVKFKRTPIPSSDYE-TKRSLLIASGD-APDIIPvLYPGEENEFVASGALLPISDYldympnykkyvEKWGLGKEL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 129 AAGpwnkLQYNNKPYALP---IDSGPEM-FFYNKAVFDKAGVDgeSIKTWDDYYEAAKKIRAIG--SY------ITNLAG 196
Cdd:cd13583  105 ATG----RQSDGKYYSLPglhEDPGVQYsFLYRKDIFEKAGIK--IPTTWDEFYAALKKLKEKYpdSYpysdrwNSNALL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 197 TSNDYQPFTAQIWQAGAQPWKVDGENITINMTKDEgMQRYVQFVQKLIDEDLVD----TKTpnwSDDWNRELNDGTLASL 272
Cdd:cd13583  179 LIAAPAFGTTAGWGFSNYTYDPDTDKFVYGATTDE-YKDMLQYFNKLYAEGLLDpesfTQT---DDQAKAKFLNGKSFVI 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 273 TIGAWMPINL--MTGAPDQAGNWRVA-QLPQWEDGKEVSA---EDGGSALAVTSQSKNQAAAYKLVEYMTHGEGaQTMA- 345
Cdd:cd13583  255 TTNPQTVDELqrNLRAADGGNYEVVSiTPPAGPAGKAINGsrlENGFMISSKAKDSKNFEALLQFLDWLYSDEG-QELAt 333

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 518557630 346 ----------DTGTFPSLKKILKSDSFTDPTtesnKKTNDYFG 378
Cdd:cd13583  334 wgvegetytkEGDGKVYLADSNTPALNPSGT----KLLQKDFG 372
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 40-374 6.68e-11

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: 63.66  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  40 ELVFW--GWDSGNSMKEILADFEKANpGITVKFNNTGTAEKTStALSNAIAAGNGaPDVVMLEDPTVTQfAVTDGLvdLS 117
Cdd:cd13658    1 QLTVWvdEDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLE-KLSLDGPAGKG-PDVMVAPHDRIGS-AVLQGL--LS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 118 RFGADKLA-DDFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKAgvdgesIKTWDDYYEAAKKI--RAIGSYiTNL 194
Cdd:cd13658   75 PIKLSKDKkKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA------PKTFDELEALAKDLtkEKGKQY-GFL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 195 AGTSNDYQPFTAqIWQAGAQPWKVDGENITINMT--KDEGMQRYVQFVQKLIDEDLVDTKTPNwsDDWNRELNDGTLASL 272
Cdd:cd13658  148 ADATNFYYSYGL-LAGNGGYIFKKNGSDLDINDIglNSPGAVKAVKFLKKWYTEGYLPKGMTG--DVIQGLFKEGKAAAV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 273 TIGAWMPINLMTgapdqAG-NWRVAQLPQWEDGKEVSAEDGGSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMAD-TGTF 350
Cdd:cd13658  225 IDGPWAIQEYQE-----AGvNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDeTNEI 299

                        330       340
                 ....*....|....*....|....
gi 518557630 351 PSLKKILKsdsftDPTTESNKKTN 374
Cdd:cd13658  300 PPRKDVRS-----DPEIKNNPLTS 318
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 47-364 2.29e-10

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


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 61.98  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  47 DSGNSMKEILADFEKANPGITVKFNNTGTAEktSTALSNAIAAGNGAPDVVMLEDPTVTQFAVTDGLVDLSRFGADKLAD 126
Cdd:cd13655    9 EDQEWLKEMVDAFKEKHPEWKITITIGVVGE--ADAKDEVLKDPSAAADVFAFANDQLGELVDAGAIYPLTGSAVDKIKN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 127 DFAAGPWNKLQYNNKPYALPIDSGPEMFFYNKAVFDKagvdgESIKTWDDYYEAAKKirAIGSYITNLAGTSNDYQPFTA 206
Cdd:cd13655   87 TNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTE-----DDVKSLDTMLAKAPD--AKGKVSFDLSNSWYLYAFFFG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 207 qiwqAGAQPWKVDGENIT-INMTKDEGmqryVQFVQKLIDEdlvdTKTPNWSDDWNRE----LNDGTLASLTIGAWMPIN 281
Cdd:cd13655  160 ----AGCKLFGNNGGDTAgCDFNNEKG----VAVTNYLVDL----VANPKFVNDADGDaisgLKDGTLGAGVSGPWDAAN 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 282 LMTGAPDqagNWRVAQLPQWE-DGKEV--SAEDGGSALAVTSQSKNQAAAYKLVEYMThGEGAQTM--ADTGTFPSLKKI 356
Cdd:cd13655  228 LKKALGD---NYAVAKLPTYTlGGKDVqmKSFAGYKAIGVNSNTKNPEAAMALADYLT-NEESQLTrfEKRGIGPTNKEA 303


                 ....*...
gi 518557630 357 LKSDSFTD 364
Cdd:cd13655  304 AESDAVKA 311
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
17-176 6.83e-10

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 60.31  E-value: 6.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  17 LVGLAACGSSNdnsvnkgdADKAELVFWGWdSGNSMKEILADFEKANpGITVKFNNTGTAEktstALSNAIAAGNGAPDV 96
Cdd:COG0687   15 AAALAGGAPAA--------AAEGTLNVYNW-GGYIDPDVLEPFEKET-GIKVVYDTYDSNE----EMLAKLRAGGSGYDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  97 VMLEDPTVtQFAVTDGLV---DLSRF-GADKLADDFAAGPWNKlqynNKPYALPIDSGPEMFFYNKAVFDKAgvdgesIK 172
Cdd:COG0687   81 VVPSDYFV-ARLIKAGLLqplDKSKLpNLANLDPRFKDPPFDP----GNVYGVPYTWGTTGIAYNTDKVKEP------PT 149


                 ....
gi 518557630 173 TWDD 176
Cdd:COG0687  150 SWAD 153
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 65-344 1.21e-08

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: 56.95  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  65 GITVKFNNTGTAEKTsTALSNAIAAGNgAPDVVMLEDP-TVTQFAVTDGLVDLSRF---GADKLADDFAAGPWNKLQYNN 140
Cdd:cd13580   33 NIDVKVKWVPDSSYD-EKLNLALASGD-LPDIVVVNDPqLSITLVKQGALWDLTDYldkYYPNLKKIIEQEGWDSASVDG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 141 KPYALP--IDSGPEMF-FYNKAVFDKAGVdgESIKTWDDYYEAAKKIR-------AIGSYITNLAGTSNDYQPFTAQIWQ 210
Cdd:cd13580  111 KIYGIPrkRPLIGRNGlWIRKDWLDKLGL--EVPKTLDELYEVAKAFTekdpdgnGKKDTYGLTDTKDLIGSGFTGLFGA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 211 AGAQP--WKVDGENITINMTKDEGMQRYVQFVQKLIDEDLVDtktPNW----SDDWNRELNDGTLASLTIGAWMPIN--- 281
Cdd:cd13580  189 FGAPPnnWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLID---PEFavndGTKANEKFISGKAGIFVGNWWDPAWpqa 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518557630 282 -LMTGAPDqaGNWRVAQLPQWEDGKEVSAEDGGSA--LAVTSQSKNQAAAYKLVEYMTHGEGAQTM 344
Cdd:cd13580  266 sLKKNDPD--AEWVAVPIPSGPDGKYGVWAESGVNgfFVIPKKSKKPEAILKLLDFLSDPEVQKLL 329
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 55-348 2.13e-05

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 46.08  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  55 ILADFEKANpGITVKFNNTGTAEktstaLSNAIAA--GNGAPDVVMLEDPTVTQFAVTDGLV-DLSRFGADKLADDFAag 131
Cdd:COG1840    1 LLEAFEKKT-GIKVNVVRGGSGE-----LLARLKAegGNPPADVVWSGDADALEQLANEGLLqPYKSPELDAIPAEFR-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 132 pwnklqyNNKPYALPIDSGPEMFFYNKAVFDKAGVdgesIKTWDDYYEAAKKIRaIGSYITNLAGTsndyqpftaqiwqa 211
Cdd:COG1840   73 -------DPDGYWFGFSVRARVIVYNTDLLKELGV----PKSWEDLLDPEYKGK-IAMADPSSSGT-------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630 212 gaqpwkvdGENITINMTKDEGMQRYVQFVQKLIDEDLVDTKTpnwSDDWNRELNDGTLAsltIGAWMPINLMTgAPDQAG 291
Cdd:COG1840  127 --------GYLLVAALLQAFGEEKGWEWLKGLAANGARVTGS---SSAVAKAVASGEVA---IGIVNSYYALR-AKAKGA 191

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518557630 292 NWRVaqlpqwedgkeVSAEDG----GSALAVTSQSKNQAAAYKLVEYMTHGEGAQTMADTG 348
Cdd:COG1840  192 PVEV-----------VFPEDGtlvnPSGAAILKGAPNPEAAKLFIDFLLSDEGQELLAEEG 241
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 57-195 2.71e-04

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


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 42.67  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  57 ADFEKANpGITVKFNNTGTaektSTALSNAIAAGNGAPDVVMLEdPTVTQFAVTDGLV---DLSRF-GADKLADDFAAGP 132
Cdd:cd13588   17 TAFEEAT-GCKVVVKFFGS----EDEMVAKLRSGGGDYDVVTPS-GDALLRLIAAGLVqpiDTSKIpNYANIDPRLRNLP 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518557630 133 WNKLqyNNKPYALPIDSGPEMFFYNKAVFDKAGVdgESIKT-WDDYYeaAKKIRAIGSYITNLA 195
Cdd:cd13588   91 WLTV--DGKVYGVPYDWGANGLAYNTKKVKTPPT--SWLALlWDPKY--KGRVAARDDPIDAIA 148
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 50-115 2.81e-04

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 42.55  E-value: 2.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518557630  50 NSMKEILADFEKANPGITVKFNNTGtaektSTALSNAIAagNGAP-DVVMLEDPTVTQFAVTDGLVD 115
Cdd:COG0725   37 EALEELAAAFEKEHPGVKVELSFGG-----SGALARQIE--QGAPaDVFISADEKYMDKLAKKGLIL 96
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 53-165 1.18e-03

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


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 40.75  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518557630  53 KEILADFEKANpGITVKFNNTGTAektSTALSNAIAAGNG-APDVVMLEDPTVTQFAVTDGLVDLSRFGADKLADDFaag 131
Cdd:cd13545   18 PEVKAEFEKET-GCKVEFVKPGDA---GELLNRLILEKNNpRADVVLGLDNNLLSRALKEGLFEPYRSPALDVVPEV--- 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 518557630 132 pwNKLQYNNkpYALPIDSGPEMFFYNKAVFDKAG 165
Cdd:cd13545   91 --PVFDPED--RLIPYDYGYLAFNYDKKKFKEPP 120
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
144-188 8.27e-03

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 38.24  E-value: 8.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518557630 144 ALPIDSGPEMFFYNKAVFDKAGVDGESI-KTWDDYYEAAKKIRAIG 188
Cdd:PRK10974 139 SQPFNSSTPVLYYNKDAFKKAGLDPEQPpKTWQDLAAYAAKLRAAG 184
 
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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