|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
3-454 |
1.66e-46 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 165.60 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 3 RKWKIALLLTLVVAMiSGCFGEKPvlDELGKDGKGKIKVVYYS--EEGFYSDYGNSFNVKYPDIEFEVVSQQEmyqelqg 80
Cdd:COG1653 2 RRLALALAAALALAL-AACGGGGS--GAAAAAGKVTLTVWHTGggEAAALEALIKEFEAEHPGIKVEVESVPY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 81 nedADYREEMR-KFLDKHKPDVLMIDLQTMEKMAQEGKLYNLDAIIAQEKFDLEGFMPGLIDMIRAKgsGSLYGLAPNFY 159
Cdd:COG1653 72 ---DDYRTKLLtALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYD--GKLYGVPFNTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 160 TNVIFYNAGLFREHNIEPPRnkmTWQELIDLSSRFsgigSGENQIYGYYERfGSADQLLNRIAQGSSLRLFDAKGeKLVF 239
Cdd:COG1653 147 TLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKL----KAKDGVYGFALG-GKDGAAWLDLLLSAGGDLYDEDG-KPAF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 240 NTDGWKQAMKLASEAIRNKAIytqpMDESNERVFMGDDDLFFKGKAAMILDGPWVISEFKNrmmwdkEAKEIDWGMVTAP 319
Cdd:COG1653 218 DSPEAVEALEFLKDLVKDGYV----PPGALGTDWDDARAAFASGKAAMMINGSWALGALKD------AAPDFDVGVAPLP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 320 VDPANPEESSYASlNEVFAIAADSPNKRAAWEFVKFVNGTEmakaasrssrgtlptrnqfmkemdgksteafyllrpkae 399
Cdd:COG1653 288 GGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSPE--------------------------------------- 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2537007657 400 yesmwggpnvripsdfyrdfSQIMTTEMKAVVDNKKTVEEAAAAIQAKGEEALQK 454
Cdd:COG1653 328 --------------------AQAKWDALQAVLLGQKTPEEALDAAQAAANAALAR 362
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
57-447 |
3.68e-40 |
|
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: 148.98 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 57 FNVKYPDIEFEVVSQQEMYQELQ--------GNEdadyreemrkfldkhkPDVLMIDLQTMEKMAQEGKLYNLDAIIAQE 128
Cdd:cd14748 23 FNKSHPDIKVKAVYQGSYDDTLTkllaalaaGTA----------------PDVAQVDASWVAQLADSGALEPLDDYIDKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 129 KFDLEGFMPGLIDMirAKGSGSLYGLAPNFYTNVIFYNAGLFREH---NIEPPRnkmTWQELIDLSSRFSGIGSGENQiY 205
Cdd:cd14748 87 GVDDDDFYPAALDA--GTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldPEKPPK---TWDELEEAAKKLKDKGGKTGR-Y 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 206 GYYERFGSADQLLNRIAQGSSLRLFDAKGEKLVFNTDGWKQAMKLASEAIRNKAiYTQPMDESNErvfmgdDDLFFKGKA 285
Cdd:cd14748 161 GFALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDG-VSPLNDWGDA------QDAFISGKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 286 AMILDGPWVISEFKnrmmwdKEAKEIDWGMVTAPVDPANPEESSYASLNevFAIAADSP-NKRAAWEFVKFVNGTEMAKA 364
Cdd:cd14748 234 AMTINGTWSLAGIR------DKGAGFEYGVAPLPAGKGKKGATPAGGAS--LVIPKGSSkKKEAAWEFIKFLTSPENQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 365 ASRSSrGTLPTRNQFMkemdgKSTEAFYLLRP--KAEYESMWGGPNVRIPSDFYRDFSQIMTTEMKAVVDNKKTVEEAAA 442
Cdd:cd14748 306 WAKAT-GYLPVRKSAA-----EDPEEFLAENPnyKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALK 379
|
....*
gi 2537007657 443 AIQAK 447
Cdd:cd14748 380 EAQEK 384
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
57-363 |
2.47e-18 |
|
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: 85.55 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 57 FNVKYPDIEFEVVSQqemyqelqgnEDADYREEMRKFLDKHKP--DVLMIDLQTMEKMAQEGKLYNLDAIIAQEKFDleg 134
Cdd:pfam01547 17 FEKEHPGIKVEVESV----------GSGSLAQKLTTAIAAGDGpaDVFASDNDWIAELAKAGLLLPLDDYVANYLVL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 135 fmpglidmirakGSGSLYGLAPNFYTNVIFYNAGLFREHNIEPPRnkmTWQELIDLSSRFSGIGsGENQIYGYYERFGSA 214
Cdd:pfam01547 84 ------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPK---TWDELLEAAKKLKEKG-KSPGGAGGGDASGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 215 DQLLNRIAQGSSLRLFDAKGEKLVF----NTDGWKQAMKLASEAIRNKAIYTQPMDESNERVfmgddDLFFKGKAAMILD 290
Cdd:pfam01547 148 GYFTLALLASLGGPLFDKDGGGLDNpeavDAITYYVDLYAKVLLLKKLKNPGVAGADGREAL-----ALFEQGKAAMGIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537007657 291 GPWVISEFKN-----RMMWDKEAKEIDWGMVTAPVDPANPEESSYaslnevFAIAADSPNKRAAWEFVKFVNGTEMAK 363
Cdd:pfam01547 223 GPWAALAANKvklkvAFAAPAPDPKGDVGYAPLPAGKGGKGGGYG------LAIPKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
239-354 |
9.19e-03 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 38.45 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 239 FNTDGWKQAMKLASEAIRNKAIyTQPMDESnerVFMGDddlFFKGKAAMILDGPWVISEFknrmmwdkEAKEIDWGMVTA 318
Cdd:PRK09474 209 VNNAGAKAGLQFLVDLVKNKHM-NADTDYS---IAEAA---FNKGETAMTINGPWAWSNI--------DKSGINYGVTVL 273
|
90 100 110
....*....|....*....|....*....|....*.
gi 2537007657 319 PVDPANPEESSYASLNEvfAIAADSPNKRAAWEFVK 354
Cdd:PRK09474 274 PTFNGKPSKPFVGVLSA--GINAASPNKELAKEFLE 307
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
3-454 |
1.66e-46 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 165.60 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 3 RKWKIALLLTLVVAMiSGCFGEKPvlDELGKDGKGKIKVVYYS--EEGFYSDYGNSFNVKYPDIEFEVVSQQEmyqelqg 80
Cdd:COG1653 2 RRLALALAAALALAL-AACGGGGS--GAAAAAGKVTLTVWHTGggEAAALEALIKEFEAEHPGIKVEVESVPY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 81 nedADYREEMR-KFLDKHKPDVLMIDLQTMEKMAQEGKLYNLDAIIAQEKFDLEGFMPGLIDMIRAKgsGSLYGLAPNFY 159
Cdd:COG1653 72 ---DDYRTKLLtALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYD--GKLYGVPFNTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 160 TNVIFYNAGLFREHNIEPPRnkmTWQELIDLSSRFsgigSGENQIYGYYERfGSADQLLNRIAQGSSLRLFDAKGeKLVF 239
Cdd:COG1653 147 TLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKL----KAKDGVYGFALG-GKDGAAWLDLLLSAGGDLYDEDG-KPAF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 240 NTDGWKQAMKLASEAIRNKAIytqpMDESNERVFMGDDDLFFKGKAAMILDGPWVISEFKNrmmwdkEAKEIDWGMVTAP 319
Cdd:COG1653 218 DSPEAVEALEFLKDLVKDGYV----PPGALGTDWDDARAAFASGKAAMMINGSWALGALKD------AAPDFDVGVAPLP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 320 VDPANPEESSYASlNEVFAIAADSPNKRAAWEFVKFVNGTEmakaasrssrgtlptrnqfmkemdgksteafyllrpkae 399
Cdd:COG1653 288 GGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSPE--------------------------------------- 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2537007657 400 yesmwggpnvripsdfyrdfSQIMTTEMKAVVDNKKTVEEAAAAIQAKGEEALQK 454
Cdd:COG1653 328 --------------------AQAKWDALQAVLLGQKTPEEALDAAQAAANAALAR 362
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
57-447 |
3.68e-40 |
|
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: 148.98 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 57 FNVKYPDIEFEVVSQQEMYQELQ--------GNEdadyreemrkfldkhkPDVLMIDLQTMEKMAQEGKLYNLDAIIAQE 128
Cdd:cd14748 23 FNKSHPDIKVKAVYQGSYDDTLTkllaalaaGTA----------------PDVAQVDASWVAQLADSGALEPLDDYIDKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 129 KFDLEGFMPGLIDMirAKGSGSLYGLAPNFYTNVIFYNAGLFREH---NIEPPRnkmTWQELIDLSSRFSGIGSGENQiY 205
Cdd:cd14748 87 GVDDDDFYPAALDA--GTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldPEKPPK---TWDELEEAAKKLKDKGGKTGR-Y 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 206 GYYERFGSADQLLNRIAQGSSLRLFDAKGEKLVFNTDGWKQAMKLASEAIRNKAiYTQPMDESNErvfmgdDDLFFKGKA 285
Cdd:cd14748 161 GFALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDG-VSPLNDWGDA------QDAFISGKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 286 AMILDGPWVISEFKnrmmwdKEAKEIDWGMVTAPVDPANPEESSYASLNevFAIAADSP-NKRAAWEFVKFVNGTEMAKA 364
Cdd:cd14748 234 AMTINGTWSLAGIR------DKGAGFEYGVAPLPAGKGKKGATPAGGAS--LVIPKGSSkKKEAAWEFIKFLTSPENQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 365 ASRSSrGTLPTRNQFMkemdgKSTEAFYLLRP--KAEYESMWGGPNVRIPSDFYRDFSQIMTTEMKAVVDNKKTVEEAAA 442
Cdd:cd14748 306 WAKAT-GYLPVRKSAA-----EDPEEFLAENPnyKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALK 379
|
....*
gi 2537007657 443 AIQAK 447
Cdd:cd14748 380 EAQEK 384
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
57-447 |
6.14e-38 |
|
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: 142.93 E-value: 6.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 57 FNVKYPDIEFEVVSQQE--MYQ----ELQGNEDadyreemrkfldkhkPDVLMIDLQTMEKMAQEGKLYNLDAIIAQEKF 130
Cdd:cd13585 23 FEKENPGVKVEVVPVPYddYWTklttAAAAGTA---------------PDVFYVDGPWVPEFASNGALLDLDDYIEKDGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 131 DlEGFMPGLIDMIRAKGSgsLYGLAPNFYTNVIFYNAGLFRE--HNIEPPrnkMTWQELIDLSSRFsgiGSGENQIYGYY 208
Cdd:cd13585 88 D-DDFPPGLLDAGTYDGK--LYGLPFDADTLVLFYNKDLFDKagPGPKPP---WTWDELLEAAKKL---TDKKGGQYGFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 209 ERFGSADQ-LLNRIAQGSSLRLFDAKGEKLVFNTDGWKQAMKLASEAIRNKAiytqpMDESNERVFMGDDDLFFKGKAAM 287
Cdd:cd13585 159 LRGGSGGQtQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGV-----APSSATTGGDEAVDLFASGKVAM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 288 ILDGPWVISEFKNrmmwdkEAKEIDWGMVTAPVDPANPEESSYASLNevFAIAADSPNKRAAWEFVKFVNGTEMAKAASR 367
Cdd:cd13585 234 MIDGPWALGTLKD------SKVKFKWGVAPLPAGPGGKRASVLGGWG--LAISKNSKHPEAAWKFIKFLTSKENQLKLGG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 368 SSRGTLPTRNQFMKEMDGKSTEAFYLLRPKAEYESMWgGPNVRIPSDFYRDFSQIMTTEMKAVVdnKKTVEEAAAAIQAK 447
Cdd:cd13585 306 AAGPAALAAAAASAAAPDAKPALALAAAADALAAAVP-PPVPPPWPEVYPILSEALQEALLGAL--GKSPEEALKEAAKE 382
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-454 |
2.00e-33 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 130.84 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 1 MLRKWKIALLLTLVVAM-ISGCFG-EKPVLDELGKDGKGKIKVVYYSEEG-FYSDYGNSFNVKyPDIEFEVVSQQemyqe 77
Cdd:COG2182 1 MKRRLLAALALALALALaLAACGSgSSSSGSSSAAGAGGTLTVWVDDDEAeALEEAAAAFEEE-PGIKVKVVEVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 78 lqgneDADYREEMRKFLDKHK-PDVLMIDLQTMEKMAQEGKLYNLDAIIAqekfDLEGFMPGLIDMIRAKGSgsLYGLAP 156
Cdd:COG2182 75 -----WDDLREKLTTAAPAGKgPDVFVGAHDWLGELAEAGLLAPLDDDLA----DKDDFLPAALDAVTYDGK--LYGVPY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 157 NFYTNVIFYNAGLFREhniEPPRnkmTWQELIDLSSRF-----SGIGSGENQIYGYYERFGSADQllnriaqgsslRLFD 231
Cdd:COG2182 144 AVETLALYYNKDLVKA---EPPK---TWDELIAAAKKLtaagkYGLAYDAGDAYYFYPFLAAFGG-----------YLFG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 232 AKGE---KLVFNTDGWKQAMKLASEAIRNKAIYTQpMDESNErvfmgdDDLFFKGKAAMILDGPWVISEFknrmmwdKEA 308
Cdd:COG2182 207 KDGDdpkDVGLNSPGAVAALEYLKDLIKDGVLPAD-ADYDAA------DALFAEGKAAMIINGPWAAADL-------KKA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 309 KEIDWGMVTAPVDPANPEESSYASlNEVFAIAADSPNKRAAWEFVKFVNGTEMAKAASrSSRGTLPTRNQFMKEMDGKST 388
Cdd:COG2182 273 LGIDYGVAPLPTLAGGKPAKPFVG-VKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALF-EATGRIPANKAAAEDAEVKAD 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537007657 389 EAFYLLRPKAEY-ESMwggPNvrIPSdfYRDFSQIMTTEMKAVVDNKKTVEEAAAAIQAKGEEALQK 454
Cdd:COG2182 351 PLIAAFAEQAEYaVPM---PN--IPE--MGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
57-447 |
6.00e-28 |
|
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: 115.08 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 57 FNVKYPDIEFEVVsqqemyqELQGNEDaDYREEMRKFLDKHK--PDVLMIDLQTMEKMAQEGKLYNLDAIIAQEKFDleG 134
Cdd:cd14750 23 FEKKHPDIKVEIE-------ELPASSD-DQRQQLVTALAAGSsaPDVLGLDVIWIPEFAEAGWLLPLTEYLKEEEDD--D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 135 FMPGLIDMirAKGSGSLYGLApnFYTNV--IFYNAGLFREHNIEPPRnkmTWQELIDLSSrfsGIGSGENQIYGY----- 207
Cdd:cd14750 93 FLPATVEA--NTYDGKLYALP--WFTDAglLYYRKDLLEKYGPEPPK---TWDELLEAAK---KRKAGEPGIWGYvfqgk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 208 -YErfGSADQLLNRI-AQGSSLrlFDAKGEKLVFNTDGWKQAMKLASEAIRNKAIyTQPMDESNERVFmgdDDLFFKGKA 285
Cdd:cd14750 163 qYE--GLVCNFLELLwSNGGDI--FDDDSGKVTVDSPEALEALQFLRDLIGEGIS-PKGVLTYGEEEA---RAAFQAGKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 286 AMILDGPWVISEFKNrmmwDKEAKEIDWGMvtAPvDPANPEESSYASL-NEVFAIAADSPNKRAAWEFVKFVNGTEMAKA 364
Cdd:cd14750 235 AFMRNWPYAYALLQG----PESAVAGKVGV--AP-LPAGPGGGSASTLgGWNLAISANSKHKEAAWEFVKFLTSPEVQKR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 365 ASRSSrGTLPTRNQFMKEMDGKSTEAFYllrpKAEYESMWGGpNVRIPSDFYRDFSQIMTTEMKAVVDNKKTVEEAAAAI 444
Cdd:cd14750 308 RAING-GLPPTRRALYDDPEVLEAYPFL----PALLEALENA-VPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQA 381
|
...
gi 2537007657 445 QAK 447
Cdd:cd14750 382 QEK 384
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
40-446 |
1.53e-25 |
|
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: 107.77 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 40 KVVYYSEEGFYSDYGNS----FNVKYpDIEFEVVSQqemyqelqGNEDAdyreeMRKFLDKHK----PDVLMIDLQTMEK 111
Cdd:cd13586 1 TITVWTDEDGELEYLKElaeeFEKKY-GIKVEVVYV--------DSGDT-----REKFITAGPagkgPDVFFGPHDWLGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 112 MAQEGKLYNLDAIIAQEKFDLEGFMPGLidmiraKGSGSLYGLAPNFYTNVIFYNAGLFrehnIEPPRnkmTWQELIDLS 191
Cdd:cd13586 67 LAAAGLLAPIPEYLAVKIKNLPVALAAV------TYNGKLYGVPVSVETIALFYNKDLV----PEPPK---TWEELIALA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 192 SRFSGIGSGE-----NQIYGYYERFgsadqllnrIAQGSSLRLFDAKGE---KLVFNTDGWKQAMKLASEAIRNKAIYTQ 263
Cdd:cd13586 134 KKFNDKAGGKygfayDQTNPYFSYP---------FLAAFGGYVFGENGGdptDIGLNNEGAVKGLKFIKDLKKKYKVLPP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 264 PMDESNErvfmgdDDLFFKGKAAMILDGPWVISEFKNRmmwdkeakEIDWGMVTAPVDPANPEESSYASlNEVFAIAADS 343
Cdd:cd13586 205 DLDYDIA------DALFKEGKAAMIINGPWDLADYKDA--------GINFGVAPLPTLPGGKQAAPFVG-VQGAFVSAYS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 344 PNKRAAWEFVKFVNGTEMAKAASRSSrGTLPTRNQFMKEMDGKSTEAFYLLRPKAEY-ESMwggPNvrIPS-DFYRDFsq 421
Cdd:cd13586 270 KNKEAAVEFAEYLTSDEAQLLLFEKT-GRIPALKDALNDAAVKNDPLVKAFAEQAQYgVPM---PN--IPEmAAVWDA-- 341
|
410 420
....*....|....*....|....*
gi 2537007657 422 iMTTEMKAVVDNKKTVEEAAAAIQA 446
Cdd:cd13586 342 -MGNALNLVASGKATPEEAAKDAVA 365
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
44-446 |
3.08e-22 |
|
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: 98.25 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 44 YSEEGFYSDYGNSFNVKYPDIEFEVVsqqemYQElqgnedadyREEMRKFLD-----KHKPDVLMIDLQTMEKMAQEGKL 118
Cdd:cd13522 10 TGENQAVNELIAKFEKAYPGITVEVT-----YQD---------TEARRQFFStaaagGKGPDVVFGPSDSLGPFAAAGLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 119 YNLDAIIAQEKFDLEGFMPGLidmiraKGSGSLYGLAPNFYTNVIFYNAGLFREhniEPPRnkmTWQELIDLSSR----- 193
Cdd:cd13522 76 APLDEYVSKSGKYAPNTIAAM------KLNGKLYGVPVSVGAHLMYYNKKLVPK---NPPK---TWQELIALAQGlkakn 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 194 FSGIGSGENQIYGYYERFGsadqllnriAQGSSLRLFDAKGEKLVFNTDGWKQAMKLASEAIRNKAIYTQPMDESNErvf 273
Cdd:cd13522 144 VWGLVYNQNEPYFFAAWIG---------GFGGQVFKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIA--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 274 mgdDDLFFKGKAAMILDGPWVISEFknrmmwdKEAKEIDWGMVTAPVDPANPEESSYASlNEVFAIAADSPNKRAAWEFV 353
Cdd:cd13522 212 ---DALFKAGKAAMIINGPWDLGDY-------RQALKINLGVAPLPTFSGTKHAAPFVG-GKGFGINKESQNKAAAVEFV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 354 KFVNGTEMAKAASRSSrGTLPTRNQFMKEMDGKSTEAFYLLRPKAEYesmwGGPNVRIPSdfYRDFSQIMTTEMKAVVDN 433
Cdd:cd13522 281 KYLTSYQAQLVLFDDA-GDIPANLQAYESPAVQNKPAQKASAEQAAY----GVPMPNIPE--MRAVWDAFRIAVNSVLAG 353
|
410
....*....|...
gi 2537007657 434 KKTVEEAAAAIQA 446
Cdd:cd13522 354 KVTPEAAAKDAQQ 366
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
55-447 |
4.31e-22 |
|
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: 97.84 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 55 NSFNVKYPDIEFEVVS-QQEMYQE-----LQGNEdadyreemrkfldkhKPDVLMIDLQT-MEKMAQEGKLYNLDAIIAQ 127
Cdd:cd14749 22 ADFEKENPNIKVKVVVfPYDNYKTklktaVAAGE---------------GPDVFNLWPGGwLAEFVKAGLLLPLTDYLDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 128 EKFDlEGFMPGLIDMirAKGSGSLYGLAPNFYTNVIFYNAGLFREHNI-EPPRnkmTWQELIDLSSRF-------SGIGS 199
Cdd:cd14749 87 NGVD-KRFLPGLADA--VTFNGKVYGIPFAARALALFYNKDLFEEAGGvKPPK---TWDELIEAAKKDkfkakgqTGFGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 200 GENQIYGYYERfgsadQLLNRIAQGSSLrlFDAKGEKLVFNTDGWKQAMKLASEAIRNKAiytqpMDESNERVFMGDD-D 278
Cdd:cd14749 161 LLGAQGGHWYF-----QYLVRQAGGGPL--SDDGSGKATFNDPAFVQALQKLQDLVKAGA-----FQEGFEGIDYDDAgQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 279 LFFKGKAAMILDGPWVISEFKNRMmwdkeaKEIDWGMVTAPVDPANPEESSYASLNEVFAIAADSPNKRAAWEFVKFVNG 358
Cdd:cd14749 229 AFAQGKAAMNIGGSWDLGAIKAGE------PGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 359 TEmAKAASRSSRGTLPTRNQFMKEMDGKsteafyllrPKAEYESMWGGPNVRIP---SDFYR-DFSQIMTTEMKAVVDNK 434
Cdd:cd14749 303 PE-VMKQYLEDVGLLPAKEVVAKDEDPD---------PVAILGPFADVLNAAGStpfLDEYWpAAAQVHKDAVQKLLTGK 372
|
410
....*....|...
gi 2537007657 435 KTVEEAAAAIQAK 447
Cdd:cd14749 373 IDPEQVVKQAQSA 385
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
45-447 |
5.84e-20 |
|
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: 91.29 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 45 SEEGFYSDYGNSFNVKYPDIEFEVVS------QQEMYQELQGNEdadyreemrkfldkhKPDVLMIDLQTMEKMAQEGKL 118
Cdd:cd14751 11 EEKVLYEKLIPAFEKEYPKIKVKAVRvpfdglHNQIKTAAAGGQ---------------APDVMRADIAWVPEFAKLGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 119 YNLDAIIAQekFDLEGFMPGliDMIRAKGSGSLYGLAPNFYTNVIFYNAGLFREHNIEPPRnkmTWQELIDLSSRfsgIG 198
Cdd:cd14751 76 QPLDGTPAF--DDIVDYLPG--PMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPK---TMDELVAAAKA---IK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 199 SGENQiYGYYerfgsadqlLNRIAQGSSLRLFDAKGEKLvfnTDGWKQAMKLASEA----------IRNKAIYTQPMDES 268
Cdd:cd14751 146 KKKGR-YGLY---------ISGDGPYWLLPFLWSFGGDL---TDEKKATGYLNSPEsvraletivdLYDEGAITPCASGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 269 NERvfMGDDdlFFKGKAAMILDGPWVISEFKNrmmwDKEAKEIDwGMVTAPVdPANPEESSYASLNEVFAIAADSPNKRA 348
Cdd:cd14751 213 YPN--MQDG--FKSGRYAMIVNGPWAYADILG----GKEFKDPD-NLGIAPV-PAGPGGSGSPVGGEDLVIFKGSKNKDA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 349 AWEFVKFVNGTEmAKAASRSSRGTLPTRNQFMKEMDGKSTEAFyllrpkAEYESMWGGPNVRIPSDFYRDFSQIMTTEMK 428
Cdd:cd14751 283 AWKFVKFMSSAE-AQALTAAKLGLLPTRTSAYESPEVANNPMV------AAFKPALETAVPRPPIPEWGELFEPLTLAFA 355
|
410
....*....|....*....
gi 2537007657 429 AVVDNKKTVEEAAAAIQAK 447
Cdd:cd14751 356 KVLRGEKSPREALDEAAKQ 374
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
57-363 |
2.47e-18 |
|
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: 85.55 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 57 FNVKYPDIEFEVVSQqemyqelqgnEDADYREEMRKFLDKHKP--DVLMIDLQTMEKMAQEGKLYNLDAIIAQEKFDleg 134
Cdd:pfam01547 17 FEKEHPGIKVEVESV----------GSGSLAQKLTTAIAAGDGpaDVFASDNDWIAELAKAGLLLPLDDYVANYLVL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 135 fmpglidmirakGSGSLYGLAPNFYTNVIFYNAGLFREHNIEPPRnkmTWQELIDLSSRFSGIGsGENQIYGYYERFGSA 214
Cdd:pfam01547 84 ------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPK---TWDELLEAAKKLKEKG-KSPGGAGGGDASGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 215 DQLLNRIAQGSSLRLFDAKGEKLVF----NTDGWKQAMKLASEAIRNKAIYTQPMDESNERVfmgddDLFFKGKAAMILD 290
Cdd:pfam01547 148 GYFTLALLASLGGPLFDKDGGGLDNpeavDAITYYVDLYAKVLLLKKLKNPGVAGADGREAL-----ALFEQGKAAMGIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537007657 291 GPWVISEFKN-----RMMWDKEAKEIDWGMVTAPVDPANPEESSYaslnevFAIAADSPNKRAAWEFVKFVNGTEMAK 363
Cdd:pfam01547 223 GPWAALAANKvklkvAFAAPAPDPKGDVGYAPLPAGKGGKGGGYG------LAIPKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
135-453 |
2.85e-14 |
|
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: 74.27 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 135 FMPGLIDMIraKGSGSLYGLAPNFYTNVIFYNAGLFREHN-IEPPRnkmTWQELIDLSSR-------FSGIG--SGENQI 204
Cdd:cd14747 91 LFPGLVDTG--TVDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPK---TWDELEAAAKKikadgpdVSGFAipGKNDVW 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 205 YGYYERFGSAdqllnriaqGSSLRLFDAKgeKLVFNT----DGWKQAMKLASEAIRNKAiytQPMDESNErvfmgdDDLF 280
Cdd:cd14747 166 HNALPFVWGA---------GGDLATKDKW--KATLDSpeavAGLEFYTSLYQKGLSPKS---TLENSADV------EQAF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 281 FKGKAAMILDGPWVISEFKNRMMWDKEakeiDWGmvTAPVdPANPEESSYASL-NEVFAIAADSPNKRAAWEFVKFVNGT 359
Cdd:cd14747 226 ANGKVAMIISGPWEIGAIREAGPDLAG----KWG--VAPL-PGGPGGGSPSFAgGSNLAVFKGSKNKDLAWKFIEFLSSP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 360 EMAKAASRSSrGTLPTRNQFMKEMDGKSTEAFYLLRPKAEYEsmWGGPNV----RIpsdfyrdfSQIMTTE-MKAVVDNK 434
Cdd:cd14747 299 ENQAAYAKAT-GMLPANTSAWDDPSLANDPLLAVFAEQLKTG--KATPATpewgEI--------EAELVLVlEEVWIGVG 367
|
330
....*....|....*....
gi 2537007657 435 KTVEEAAAAIQAKGEEALQ 453
Cdd:cd14747 368 ADVEDALDKAAAEINEILN 386
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
77-447 |
4.44e-13 |
|
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: 70.48 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 77 ELQGNEDADYREEMRKFLDKHKPDVLMIDLQtmEKMAQEGKLYNldAIIAQEKFDLEGF---------MPGLIDMIRAKG 147
Cdd:cd13657 7 ALTGAEEDALQQIIDEFEAKYPVPNVKVPFE--KKPDLQNKLLT--AIPAGEGPDLFIWahdwigqfaEAGLLVPISDYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 148 S------------------GSLYGLAPNFYTNVIFYNAGLFREhniePPRnkmTWQELIDLSSRFSGIGSGE----NQIY 205
Cdd:cd13657 83 SeddfenylptaveavtykGKVYGLPEAYETVALIYNKALVDQ----PPE---TTDELLAIMKDHTDPAAGSyglaYQVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 206 GYYerFGSAdqllnrIAQGSSLRLFDAKGEKLVFNTDGWKQAMKLASEAIRnKAIYTQPMDESNERVFMgdddlffKGKA 285
Cdd:cd13657 156 DAY--FVSA------WIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFN-------EGKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 286 AMILDGPWVISEFKnrmmwdkeAKEIDWGMVTAP-VDPANPE------ESSYaslnevFAIAADSPNKRAAWEFVKFVNG 358
Cdd:cd13657 220 AMIINGPWFIGGIK--------AAGIDLGVAPLPtVDGTNPPrpysgvEGIY------VTKYAERKNKEAALDFAKFFTT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 359 TEMAKAASRSSrGTLPTRNQFMKEMDGKSTEAFYLLRPKAEY----------ESMWGGpnvripsdfyrdfsqiMTTEMK 428
Cdd:cd13657 286 AEASKILADEN-GYVPAATNAYDDAEVAADPVIAAFKAQAEHgvpmpnspemASVWGP----------------VTLALA 348
|
410
....*....|....*....
gi 2537007657 429 AVVDNKKTVEEAAAAIQAK 447
Cdd:cd13657 349 AVYQGGQDPQEALAAAQQE 367
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
99-389 |
1.03e-09 |
|
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: 60.19 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 99 PDVLMIDLQTMEKMAQEGKLynldAIIAQEKFDLEGFMPGLIDMIRAKGSgsLYGLAPNFYTNVIFYNAGLFREhniePP 178
Cdd:cd13658 54 PDVMVAPHDRIGSAVLQGLL----SPIKLSKDKKKGFTDQALKALTYDGK--LYGLPAAVETLALYYNKDLVKN----AP 123
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 179 RnkmTWQELIDLSSRFSGigSGENQI----------YGYYERFGSADQLLNRiaQGSSLRLFDakgekLVFNTDGWKQAM 248
Cdd:cd13658 124 K---TFDELEALAKDLTK--EKGKQYgfladatnfyYSYGLLAGNGGYIFKK--NGSDLDIND-----IGLNSPGAVKAV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 249 KLAsEAIRNKAIYTQPMdesnervfMGD--DDLFFKGKAAMILDGPWVISEFknrmmwdKEAKeIDWGMVTAPVDPANPE 326
Cdd:cd13658 192 KFL-KKWYTEGYLPKGM--------TGDviQGLFKEGKAAAVIDGPWAIQEY-------QEAG-VNYGVAPLPTLPNGKP 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2537007657 327 ESSYASLnEVFAIAADSPNKRAAWEFVKFVNGTEMAKAASRSSrGTLPTRNQFMKEMDGKSTE 389
Cdd:cd13658 255 MAPFLGV-KGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDET-NEIPPRKDVRSDPEIKNNP 315
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| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
99-360 |
3.05e-06 |
|
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: 49.76 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 99 PDVLMID--LQTMEKMAQEGKLYNLDAIIAQekfdlegfMPGLIDMIRAKGS---------GSLYGLA---PNFYTN-VI 163
Cdd:cd13521 58 PDIVGADylKDKFIAYGMEGAFLPLSKYIDQ--------YPNLKAFFKQHPDvlrastasdGKIYLIPyepPKDVPNqGY 129
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 164 FYNAGLFREHNIEPPRnkmTWQELIDLSSRFSgigSGENQIYGYYERFGSAD--------QLLN----RIAQGSSLRLFD 231
Cdd:cd13521 130 FIRKDWLDKLNLKTPK---TLDELYNVLKAFK---EKDPNGNGKADEIPFIDrdplygafRLINswgaRSAGGSTDSDWY 203
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 232 AKGEKLV--FNTDGWKQAM----KLASEAIRNKAIYTQPMDESNErvfmgdddLFFKGKAAMILDGPWVISEFKNRMMWD 305
Cdd:cd13521 204 EDNGKFKhpFASEEYKDGMkymnKLYTEGLIDKESFTQKDDQAEQ--------KFSNGKLGGFTHNWFASDNLFTAQLGK 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2537007657 306 KEAKEIDWGMVTA-PVDPANPEESSYASLNEVFAIAADSPNKRAAWEFVKFVNGTE 360
Cdd:cd13521 276 EKPMYILLPIAPAgNVKGRREEDSPGYTGPDGVAISKKAKNPVAALKFFDWLASEE 331
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| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
100-376 |
9.73e-06 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 47.40 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 100 DVLMIDLQTMEKMAQEGKLYNLDAIIAQEKFDlEGFMPGLIDmirakgsGSLYGLAPNFYT-NVIFYNAGLFREHNIEPp 178
Cdd:pfam13416 41 DVVWIAADQLATLAEAGLLADLSDVDNLDDLP-DALDAAGYD-------GKLYGVPYAASTpTVLYYNKDLLKKAGEDP- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 179 rnkMTWQELIDLSSRFSGigsgenqiygyyeRFGSADQLLN--RIAQGSSLRLFDAKGEKLvfntDGWKQAMKLASEAIR 256
Cdd:pfam13416 112 ---KTWDELLAAAAKLKG-------------KTGLTDPATGwlLWALLADGVDLTDDGKGV----EALDEALAYLKKLKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 257 NKAIYtqpmdESNERVfmgdDDLFFKGKAAMILDGPWVISEFKNRmmwdkeakEIDWGMVtAPVDpanpeesSYASLNEV 336
Cdd:pfam13416 172 NGKVY-----NTGADA----VQLFANGEVAMTVNGTWAAAAAKKA--------GKKLGAV-VPKD-------GSFLGGKG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2537007657 337 FAIAADSPNKR-AAWEFVKFVNGTEMAKAASRsSRGTLPTR 376
Cdd:pfam13416 227 LVVPAGAKDPRlAALDFIKFLTSPENQAALAE-DTGYIPAN 266
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|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
239-354 |
9.19e-03 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 38.45 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007657 239 FNTDGWKQAMKLASEAIRNKAIyTQPMDESnerVFMGDddlFFKGKAAMILDGPWVISEFknrmmwdkEAKEIDWGMVTA 318
Cdd:PRK09474 209 VNNAGAKAGLQFLVDLVKNKHM-NADTDYS---IAEAA---FNKGETAMTINGPWAWSNI--------DKSGINYGVTVL 273
|
90 100 110
....*....|....*....|....*....|....*.
gi 2537007657 319 PVDPANPEESSYASLNEvfAIAADSPNKRAAWEFVK 354
Cdd:PRK09474 274 PTFNGKPSKPFVGVLSA--GINAASPNKELAKEFLE 307
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