|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
3-365 |
1.24e-41 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 152.51 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 3 KKWKIALLLTMVVALlSGCFGEKpvlDELGKGGKGKIKVVYHNEDS---FYRQYGNYFNVKYPDIEFEIVNMQemYQELQ 79
Cdd:COG1653 2 RRLALALAAALALAL-AACGGGG---SGAAAAAGKVTLTVWHTGGGeaaALEALIKEFEAEHPGIKVEVESVP--YDDYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 80 DKENVDyeeerkkFLDKHKPDVLMIDLDTMEKLVQEGKLYNLDAVIAQEKFDLEGYMPGLVDMIRErgGGSLYGLAPYFY 159
Cdd:COG1653 76 TKLLTA-------LAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTY--DGKLYGVPFNTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 160 TTVIYYNAELFRDHNIEPPRnkmTWQEILDLSSRFASVGsGENQIygyyqRYGGGAQELLLDIANASSLRFFDAKGeKLV 239
Cdd:COG1653 147 TLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKLKAKD-GVYGF-----ALGGKDGAAWLDLLLSAGGDLYDEDG-KPA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 240 FNTDGWKQLVKLTTDAIRNKGV--YSQTWDEGDSRgfssddDLFFKGRAAMIMDGPWFISQIKNramwdkEAKPIDWGMV 317
Cdd:COG1653 217 FDSPEAVEALEFLKDLVKDGYVppGALGTDWDDAR------AAFASGKAAMMINGSWALGALKD------AAPDFDVGVA 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2537007659 318 SVPVDPASPDESSYASlNEVYAIAADSPNKRAAWEFVKFVNGPEMAKA 365
Cdd:COG1653 285 PLPGGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSPEAQAK 331
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
57-448 |
4.48e-37 |
|
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: 140.51 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 57 FNVKYPDIEFEIVNMQemyqelqdkenvDYEEERKKFLDKHK----PDVLMIDLDTMEKLVQEGKLYNLDAVIAQEKFDL 132
Cdd:cd14748 23 FNKSHPDIKVKAVYQG------------SYDDTLTKLLAALAagtaPDVAQVDASWVAQLADSGALEPLDDYIDKDGVDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 133 EGYMPGLVDMIRErgGGSLYGLaPYFYTT-VIYYNAELFRDH---NIEPPRnkmTWQEILDLSSRFASVGSGENQIygYY 208
Cdd:cd14748 91 DDFYPAALDAGTY--DGKLYGL-PFDTSTpVLYYNKDLFEEAgldPEKPPK---TWDELEEAAKKLKDKGGKTGRY--GF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 209 QRYGGGAQELLLDIANASSLRFFDAKGEKLVFNTDGWKQLVKLTTDAIRNKGVySQTWDEGDSrgfssdDDLFFKGRAAM 288
Cdd:cd14748 163 ALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGV-SPLNDWGDA------QDAFISGKVAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 289 IMDGPWFISQIKnramwdKEAKPIDWGMVSVPVDPASPDESSYASLNevYAIAADSP-NKRAAWEFVKFVNGPEMAKAAS 367
Cdd:cd14748 236 TINGTWSLAGIR------DKGAGFEYGVAPLPAGKGKKGATPAGGAS--LVIPKGSSkKKEAAWEFIKFLTSPENQAKWA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 368 RsMDGNLPTRNQFMkeidgKSTEAFYALRPKAK--YESMWGGPDVEVPSEFYSDFRTILDKELRAVIDNKKTVDEAVAAI 445
Cdd:cd14748 308 K-ATGYLPVRKSAA-----EDPEEFLAENPNYKvaVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEA 381
|
...
gi 2537007659 446 QSE 448
Cdd:cd14748 382 QEK 384
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
44-364 |
3.68e-20 |
|
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: 90.55 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 44 HNEDSFYRQYGNYFNVKYPDIEFEIVNMQemYQELQDKENVDYEEERKKfldkhkPDVLMIDLDTMEKLVQEGKLYNLDA 123
Cdd:pfam01547 4 LTEAAALQALVKEFEKEHPGIKVEVESVG--SGSLAQKLTTAIAAGDGP------ADVFASDNDWIAELAKAGLLLPLDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 124 VIAQEKFDlegympglvdmirerGGGSLYGLAPYFYTTVIYYNAELFRDHNIEPPRnkmTWQEILDLSSRFasVGSGENQ 203
Cdd:pfam01547 76 YVANYLVL---------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPK---TWDELLEAAKKL--KEKGKSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 204 IYGYYQRYGGGAQELLLDIANASSLRFFDAKGEKLV-------FNTDGWKQLVKLTTDAIRNKGVYSQTWDEGDsrgfss 276
Cdd:pfam01547 136 GGAGGGDASGTLGYFTLALLASLGGPLFDKDGGGLDnpeavdaITYYVDLYAKVLLLKKLKNPGVAGADGREAL------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 277 ddDLFFKGRAAMIMDGPWFISQ-----IKNRAMWDKEAKPIDWGMVSVPVDPASPDESSYaslnevYAIAADSPNKRAAW 351
Cdd:pfam01547 210 --ALFEQGKAAMGIVGPWAALAankvkLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYG------LAIPKGSKNKEAAK 281
|
330
....*....|...
gi 2537007659 352 EFVKFVNGPEMAK 364
Cdd:pfam01547 282 KFLDFLTSPEAQA 294
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
3-365 |
1.24e-41 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 152.51 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 3 KKWKIALLLTMVVALlSGCFGEKpvlDELGKGGKGKIKVVYHNEDS---FYRQYGNYFNVKYPDIEFEIVNMQemYQELQ 79
Cdd:COG1653 2 RRLALALAAALALAL-AACGGGG---SGAAAAAGKVTLTVWHTGGGeaaALEALIKEFEAEHPGIKVEVESVP--YDDYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 80 DKENVDyeeerkkFLDKHKPDVLMIDLDTMEKLVQEGKLYNLDAVIAQEKFDLEGYMPGLVDMIRErgGGSLYGLAPYFY 159
Cdd:COG1653 76 TKLLTA-------LAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTY--DGKLYGVPFNTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 160 TTVIYYNAELFRDHNIEPPRnkmTWQEILDLSSRFASVGsGENQIygyyqRYGGGAQELLLDIANASSLRFFDAKGeKLV 239
Cdd:COG1653 147 TLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKLKAKD-GVYGF-----ALGGKDGAAWLDLLLSAGGDLYDEDG-KPA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 240 FNTDGWKQLVKLTTDAIRNKGV--YSQTWDEGDSRgfssddDLFFKGRAAMIMDGPWFISQIKNramwdkEAKPIDWGMV 317
Cdd:COG1653 217 FDSPEAVEALEFLKDLVKDGYVppGALGTDWDDAR------AAFASGKAAMMINGSWALGALKD------AAPDFDVGVA 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2537007659 318 SVPVDPASPDESSYASlNEVYAIAADSPNKRAAWEFVKFVNGPEMAKA 365
Cdd:COG1653 285 PLPGGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSPEAQAK 331
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
57-448 |
4.48e-37 |
|
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: 140.51 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 57 FNVKYPDIEFEIVNMQemyqelqdkenvDYEEERKKFLDKHK----PDVLMIDLDTMEKLVQEGKLYNLDAVIAQEKFDL 132
Cdd:cd14748 23 FNKSHPDIKVKAVYQG------------SYDDTLTKLLAALAagtaPDVAQVDASWVAQLADSGALEPLDDYIDKDGVDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 133 EGYMPGLVDMIRErgGGSLYGLaPYFYTT-VIYYNAELFRDH---NIEPPRnkmTWQEILDLSSRFASVGSGENQIygYY 208
Cdd:cd14748 91 DDFYPAALDAGTY--DGKLYGL-PFDTSTpVLYYNKDLFEEAgldPEKPPK---TWDELEEAAKKLKDKGGKTGRY--GF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 209 QRYGGGAQELLLDIANASSLRFFDAKGEKLVFNTDGWKQLVKLTTDAIRNKGVySQTWDEGDSrgfssdDDLFFKGRAAM 288
Cdd:cd14748 163 ALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGV-SPLNDWGDA------QDAFISGKVAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 289 IMDGPWFISQIKnramwdKEAKPIDWGMVSVPVDPASPDESSYASLNevYAIAADSP-NKRAAWEFVKFVNGPEMAKAAS 367
Cdd:cd14748 236 TINGTWSLAGIR------DKGAGFEYGVAPLPAGKGKKGATPAGGAS--LVIPKGSSkKKEAAWEFIKFLTSPENQAKWA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 368 RsMDGNLPTRNQFMkeidgKSTEAFYALRPKAK--YESMWGGPDVEVPSEFYSDFRTILDKELRAVIDNKKTVDEAVAAI 445
Cdd:cd14748 308 K-ATGYLPVRKSAA-----EDPEEFLAENPNYKvaVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEA 381
|
...
gi 2537007659 446 QSE 448
Cdd:cd14748 382 QEK 384
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
57-448 |
4.44e-35 |
|
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: 134.84 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 57 FNVKYPDIEFEIVNMQemYQELQDKENVDyeeerkkFLDKHKPDVLMIDLDTMEKLVQEGKLYNLDAVIAQEKFDlEGYM 136
Cdd:cd13585 23 FEKENPGVKVEVVPVP--YDDYWTKLTTA-------AAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKDGLD-DDFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 137 PGLVDMIRerGGGSLYGLAPYFYTTVIYYNAELFRD--HNIEPPrnkMTWQEILDLSSRFASVGSGENQIYGYYQRYGGG 214
Cdd:cd13585 93 PGLLDAGT--YDGKLYGLPFDADTLVLFYNKDLFDKagPGPKPP---WTWDELLEAAKKLTDKKGGQYGFALRGGSGGQT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 215 AQELLLDIANASslrFFDAKGEKLVFNTDGWKQLVKLTTDAIRNKGVYSQTWDegdsrGFSSDDDLFFKGRAAMIMDGPW 294
Cdd:cd13585 168 QWYPFLWSNGGD---LLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATT-----GGDEAVDLFASGKVAMMIDGPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 295 FISQIKNramwdkEAKPIDWGMVSVPVDPASPDESSYASLNevYAIAADSPNKRAAWEFVKFVNGPEMAKAASRSMDGNL 374
Cdd:cd13585 240 ALGTLKD------SKVKFKWGVAPLPAGPGGKRASVLGGWG--LAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAA 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537007659 375 PTRNQFMKEIDGKSTEAFYALRPKAKYESMWgGPDVEVPSEFYSDFRTILDKELRAVIdnKKTVDEAVAAIQSE 448
Cdd:cd13585 312 LAAAAASAAAPDAKPALALAAAADALAAAVP-PPVPPPWPEVYPILSEALQEALLGAL--GKSPEEALKEAAKE 382
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-455 |
2.40e-33 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 130.84 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 1 MLKKWKIALLLTMVVAL-LSGCFGEKPVLDELGKGGKGKIKVVYHNED--SFYRQYGNYFNVKyPDIEFEIVNmqemyqe 77
Cdd:COG2182 1 MKRRLLAALALALALALaLAACGSGSSSSGSSSAAGAGGTLTVWVDDDeaEALEEAAAAFEEE-PGIKVKVVE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 78 lqdkenVDYEEERKKFLDKHK----PDVLMIDLDTMEKLVQEGKLYNLDAVIAqekfDLEGYMPGLVDMIRErgGGSLYG 153
Cdd:COG2182 73 ------VPWDDLREKLTTAAPagkgPDVFVGAHDWLGELAEAGLLAPLDDDLA----DKDDFLPAALDAVTY--DGKLYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 154 LaPYFY-TTVIYYNAELFRDhniEPPRnkmTWQEILDLSSRFASVGSgenqiygyyqrygggaQELLLDIANA---SSL- 228
Cdd:COG2182 141 V-PYAVeTLALYYNKDLVKA---EPPK---TWDELIAAAKKLTAAGK----------------YGLAYDAGDAyyfYPFl 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 229 -----RFFDAKGE---KLVFNTDG-------WKQLVKlttdairnKGVYSQTWDEGDSrgfssdDDLFFKGRAAMIMDGP 293
Cdd:COG2182 198 aafggYLFGKDGDdpkDVGLNSPGavaaleyLKDLIK--------DGVLPADADYDAA------DALFAEGKAAMIINGP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 294 WFISQIKnramwdkEAKPIDWGMVSVPVDPASPDESSYASlNEVYAIAADSPNKRAAWEFVKFVNGPEMAKAASrSMDGN 373
Cdd:COG2182 264 WAAADLK-------KALGIDYGVAPLPTLAGGKPAKPFVG-VKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALF-EATGR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 374 LPTRNQFMKEIDGKSTEAFYALRPKAKY-ESMWGGPDvevpsefYSDFRTILDKELRAVIDNKKTVDEAVAAIQSEGEAA 452
Cdd:COG2182 335 IPANKAAAEDAEVKADPLIAAFAEQAEYaVPMPNIPE-------MGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
|
...
gi 2537007659 453 LQK 455
Cdd:COG2182 408 IAQ 410
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
41-446 |
1.65e-21 |
|
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: 95.82 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 41 VVYHNED---SFYRQYGNYFNVKYpDIEFEIVNmqemyqelqdkenVDYEEERKKFLDKHK----PDVLMIDLDTMEKLV 113
Cdd:cd13586 3 TVWTDEDgelEYLKELAEEFEKKY-GIKVEVVY-------------VDSGDTREKFITAGPagkgPDVFFGPHDWLGELA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 114 QEGKLYNLDAVIAQEKFDLEGYMPGLvdmireRGGGSLYGLaPY-FYTTVIYYNAELFrdhnIEPPRnkmTWQEILDLSS 192
Cdd:cd13586 69 AAGLLAPIPEYLAVKIKNLPVALAAV------TYNGKLYGV-PVsVETIALFYNKDLV----PEPPK---TWEELIALAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 193 RFasVGSGENQIygyyqrygggaqELLLDIANASSL---------RFFDAKGE---KLVFNTDGWKQLVKLTTDAIRNKG 260
Cdd:cd13586 135 KF--NDKAGGKY------------GFAYDQTNPYFSypflaafggYVFGENGGdptDIGLNNEGAVKGLKFIKDLKKKYK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 261 VysqtWDEGDSRGFSsdDDLFFKGRAAMIMDGPWFISQIknramwdKEAKpIDWGMVSVPVDPASPDESSYASlNEVYAI 340
Cdd:cd13586 201 V----LPPDLDYDIA--DALFKEGKAAMIINGPWDLADY-------KDAG-INFGVAPLPTLPGGKQAAPFVG-VQGAFV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 341 AADSPNKRAAWEFVKFVNGPEMAKAASRsMDGNLPTRNQFMKEIDGKSTEAFYALRPKAKYesmwGGPDVEVP--SEFYS 418
Cdd:cd13586 266 SAYSKNKEAAVEFAEYLTSDEAQLLLFE-KTGRIPALKDALNDAAVKNDPLVKAFAEQAQY----GVPMPNIPemAAVWD 340
|
410 420
....*....|....*....|....*...
gi 2537007659 419 DFRTildkELRAVIDNKKTVDEAVAAIQ 446
Cdd:cd13586 341 AMGN----ALNLVASGKATPEEAAKDAV 364
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
57-448 |
3.16e-21 |
|
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: 95.44 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 57 FNVKYPDIEFEIVnmqemyqelqdkENVDYEEERKKFLDKH------KPDVLMIDLDTMEKLVQEGKLYNLDAVIAQEKF 130
Cdd:cd14750 23 FEKKHPDIKVEIE------------ELPASSDDQRQQLVTAlaagssAPDVLGLDVIWIPEFAEAGWLLPLTEYLKEEED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 131 DleGYMPGLVDMIRERGggSLYGLaPYFY-TTVIYYNAELFRDHNIEPPRnkmTWQEILDLSSrfASVGSGENQI----- 204
Cdd:cd14750 91 D--DFLPATVEANTYDG--KLYAL-PWFTdAGLLYYRKDLLEKYGPEPPK---TWDELLEAAK--KRKAGEPGIWgyvfq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 205 YGYYQRYGGGAQELLldiaNASSLRFFDAKGEKLVFNTDGWKQ----LVKLTTDAIRNKGVYsqTWDEGDSRgfssddDL 280
Cdd:cd14750 161 GKQYEGLVCNFLELL----WSNGGDIFDDDSGKVTVDSPEALEalqfLRDLIGEGISPKGVL--TYGEEEAR------AA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 281 FFKGRAAMIMDGP--WFISQIKNRAMWDKeakpidwgmVSVPVDPASPDESSYASL-NEVYAIAADSPNKRAAWEFVKFV 357
Cdd:cd14750 229 FQAGKAAFMRNWPyaYALLQGPESAVAGK---------VGVAPLPAGPGGGSASTLgGWNLAISANSKHKEAAWEFVKFL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 358 NGPEMAKAASRsMDGNLPTR------------NQFMKEIdGKSTEAFYAlRPKakyesmwggpdvevpSEFYSDFRTILD 425
Cdd:cd14750 300 TSPEVQKRRAI-NGGLPPTRralyddpevleaYPFLPAL-LEALENAVP-RPV---------------TPKYPEVSTAIQ 361
|
410 420
....*....|....*....|...
gi 2537007659 426 KELRAVIDNKKTVDEAVAAIQSE 448
Cdd:cd14750 362 IALSAALSGQATPEEALKQAQEK 384
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
44-364 |
3.68e-20 |
|
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: 90.55 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 44 HNEDSFYRQYGNYFNVKYPDIEFEIVNMQemYQELQDKENVDYEEERKKfldkhkPDVLMIDLDTMEKLVQEGKLYNLDA 123
Cdd:pfam01547 4 LTEAAALQALVKEFEKEHPGIKVEVESVG--SGSLAQKLTTAIAAGDGP------ADVFASDNDWIAELAKAGLLLPLDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 124 VIAQEKFDlegympglvdmirerGGGSLYGLAPYFYTTVIYYNAELFRDHNIEPPRnkmTWQEILDLSSRFasVGSGENQ 203
Cdd:pfam01547 76 YVANYLVL---------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPK---TWDELLEAAKKL--KEKGKSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 204 IYGYYQRYGGGAQELLLDIANASSLRFFDAKGEKLV-------FNTDGWKQLVKLTTDAIRNKGVYSQTWDEGDsrgfss 276
Cdd:pfam01547 136 GGAGGGDASGTLGYFTLALLASLGGPLFDKDGGGLDnpeavdaITYYVDLYAKVLLLKKLKNPGVAGADGREAL------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 277 ddDLFFKGRAAMIMDGPWFISQ-----IKNRAMWDKEAKPIDWGMVSVPVDPASPDESSYaslnevYAIAADSPNKRAAW 351
Cdd:pfam01547 210 --ALFEQGKAAMGIVGPWAALAankvkLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYG------LAIPKGSKNKEAAK 281
|
330
....*....|...
gi 2537007659 352 EFVKFVNGPEMAK 364
Cdd:pfam01547 282 KFLDFLTSPEAQA 294
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
57-462 |
1.04e-18 |
|
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: 87.82 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 57 FNVKYPDIEFEIVNMqemyqelqdkENVDYEEERKKFLDKHK-PDVLMIDLDT-MEKLVQEGKLYNLDAVIAQEKFDlEG 134
Cdd:cd14749 24 FEKENPNIKVKVVVF----------PYDNYKTKLKTAVAAGEgPDVFNLWPGGwLAEFVKAGLLLPLTDYLDPNGVD-KR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 135 YMPGLVDMirERGGGSLYGLAPYFYTTVIYYNAELFRDHNI-EPPRnkmTWQEILDLSSRFASVGSGENQIYGYYQRYGG 213
Cdd:cd14749 93 FLPGLADA--VTFNGKVYGIPFAARALALFYNKDLFEEAGGvKPPK---TWDELIEAAKKDKFKAKGQTGFGLLLGAQGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 214 GAQELLLDIANASSLRFFDAKGeKLVFNTDGWKQLVKLTTDAIRNKGVysqtwDEGDSrGFSSDDD--LFFKGRAAMIMD 291
Cdd:cd14749 168 HWYFQYLVRQAGGGPLSDDGSG-KATFNDPAFVQALQKLQDLVKAGAF-----QEGFE-GIDYDDAgqAFAQGKAAMNIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 292 GPWFISQIKNramwdkEAKPIDWGMVSVPVDPASPDESSYASLNEVYAIAADSPNKRAAWEFVKFVNGPEMAKAasRSMD 371
Cdd:cd14749 241 GSWDLGAIKA------GEPGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQ--YLED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 372 GNLPTRNQfmkeidGKSTEAFYALRPKAkyesmwgGPDVEVPSEFYSDFRtiLDKELRAVIDN-KKTVDEAVAAiQSEGE 450
Cdd:cd14749 313 VGLLPAKE------VVAKDEDPDPVAIL-------GPFADVLNAAGSTPF--LDEYWPAAAQVhKDAVQKLLTG-KIDPE 376
|
410
....*....|..
gi 2537007659 451 AALQKGREAEKA 462
Cdd:cd14749 377 QVVKQAQSAAAK 388
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
46-445 |
1.05e-17 |
|
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: 84.74 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 46 EDSFYRQYGNYFNVKYPDIEfeiVNMQemyqelqdkeNVDYEEERKKFLDKHK----PDVLMIDLDTMEKLVQEGKLYNL 121
Cdd:cd14751 12 EKVLYEKLIPAFEKEYPKIK---VKAV----------RVPFDGLHNQIKTAAAggqaPDVMRADIAWVPEFAKLGYLQPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 122 DAVIAQekFDLEGYMPGlvDMIRERGGGSLYGLAPYFYTTVIYYNAELFRDHNIEPPRnkmTWQEILDLSsRFASVGSGE 201
Cdd:cd14751 79 DGTPAF--DDIVDYLPG--PMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPK---TMDELVAAA-KAIKKKKGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 202 NQIYGYYQRYGggaqellldianaSSLRFFDAKGEKLvfnTDGWKQLVKLTT-DAIRNKGVYSQTWDEGDSRGFSSDDDL 280
Cdd:cd14751 151 YGLYISGDGPY-------------WLLPFLWSFGGDL---TDEKKATGYLNSpESVRALETIVDLYDEGAITPCASGGYP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 281 -----FFKGRAAMIMDGPWFISQIKNramwDKEAKPID-WGMVSVpvdPASPDESSYASLNEVYAIAADSPNKRAAWEFV 354
Cdd:cd14751 215 nmqdgFKSGRYAMIVNGPWAYADILG----GKEFKDPDnLGIAPV---PAGPGGSGSPVGGEDLVIFKGSKNKDAAWKFV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 355 KFVNGPEMAKAASRSMdGNLPTrNQFMKEIDGKSTEAFYALRpKAKYESMWGGPDVEVPSEFYSDFRTILDKELRAVIDN 434
Cdd:cd14751 288 KFMSSAEAQALTAAKL-GLLPT-RTSAYESPEVANNPMVAAF-KPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSP 364
|
410
....*....|.
gi 2537007659 435 KKTVDEAVAAI 445
Cdd:cd14751 365 REALDEAAKQW 375
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
45-448 |
1.19e-14 |
|
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: 75.49 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 45 NEDSFYRQYGNYFNVKYPDIEFEIVnmQEMYQELQDKENVDYEEERKkfldkhkPDVLMIDLDTMEKLVQEGKLYNLDAV 124
Cdd:cd13657 11 AEEDALQQIIDEFEAKYPVPNVKVP--FEKKPDLQNKLLTAIPAGEG-------PDLFIWAHDWIGQFAEAGLLVPISDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 125 IAQEKFDLegYMPGLVDMIRERGGgsLYGLaPYFYTTV-IYYNAELFRdhniEPPRnkmTWQEILDLSSRFASVGSGENQ 203
Cdd:cd13657 82 LSEDDFEN--YLPTAVEAVTYKGK--VYGL-PEAYETVaLIYNKALVD----QPPE---TTDELLAIMKDHTDPAAGSYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 204 IYGYYQRYGGGAQellldIANASSLRFFDAKGEKLVFNTDGWKQLVKLTTDAIRNkgvYSQTWDEGDSRgfssdDDLFFK 283
Cdd:cd13657 150 LAYQVSDAYFVSA-----WIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWP---YMPSDPSYNTQ-----TSLFNE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 284 GRAAMIMDGPWFISQIKnramwdkeAKPIDWGMVSVP-VDPASPdESSYASLNEVY-AIAADSPNKRAAWEFVKFVNGPE 361
Cdd:cd13657 217 GKAAMIINGPWFIGGIK--------AAGIDLGVAPLPtVDGTNP-PRPYSGVEGIYvTKYAERKNKEAALDFAKFFTTAE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 362 MAKAASRsMDGNLPTRNQFMKEIDGKSTEAFYALRPKAKY----------ESMWGGpdvevpsefysdfrtiLDKELRAV 431
Cdd:cd13657 288 ASKILAD-ENGYVPAATNAYDDAEVAADPVIAAFKAQAEHgvpmpnspemASVWGP----------------VTLALAAV 350
|
410
....*....|....*..
gi 2537007659 432 IDNKKTVDEAVAAIQSE 448
Cdd:cd13657 351 YQGGQDPQEALAAAQQE 367
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
41-448 |
1.45e-14 |
|
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: 75.14 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 41 VVYHNEDSFYRQYGN----YFNVKYPDIEFEIVNmqemyqelQDKEnvdyeeERKKFLD-----KHKPDVLMIDLDTMEK 111
Cdd:cd13522 3 TVWHQYDTGENQAVNeliaKFEKAYPGITVEVTY--------QDTE------ARRQFFStaaagGKGPDVVFGPSDSLGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 112 LVQEGKLYNLDAVIAQEKFDLEGYMPGLvdmireRGGGSLYGLAPYFYTTVIYYNAELFRDhniEPPRnkmTWQEILDLS 191
Cdd:cd13522 69 FAAAGLLAPLDEYVSKSGKYAPNTIAAM------KLNGKLYGVPVSVGAHLMYYNKKLVPK---NPPK---TWQELIALA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 192 SRFASVGsgenqiygyYQRYGGGAQELLLDIAnasslrFFDAKGEKlVFNTDGwkQLVKLTTDAIRNKGVYSQTWDEGD- 270
Cdd:cd13522 137 QGLKAKN---------VWGLVYNQNEPYFFAA------WIGGFGGQ-VFKANN--GKNNPTLDTPGAVEALQFLVDLKSk 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 271 ------SRGFSSDDDLFFKGRAAMIMDGPWFISQIKNRAMWDKEAKPidWGMVSVPVDPASPDESSYASLNevyaiaADS 344
Cdd:cd13522 199 ykimppETDYSIADALFKAGKAAMIINGPWDLGDYRQALKINLGVAP--LPTFSGTKHAAPFVGGKGFGIN------KES 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 345 PNKRAAWEFVKFVNGPEMAKAASRSMdGNLPTRNQFMKEIDGKSTEAFYALRPKAKYesmwGGPDVEVPSefYSDFRTIL 424
Cdd:cd13522 271 QNKAAAVEFVKYLTSYQAQLVLFDDA-GDIPANLQAYESPAVQNKPAQKASAEQAAY----GVPMPNIPE--MRAVWDAF 343
|
410 420
....*....|....*....|....
gi 2537007659 425 DKELRAVIDNKKTVDEAVAAIQSE 448
Cdd:cd13522 344 RIAVNSVLAGKVTPEAAAKDAQQE 367
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
135-454 |
1.76e-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: 75.04 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 135 YMPGLVDMIRerGGGSLYGLAPYFYTTVIYYNAELFRDHN-IEPPRnkmTWQEILDLSSRFASVGSGenqIYGYYQRYGG 213
Cdd:cd14747 91 LFPGLVDTGT--VDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPK---TWDELEAAAKKIKADGPD---VSGFAIPGKN 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 214 GAQELLLDIANASSLRFFDAKGEKLVFNT----DGWKQLVKLTTDAIRNKgvySQTWDEGDSrgfssdDDLFFKGRAAMI 289
Cdd:cd14747 163 DVWHNALPFVWGAGGDLATKDKWKATLDSpeavAGLEFYTSLYQKGLSPK---STLENSADV------EQAFANGKVAMI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 290 MDGPWFISQIKNRAMWDKEakpiDWGMVSVpvdPASPDESSYASL-NEVYAIAADSPNKRAAWEFVKFVNGPEMAKAASR 368
Cdd:cd14747 234 ISGPWEIGAIREAGPDLAG----KWGVAPL---PGGPGGGSPSFAgGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 369 SMdGNLPTRNQFMKEIDGKSTEAFYALRPKAKY-ESM-----WGgpDVEvpsefysdfrTILDKEL-RAVIDNKKTVDEA 441
Cdd:cd14747 307 AT-GMLPANTSAWDDPSLANDPLLAVFAEQLKTgKATpatpeWG--EIE----------AELVLVLeEVWIGVGADVEDA 373
|
330
....*....|...
gi 2537007659 442 VAAIQSEGEAALQ 454
Cdd:cd14747 374 LDKAAAEINEILN 386
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
41-390 |
8.12e-13 |
|
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: 69.82 E-value: 8.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 41 VVYHNED---SFYRQYGNYFNVKYpDIEFEIVNMQEMYQelQDKENVDYEEERKkfldkhkPDVLMIDLDTMEKLVQEGK 117
Cdd:cd13658 3 TVWVDEDkkmAFIKKIAKQYTKKT-GVKVKLVEVDQLDQ--LEKLSLDGPAGKG-------PDVMVAPHDRIGSAVLQGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 118 LynldAVIAQEKFDLEGYMPglVDMIRERGGGSLYGLAPYFYTTVIYYNAELFRDhniePPRnkmTWQEILDLSSRFAsv 197
Cdd:cd13658 73 L----SPIKLSKDKKKGFTD--QALKALTYDGKLYGLPAAVETLALYYNKDLVKN----APK---TFDELEALAKDLT-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 198 GSGENQIYgyyqrygggaqeLLLDIANASSLRFFDAKGEKLVF---NTDGWKQLVKLTTDAIRNKGVYSQTW-DEGD-SR 272
Cdd:cd13658 138 KEKGKQYG------------FLADATNFYYSYGLLAGNGGYIFkknGSDLDINDIGLNSPGAVKAVKFLKKWyTEGYlPK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 273 GFSSD--DDLFFKGRAAMIMDGPWFISQIknramwdKEAKpIDWGMVSVPVDPASPDESSYASLnEVYAIAADSPNKRAA 350
Cdd:cd13658 206 GMTGDviQGLFKEGKAAAVIDGPWAIQEY-------QEAG-VNYGVAPLPTLPNGKPMAPFLGV-KGWYLSAYSKHKEWA 276
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2537007659 351 WEFVKFVNGPEMAKAASRSMdGNLPTRNQFMKEIDGKSTE 390
Cdd:cd13658 277 QKFMEFLTSKENLKKRYDET-NEIPPRKDVRSDPEIKNNP 315
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
100-377 |
2.82e-08 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 55.10 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 100 DVLMIDLDTMEKLVQEGKLYNLDAVIAQEKFDlEGYMPGLVDmirerggGSLYGLA-PYFYTTVIYYNAELFRDHNIEPp 178
Cdd:pfam13416 41 DVVWIAADQLATLAEAGLLADLSDVDNLDDLP-DALDAAGYD-------GKLYGVPyAASTPTVLYYNKDLLKKAGEDP- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 179 rnkMTWQEILDLSSRFAsvgsgenqiygyyqrygggAQELLLDIANASSLRFFDAKGEKLVFNTDGWKQLVKLTT--DAI 256
Cdd:pfam13416 112 ---KTWDELLAAAAKLK-------------------GKTGLTDPATGWLLWALLADGVDLTDDGKGVEALDEALAylKKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 257 RNKGVYSQTWDEGDSrgfssdddLFFKGRAAMIMDGPWFISQIKNRAmwdkeakpIDWGMVsVPVDpaspdesSYASLNE 336
Cdd:pfam13416 170 KDNGKVYNTGADAVQ--------LFANGEVAMTVNGTWAAAAAKKAG--------KKLGAV-VPKD-------GSFLGGK 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2537007659 337 VYAIAADSPNKR-AAWEFVKFVNGPEMAKAASRSMdGNLPTR 377
Cdd:pfam13416 226 GLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDT-GYIPAN 266
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
100-370 |
2.68e-04 |
|
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270307 [Multi-domain] Cd Length: 268 Bit Score: 42.60 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 100 DVLMIDLDTMEKLVQEGKLYNLDAVIaqekfdlegyMPGLVDMIRERGGGSLYGLAPYFYTTVIYYNAELFRDhniEPPR 179
Cdd:cd13589 55 DVVDLDDGDAARAIAEGLLEPLDYSK----------IPNAAKDKAPAALKTGYGVGYTLYSTGIAYNTDKFKE---PPTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 180 NKMTWqeiLDLSSRFAsvgsgenqiygyyqrygggaqelLLDIANASSLRFFDAK-----GEKLVFNTD-GWKQLvkltt 253
Cdd:cd13589 122 WWLAD---FWDVGKFP-----------------------GPRILNTSGLALLEAAlladgVDPYPLDVDrAFAKL----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 254 DAIRNkgvYSQTWDegdsrgfSSDDDLffkgrAAMIMDGPWFISQIKNRAMWDKEAKpidwgmvSVPVDPASPDESSYAS 333
Cdd:cd13589 171 KELKP---NVVTWW-------TSGAQL-----AQLLQSGEVDMAPAWNGRAQALIDA-------GAPVAFVWPKEGAILG 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 2537007659 334 LNeVYAIAADSPNKRAAWEFVKFVNGPEMAKAASRSM 370
Cdd:cd13589 229 PD-TLAIVKGAPNKELAMKFINFALSPEVQAALAEAL 264
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
100-370 |
8.73e-04 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 41.43 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 100 DVLMIDLDTMEKLVQEGKLynldaviaqEKFDLEG--YMPGLVDMIRERGG--GSLYGLaPYFY-TTVIYYNAELFRdhn 174
Cdd:COG0687 79 DVVVPSDYFVARLIKAGLL---------QPLDKSKlpNLANLDPRFKDPPFdpGNVYGV-PYTWgTTGIAYNTDKVK--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 175 iEPPRnkmTWQEILD--LSSRFASVGSgenqiygyyqrygggAQELLLDIANASSLRFFDAkgeklvfNTDGWKQLVKLT 252
Cdd:COG0687 146 -EPPT---SWADLWDpeYKGKVALLDD---------------PREVLGAALLYLGYDPNST-------DPADLDAAFELL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537007659 253 TDAIRNKGVYSQTWDEGDsrgfssddDLFFKGRAAMIMDGPWFISQIKnramwdKEAKPIDWgmvsvpvdpASPDESSYA 332
Cdd:COG0687 200 IELKPNVRAFWSDGAEYI--------QLLASGEVDLAVGWSGDALALR------AEGPPIAY---------VIPKEGALL 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 2537007659 333 SLNeVYAIAADSPNKRAAWEFVKFVNGPEMAKAASRSM 370
Cdd:COG0687 257 WFD-NMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYV 293
|
|
| |
