|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
39-420 |
2.11e-83 |
|
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: 260.69 E-value: 2.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQGSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFD 118
Cdd:cd14748 1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 119 SEMlngsnKLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQY---NISMPKTWADFAADQDKLK---- 191
Cdd:cd14748 81 DYI-----DKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldPEKPPKTWDELEEAAKKLKdkgg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 192 G*DINAIELDQSYDVA-LEGMAYGAGSQLITPKL-KANLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVPFANGKAVF 269
Cdd:cd14748 156 KTGRYGFALPPGDGGWtFQALLWQNGGDLLDEDGgKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 270 GIGSSATVPVLLQQAPKsLDWGTAVIPEYEG-KRSNPLNGNYNVLFKGASKaQQAGAWAFQKFLLKSENAAQWAKDSGYV 348
Cdd:cd14748 236 TINGTWSLAGIRDKGAG-FEYGVAPLPAGKGkKGATPAGGASLVIPKGSSK-KKEAAWEFIKFLTSPENQAKWAKATGYL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 913907246 349 PVTKSASNSAtfKAYLEKNPQYKAAVSAVPQSFAS-TVFAGYTDYRNDLMSTVDSTLTKNVSGETAFNKLQKQ 420
Cdd:cd14748 314 PVRKSAAEDP--EEFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-341 |
1.83e-62 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 205.66 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 1 MKKTsfwrLLGFMGAILLLLTACGKQGSAAKSSSSaPVKITYWHrMTGTYDKSLNKLITKFNNSQKKYKVVATSQGsYNA 80
Cdd:COG1653 1 MRRL----ALALAAALALALAACGGGGSGAAAAAG-KVTLTVWH-TGGGEAAALEALIKEFEAEHPGIKVEVESVP-YDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 81 LQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFDSEMlngsnKLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTS 160
Cdd:COG1653 74 YRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLL-----DDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 161 VLFYNKKLMSQYNISMPKTWADFAADQDKLKG*D-INAIELDQSYDVALEGMAYGAGSQLITPKLKANLNAPKTLAAVNQ 239
Cdd:COG1653 149 GLYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKDgVYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 240 ILDLRKSGALKTAGEDQYFS---VPFANGKAVFGIGSSATVPVLLQQAPkSLDWGTAVIPEYEG--KRSNPLNGNYNVLF 314
Cdd:COG1653 229 LKDLVKDGYVPPGALGTDWDdarAAFASGKAAMMINGSWALGALKDAAP-DFDVGVAPLPGGPGgkKPASVLGGSGLAIP 307
|
330 340
....*....|....*....|....*..
gi 913907246 315 KGASKaqQAGAWAFQKFLLKSENAAQW 341
Cdd:COG1653 308 KGSKN--PEAAWKFLKFLTSPEAQAKW 332
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
56-363 |
1.95e-32 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 124.06 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 56 KLITKFNnSQKKYKVVATSQGsYNALQQKIMAAGKSKTLPT--MAQSPYTNIGDYVKNQLLLPFDsemlngsnKLSNrql 133
Cdd:pfam13416 1 ALAKAFE-KKTGVTVEVEPQA-SNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLS--------DVDN--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 134 KDIYPSFLAAGKYDGKYYGLPFSVSTS-VLFYNKKLMSQyNISMPKTWADFAADQDKLKG*diNAIELDQSYDVALEGMa 212
Cdd:pfam13416 68 LDDLPDALDAAGYDGKLYGVPYAASTPtVLYYNKDLLKK-AGEDPKTWDELLAAAAKLKG---KTGLTDPATGWLLWAL- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 213 yGAGSQLITPKLKANLNAPKTLAAVNQILDlrksgALKTAGEDQYFSVPFANGKAVFGIGSSATVPVLLQQAPKsldWGT 292
Cdd:pfam13416 143 -LADGVDLTDDGKGVEALDEALAYLKKLKD-----NGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKK---LGA 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 913907246 293 AVIPEyegkrSNPLNGNYNVLFKGASKAQQAgAWAFQKFLLKSENAAQWAKDSGYVPVTKSASNSATFKAY 363
Cdd:pfam13416 214 VVPKD-----GSFLGGKGLVVPAGAKDPRLA-ALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKAD 278
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
40-368 |
8.52e-25 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 105.65 E-value: 8.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 40 ITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQGSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFDS 119
Cdd:PRK10974 28 IPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPVYD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 120 EMLNGSNKLSNRQLKDIYPSFLAAGKyDGKYYGLPFSVSTSVLFYNKKLMSQYNI---SMPKTWADFAADQDKLKG*DIN 196
Cdd:PRK10974 108 VFKDAGIPFDESQFVPTVAGYYSDAK-TGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKLRAAGMK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 197 A---------IELD-----QSYDVALEGMAYGAGSQLITpklkanLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVPF 262
Cdd:PRK10974 187 CgyasgwqgwIQLEnfsawHGLPFASKNNGFDGTDAVLE------FNKPEQVKHIALLEEMNKKGDFTYVGRKDESTEKF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 263 ANGKAVFGIGSSATVPVLLQQApkSLDWGTAVIPEYEGKRSNPLN----GNYNVLFKGASKAQQAGAWAFQKFLLKSENA 338
Cdd:PRK10974 261 YNGDCAITTASSGSLANIRKYA--KFNYGVGMMPYDADVKGAPQNaiigGASLWVMQGKDKETYKGVAKFLDFLAKPENA 338
|
330 340 350
....*....|....*....|....*....|
gi 913907246 339 AQWAKDSGYVPVTKSASNSATFKAYLEKNP 368
Cdd:PRK10974 339 AEWHQKTGYLPITTAAYDLTREQGFYEKNP 368
|
|
| bind_CPR_0540 |
TIGR03850 |
carbohydrate ABC transporter substrate-binding protein, CPR_0540 family; Members of this ... |
108-423 |
1.29e-07 |
|
carbohydrate ABC transporter substrate-binding protein, CPR_0540 family; Members of this protein are the substrate-binding protein of a predicted carbohydrate transporter operon, together with permease subunits of ABC transporter homology families. This substrate-binding protein frequently co-occurs in genomes with a family of disaccharide phosphorylases, TIGR02336, suggesting that the molecule transported will include beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine and related carbohydrates. Members of this family are sporadically strain by strain, often in species with a human host association, including Propionibacterium acnes and Clostridium perfringens, and Bacillus cereus. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274815 [Multi-domain] Cd Length: 437 Bit Score: 53.54 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 108 YVKNQLLLPFdSEMLNGSNKLSNRQLKD-IYPSFLAAGK---Y-DGKYYGLPFSVSTSVLFYNKKLMSQYNISMPKTWAD 182
Cdd:TIGR03850 105 LIKDKALADL-TDVLDMKVPGEDVTVKDkILPGFVGSSAtnpYgDGKTYLAPMFYSPTGLFYNKTLFEEKGWEVPTTWDE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 183 FAADQDKLKG*DINAIELDQS--YDVALEGMAYGA-GSQLITPKLKANLNAPKTlAAVNQILDLrkSGALKTAGEDQyfS 259
Cdd:TIGR03850 184 MFALGDKAKAEGISLFTYPTTgyFDAFFYALLAEAgGDDFFNKAMNYEEGIWDT-EEAKKAFDT--VGKLATYTEPT--T 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 260 VPFAN-------------GKAVFgIGSSATVPVLLQQAPKS--LDWGTAVIPEYEGKRSNPLNGNYNVLFKGASKAQQAG 324
Cdd:TIGR03850 259 VANANnqdftknqqlvldNKALF-MPNGTWVVGEMKDAPRAdgFEWGMTALPAVKEGGDRYSYTFFEQMWIPAAAKNKDL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 325 AWAFQKFLLkSENAAQWAKDSGYVPVTKSASNsatfkaYLEKNPQ-----YKAAVSAVPQSFASTVFAGYTDYRNDLMST 399
Cdd:TIGR03850 338 AKEFIAFLY-SDEAAKIFAKSGAVQPVKGIAD------KLSGENKvfysiYDNGAKAVIGGFAATKAVEGVDMKDTLYGT 410
|
330 340
....*....|....*....|....
gi 913907246 400 VDSTLTKNVSGETAFNKLQKQTDK 423
Cdd:TIGR03850 411 VNSVVSGDKTVEEWQDSVEEASDK 434
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
39-420 |
2.11e-83 |
|
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: 260.69 E-value: 2.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQGSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFD 118
Cdd:cd14748 1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 119 SEMlngsnKLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQY---NISMPKTWADFAADQDKLK---- 191
Cdd:cd14748 81 DYI-----DKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldPEKPPKTWDELEEAAKKLKdkgg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 192 G*DINAIELDQSYDVA-LEGMAYGAGSQLITPKL-KANLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVPFANGKAVF 269
Cdd:cd14748 156 KTGRYGFALPPGDGGWtFQALLWQNGGDLLDEDGgKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 270 GIGSSATVPVLLQQAPKsLDWGTAVIPEYEG-KRSNPLNGNYNVLFKGASKaQQAGAWAFQKFLLKSENAAQWAKDSGYV 348
Cdd:cd14748 236 TINGTWSLAGIRDKGAG-FEYGVAPLPAGKGkKGATPAGGASLVIPKGSSK-KKEAAWEFIKFLTSPENQAKWAKATGYL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 913907246 349 PVTKSASNSAtfKAYLEKNPQYKAAVSAVPQSFAS-TVFAGYTDYRNDLMSTVDSTLTKNVSGETAFNKLQKQ 420
Cdd:cd14748 314 PVRKSAAEDP--EEFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-341 |
1.83e-62 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 205.66 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 1 MKKTsfwrLLGFMGAILLLLTACGKQGSAAKSSSSaPVKITYWHrMTGTYDKSLNKLITKFNNSQKKYKVVATSQGsYNA 80
Cdd:COG1653 1 MRRL----ALALAAALALALAACGGGGSGAAAAAG-KVTLTVWH-TGGGEAAALEALIKEFEAEHPGIKVEVESVP-YDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 81 LQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFDSEMlngsnKLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTS 160
Cdd:COG1653 74 YRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLL-----DDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 161 VLFYNKKLMSQYNISMPKTWADFAADQDKLKG*D-INAIELDQSYDVALEGMAYGAGSQLITPKLKANLNAPKTLAAVNQ 239
Cdd:COG1653 149 GLYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKDgVYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 240 ILDLRKSGALKTAGEDQYFS---VPFANGKAVFGIGSSATVPVLLQQAPkSLDWGTAVIPEYEG--KRSNPLNGNYNVLF 314
Cdd:COG1653 229 LKDLVKDGYVPPGALGTDWDdarAAFASGKAAMMINGSWALGALKDAAP-DFDVGVAPLPGGPGgkKPASVLGGSGLAIP 307
|
330 340
....*....|....*....|....*..
gi 913907246 315 KGASKaqQAGAWAFQKFLLKSENAAQW 341
Cdd:COG1653 308 KGSKN--PEAAWKFLKFLTSPEAQAKW 332
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-427 |
5.64e-50 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 174.37 E-value: 5.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 1 MKKTSFWrLLGFMGAILLLLTACGKQGSAAKSSSS--APVKITYWHrmTGTYDKSLNKLITKFNnSQKKYKVVATsQGSY 78
Cdd:COG2182 1 MKRRLLA-ALALALALALALAACGSGSSSSGSSSAagAGGTLTVWV--DDDEAEALEEAAAAFE-EEPGIKVKVV-EVPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 79 NALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFDsemlngsnkLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVS 158
Cdd:COG2182 76 DDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLD---------DDLADKDDFLPAALDAVTYDGKLYGVPYAVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 159 TSVLFYNKKLMSQyniSMPKTWADFAADQDKLKG*DINAIELDQSYDVALEGMAYGAGSQLITPKL----KANLNAPKTL 234
Cdd:COG2182 147 TLALYYNKDLVKA---EPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGddpkDVGLNSPGAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 235 AAVNQILDLRKSGALKTAGEDQYFSVPFANGKAVFGIGSsatvPVLLQQAPKSL--DWGTAVIPEY-EGKRSNPLNGNYN 311
Cdd:COG2182 224 AALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIING----PWAAADLKKALgiDYGVAPLPTLaGGKPAKPFVGVKG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 312 VLFKGASKAQQAgAWAFQKFLLKSENAAQWAKDSGYVPVTKSASNSATFKAylekNPQYKAAVSAVPQSFASTVFAGYTD 391
Cdd:COG2182 300 FGVSAYSKNKEA-AQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKA----DPLIAAFAEQAEYAVPMPNIPEMGA 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 913907246 392 YRNDLMSTVDSTLTKNVSGETAFNKLQKQTDKILEE 427
Cdd:COG2182 375 VWTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
39-420 |
5.13e-47 |
|
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: 165.66 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSqGSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFD 118
Cdd:cd13585 1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVP-VPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 119 SEMLNGSNKlsnrqlKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQY--NISMPKTWADF--AADQDKLKG*D 194
Cdd:cd13585 80 DYIEKDGLD------DDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAgpGPKPPWTWDELleAAKKLTDKKGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 195 IN--AIELDQSYDVALEGMAYGAGSQLITP-KLKANLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSV--PFANGKAVF 269
Cdd:cd13585 154 QYgfALRGGSGGQTQWYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 270 GIGSSATVPVLLQQAPKsLDWGTAVIPEYE-GKRSNPLNGNYNVLFKGaSKAQQAgAWAFQKFLLKSENAAQWAKDSGYV 348
Cdd:cd13585 234 MIDGPWALGTLKDSKVK-FKWGVAPLPAGPgGKRASVLGGWGLAISKN-SKHPEA-AWKFIKFLTSKENQLKLGGAAGPA 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 913907246 349 PVTKSASNSATFKAYLEKNPQYKAAvsAVPQSFASTVFAGYTDYRNDLMSTVDSTLTKNV--SGETAFNKLQKQ 420
Cdd:cd13585 311 ALAAAAASAAAPDAKPALALAAAAD--ALAAAVPPPVPPPWPEVYPILSEALQEALLGALgkSPEEALKEAAKE 382
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
39-419 |
1.83e-37 |
|
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: 140.21 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKS-LNKLITKFNNSQKKYKVVATSQGsYNALQQKIMAAGKSKTLPTMAQS-PYTNIGDYVKNQLLLP 116
Cdd:cd14749 1 TITYWQYFTGDTKKKyMDELIADFEKENPNIKVKVVVFP-YDNYKTKLKTAVAAGEGPDVFNLwPGGWLAEFVKAGLLLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 117 FDSeMLNgsnklSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNI-SMPKTWADF--AADQDKLKG* 193
Cdd:cd14749 80 LTD-YLD-----PNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGvKPPKTWDELieAAKKDKFKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 194 DINAIEL---DQSYDVALEGMAYGAGSQLITPKL--KANLNAPKTLAAVNQILDLRKSGALKTAGEDQYF--SVP-FANG 265
Cdd:cd14749 154 GQTGFGLllgAQGGHWYFQYLVRQAGGGPLSDDGsgKATFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYddAGQaFAQG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 266 KAVFGIGSSATVPVLLQQAPKsLDWGTAVIPE-YEGKRSNPLNGNYNVLFKGASKAQQAGAWAFQKFLLKSENAAQWAKD 344
Cdd:cd14749 234 KAAMNIGGSWDLGAIKAGEPG-GKIGVFPFPTvGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLED 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 913907246 345 SGYVPVTKSASNSATFKAYLEKNPQYKAAVSAVPQSFASTVFAGYTDYRNDlmsTVDSTLTKNVSGETAFNKLQK 419
Cdd:cd14749 313 VGLLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEYWPAAAQVHKD---AVQKLLTGKIDPEQVVKQAQS 384
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
40-422 |
5.37e-36 |
|
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: 135.97 E-value: 5.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 40 ITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQgSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFDS 119
Cdd:cd14751 2 ITFWHTSSDEEKVLYEKLIPAFEKEYPKIKVKAVRV-PFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 120 EMlngsnklSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNISMPKTWADF---AADQDKLKG*DIN 196
Cdd:cd14751 81 TP-------AFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELvaaAKAIKKKKGRYGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 197 AIELDQSYDVAleGMAYGAGSQLITP-KLKANLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVP--FANGKAVFGI-G 272
Cdd:cd14751 154 YISGDGPYWLL--PFLWSFGGDLTDEkKATGYLNSPESVRALETIVDLYDEGAITPCASGGYPNMQdgFKSGRYAMIVnG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 273 SSATVPVLLQQAPKSLD-WGTAVIPEYEGKRSNPLNGNYNVLFKGaSKAQQAgAWAFQKFLLKSENAAQWAKDSGYVPVT 351
Cdd:cd14751 232 PWAYADILGGKEFKDPDnLGIAPVPAGPGGSGSPVGGEDLVIFKG-SKNKDA-AWKFVKFMSSAEAQALTAAKLGLLPTR 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 913907246 352 KSASNSATfkayLEKNPQYKAAVSAVPQSFASTVFAGYTDYRNDLMSTVDSTLTKNVSGETAFNKLQKQTD 422
Cdd:cd14751 310 TSAYESPE----VANNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
39-425 |
1.37e-32 |
|
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: 127.04 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQGsYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFD 118
Cdd:cd14747 1 TLTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVLP-WGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 119 SEMLNGSnklsnrQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNIS-MPKTWADF--AADQDKLKG*DI 195
Cdd:cd14747 80 PYLEDLG------GDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDeAPKTWDELeaAAKKIKADGPDV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 196 NAIELDQSYDV--ALEGMAYGAGSQLITPKL-KANLNAPKTLAAVNQILDLRKSG---ALKTAGEDQYFSVpFANGKAVF 269
Cdd:cd14747 154 SGFAIPGKNDVwhNALPFVWGAGGDLATKDKwKATLDSPEAVAGLEFYTSLYQKGlspKSTLENSADVEQA-FANGKVAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 270 GIGSSATVPVLLQQAPKSLD-WGTAVIPEYEGKrSNP--LNGNYNVLFKGASKAQqaGAWAFQKFLLKSENAAQWAKDSG 346
Cdd:cd14747 233 IISGPWEIGAIREAGPDLAGkWGVAPLPGGPGG-GSPsfAGGSNLAVFKGSKNKD--LAWKFIEFLSSPENQAAYAKATG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 347 YVPVTKSASNsatfKAYLEKNPQYKAAVSAVPQSFASTVFAGYT----DYRNDLMSTVDstlTKNVSGETAFNKLQKQTD 422
Cdd:cd14747 310 MLPANTSAWD----DPSLANDPLLAVFAEQLKTGKATPATPEWGeieaELVLVLEEVWI---GVGADVEDALDKAAAEIN 382
|
...
gi 913907246 423 KIL 425
Cdd:cd14747 383 EIL 385
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
56-363 |
1.95e-32 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 124.06 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 56 KLITKFNnSQKKYKVVATSQGsYNALQQKIMAAGKSKTLPT--MAQSPYTNIGDYVKNQLLLPFDsemlngsnKLSNrql 133
Cdd:pfam13416 1 ALAKAFE-KKTGVTVEVEPQA-SNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLS--------DVDN--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 134 KDIYPSFLAAGKYDGKYYGLPFSVSTS-VLFYNKKLMSQyNISMPKTWADFAADQDKLKG*diNAIELDQSYDVALEGMa 212
Cdd:pfam13416 68 LDDLPDALDAAGYDGKLYGVPYAASTPtVLYYNKDLLKK-AGEDPKTWDELLAAAAKLKG---KTGLTDPATGWLLWAL- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 213 yGAGSQLITPKLKANLNAPKTLAAVNQILDlrksgALKTAGEDQYFSVPFANGKAVFGIGSSATVPVLLQQAPKsldWGT 292
Cdd:pfam13416 143 -LADGVDLTDDGKGVEALDEALAYLKKLKD-----NGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKK---LGA 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 913907246 293 AVIPEyegkrSNPLNGNYNVLFKGASKAQQAgAWAFQKFLLKSENAAQWAKDSGYVPVTKSASNSATFKAY 363
Cdd:pfam13416 214 VVPKD-----GSFLGGKGLVVPAGAKDPRLA-ALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKAD 278
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
39-361 |
8.32e-29 |
|
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: 115.86 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTgTYDKSLNKLITKFNnSQKKYKVVATSQGSyNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFD 118
Cdd:cd13586 1 TITVWTDED-GELEYLKELAEEFE-KKYGIKVEVVYVDS-GDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 119 SemlngsnklSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQynisMPKTWADF--AADQDKLKG*DIN 196
Cdd:cd13586 78 E---------YLAVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPE----PPKTWEELiaLAKKFNDKAGGKY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 197 AIELDQ--SYDVALEGMAYGA---GSQLITPKlKANLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVP-FANGKAVFG 270
Cdd:cd13586 145 GFAYDQtnPYFSYPFLAAFGGyvfGENGGDPT-DIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADAlFKEGKAAMI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 271 IGSsatvPVLLQQAPKS-LDWGTAVIPEYEG-KRSNPLNGNYNVLFKGASKaQQAGAWAFQKFLLKSENAAQWAKDSGYV 348
Cdd:cd13586 224 ING----PWDLADYKDAgINFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSK-NKEAAVEFAEYLTSDEAQLLLFEKTGRI 298
|
330
....*....|...
gi 913907246 349 PVTKSASNSATFK 361
Cdd:cd13586 299 PALKDALNDAAVK 311
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
39-420 |
7.92e-27 |
|
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: 110.85 E-value: 7.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFN--NSQKKYKVVATsQGSYNALQQKI--MAAGKSKTlPTMAQSPYTNIGDYVKNQLL 114
Cdd:cd14750 1 TITFAAGSDGQEGELLKKAIAAFEkkHPDIKVEIEEL-PASSDDQRQQLvtALAAGSSA-PDVLGLDVIWIPEFAEAGWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 115 LPFDSEmlngsnkLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNISMPKTWADF--AADQDKLKG 192
Cdd:cd14750 79 LPLTEY-------LKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELleAAKKRKAGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 193 *DINAIELD-QSY----DVALEgMAYGAGSQLITPKL-KANLNAPKTLAAVNQILDLRKSG----ALKTAGEDQYFSVpF 262
Cdd:cd14750 152 PGIWGYVFQgKQYeglvCNFLE-LLWSNGGDIFDDDSgKVTVDSPEALEALQFLRDLIGEGispkGVLTYGEEEARAA-F 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 263 ANGKAVFGIGSSATVPVLlqQAPKSL---DWGTAVIPEYEGKRSNPLNGNYNVLFKGASKAQQAgAWAFQKFLLKSENAA 339
Cdd:cd14750 230 QAGKAAFMRNWPYAYALL--QGPESAvagKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEA-AWEFVKFLTSPEVQK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 340 QWAKDSGYVPVTKSASNSAtfkAYLEKNPQYKAAVSAVPQSFASTVFAGYTDYRNDLMSTVDSTLTKNVSGETAFNKLQK 419
Cdd:cd14750 307 RRAINGGLPPTRRALYDDP---EVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQE 383
|
.
gi 913907246 420 Q 420
Cdd:cd14750 384 K 384
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
39-358 |
1.93e-25 |
|
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: 106.73 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQGSyNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFD 118
Cdd:cd13522 1 TITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDT-EARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 119 SEMLNgsnklsnrqLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQyniSMPKTWADFAADQDKLKG*DINAI 198
Cdd:cd13522 80 EYVSK---------SGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAKNVWGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 199 ELDQSYDVALEGMAYGAGSQLITP---KLKANLNAPKTLAAVNQILDLRKSGAL--KTAGEDQYFSVpFANGKAVFGI-G 272
Cdd:cd13522 148 VYNQNEPYFFAAWIGGFGGQVFKAnngKNNPTLDTPGAVEALQFLVDLKSKYKImpPETDYSIADAL-FKAGKAAMIInG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 273 SSATVpvlLQQAPKSLDWGTAVIPEY-EGKRSNPLNGNYNVLFKGASkAQQAGAWAFQKFLLKSENAAQWAKDSGYVPVT 351
Cdd:cd13522 227 PWDLG---DYRQALKINLGVAPLPTFsGTKHAAPFVGGKGFGINKES-QNKAAAVEFVKYLTSYQAQLVLFDDAGDIPAN 302
|
....*..
gi 913907246 352 KSASNSA 358
Cdd:cd13522 303 LQAYESP 309
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
40-368 |
8.52e-25 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 105.65 E-value: 8.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 40 ITYWHRMTGTYDKSLNKLITKFNNSQKKYKVVATSQGSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFDS 119
Cdd:PRK10974 28 IPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPVYD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 120 EMLNGSNKLSNRQLKDIYPSFLAAGKyDGKYYGLPFSVSTSVLFYNKKLMSQYNI---SMPKTWADFAADQDKLKG*DIN 196
Cdd:PRK10974 108 VFKDAGIPFDESQFVPTVAGYYSDAK-TGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKLRAAGMK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 197 A---------IELD-----QSYDVALEGMAYGAGSQLITpklkanLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVPF 262
Cdd:PRK10974 187 CgyasgwqgwIQLEnfsawHGLPFASKNNGFDGTDAVLE------FNKPEQVKHIALLEEMNKKGDFTYVGRKDESTEKF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 263 ANGKAVFGIGSSATVPVLLQQApkSLDWGTAVIPEYEGKRSNPLN----GNYNVLFKGASKAQQAGAWAFQKFLLKSENA 338
Cdd:PRK10974 261 YNGDCAITTASSGSLANIRKYA--KFNYGVGMMPYDADVKGAPQNaiigGASLWVMQGKDKETYKGVAKFLDFLAKPENA 338
|
330 340 350
....*....|....*....|....*....|
gi 913907246 339 AQWAKDSGYVPVTKSASNSATFKAYLEKNP 368
Cdd:PRK10974 339 AEWHQKTGYLPITTAAYDLTREQGFYEKNP 368
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
39-378 |
2.41e-19 |
|
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: 88.97 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 39 KITYWHRMTGTYDKSLNKLITKFNNSQKKYKV-VATSQGSynALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPF 117
Cdd:cd13657 1 TITIWHALTGAEEDALQQIIDEFEAKYPVPNVkVPFEKKP--DLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 118 DsemlngsNKLSNRQLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNISMPKTWADFAADQDKLKG*DINA 197
Cdd:cd13657 79 S-------DYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHTDPAAGSYGLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 198 IELDQSYDVAleGMAYGAGSQLITPK-LKANLNAPKTLAAVNQILDLrKSGALKTAGEDQYFSVPFANGKAVFGIGSsat 276
Cdd:cd13657 152 YQVSDAYFVS--AWIFGFGGYYFDDEtDKPGLDTPETIKGIQFLKDF-SWPYMPSDPSYNTQTSLFNEGKAAMIING--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 277 vPVLLQQAPKSL-DWGTAVIPEYEG-KRSNPLNGNYNVLF-KGASKAQQAGAWAFQKFLLKSENAAQWAKDSGYVPVTKS 353
Cdd:cd13657 226 -PWFIGGIKAAGiDLGVAPLPTVDGtNPPRPYSGVEGIYVtKYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATN 304
|
330 340
....*....|....*....|....*
gi 913907246 354 ASNSATFKAYLEKNPQYKAAVSAVP 378
Cdd:cd13657 305 AYDDAEVAADPVIAAFKAQAEHGVP 329
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
49-339 |
9.51e-17 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 80.15 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 49 TYDKSLNKLITKFNNSQKKYKVVATSQGSyNALQQKIMAAGKSKTLPT-MAQSPYTNIGDYVKNQLLLPFDSEMLNgsnk 127
Cdd:pfam01547 5 TEAAALQALVKEFEKEHPGIKVEVESVGS-GSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVAN---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 128 lsnrqlkdiypsflAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNISMPKTWADFAADQDKLKG*DINAIELDQSY--- 204
Cdd:pfam01547 80 --------------YLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDasg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 205 --DVALEGMAYGAGSQLITPKLKANLNAPKTLAAVN------QILDLRKSGALKTAGEDQYFSVP-FANGKAVFGIGSSA 275
Cdd:pfam01547 146 tlGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYyvdlyaKVLLLKKLKNPGVAGADGREALAlFEQGKAAMGIVGPW 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 913907246 276 TVPVLLQQAPKSL----------DWGTAVIPEYEGKRSNPLNGnynVLFKGAskAQQAGAWAFQKFLLKSENAA 339
Cdd:pfam01547 226 AALAANKVKLKVAfaapapdpkgDVGYAPLPAGKGGKGGGYGL---AIPKGS--KNKEAAKKFLDFLTSPEAQA 294
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
1-354 |
7.26e-14 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 72.25 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 1 MKKTSFwrlLGFMGAILLLLTAcgkqGSAAKSSSSAPVKITYWHrmtGTYDKSLnklITKFnnsQKKY--KVVATSQGSY 78
Cdd:COG0687 1 MSRRSL---LGLAAAALAAALA----GGAPAAAAEGTLNVYNWG---GYIDPDV---LEPF---EKETgiKVVYDTYDSN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 79 NALQQKIMAAGksktlptmaqSPY-------TNIGDYVKNQLLLPFDSEmlngsnKLSNrqLKDIYPSFLAAGKYDGKYY 151
Cdd:COG0687 65 EEMLAKLRAGG----------SGYdvvvpsdYFVARLIKAGLLQPLDKS------KLPN--LANLDPRFKDPPFDPGNVY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 152 GLPFSVSTSVLFYNKKLMSQYnismPKTWADFAadQDKLKG*DINAieLDQSYDVALEGMAYgAGsqlitpkLKANLNAP 231
Cdd:COG0687 127 GVPYTWGTTGIAYNTDKVKEP----PTSWADLW--DPEYKG-KVAL--LDDPREVLGAALLY-LG-------YDPNSTDP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 232 KTLAAVNQILD-LRKSGALKTAGEDQYFSvPFANGKAVFGIGSSATVPVLLQQAPKsLDWgtaVIPEyEGkrsNPLNGNY 310
Cdd:COG0687 190 ADLDAAFELLIeLKPNVRAFWSDGAEYIQ-LLASGEVDLAVGWSGDALALRAEGPP-IAY---VIPK-EG---ALLWFDN 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 913907246 311 NVLFKGASKaqQAGAWAFQKFLLKSENAAQWAKDSGYVPVTKSA 354
Cdd:COG0687 261 MAIPKGAPN--PDLAYAFINFMLSPEVAAALAEYVGYAPPNKAA 302
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
66-372 |
6.67e-11 |
|
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270376 [Multi-domain] Cd Length: 372 Bit Score: 63.66 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 66 KKYKV-VATSQGSYNALQQKIMAAGKSKTLPTMAQSPYTNIGDYVKNQLLLPFdsemlngsnKLSNRQLKDIYPSFLAAG 144
Cdd:cd13658 24 KKTGVkVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPI---------KLSKDKKKGFTDQALKAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 145 KYDGKYYGLPFSVSTSVLFYNKKLMSQynisMPKTWADFAADQDKLKG*DINA----IELDQSYDVALEGMAYGA----- 215
Cdd:cd13658 95 TYDGKLYGLPAAVETLALYYNKDLVKN----APKTFDELEALAKDLTKEKGKQygflADATNFYYSYGLLAGNGGyifkk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 216 -GSQLITPKLkaNLNAPKTLAAVNQILDLRKSGALKTAGEDQYFSVPFANGKAVFGIGSsatvPVLLQ--QAPKsLDWGT 292
Cdd:cd13658 171 nGSDLDINDI--GLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDG----PWAIQeyQEAG-VNYGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 293 AVIPEYE-GKRSNPLNGnynvlFKG--ASKAQQAGAWA--FQKFLLKSENAAQWAKDSGYVPVTKSASNSATFKayleKN 367
Cdd:cd13658 244 APLPTLPnGKPMAPFLG-----VKGwyLSAYSKHKEWAqkFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEIK----NN 314
|
....*
gi 913907246 368 PQYKA 372
Cdd:cd13658 315 PLTSA 319
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
83-372 |
5.33e-08 |
|
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. 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: 270374 [Multi-domain] Cd Length: 364 Bit Score: 54.52 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 83 QKIMAAGKSktlPTMAQSPYTNIGDYVKNQLLLPFDSEmlngsnKLSNRQLkdiYPSFLAAGKYDGKYYGLPFSVSTSVL 162
Cdd:cd13656 44 PQVAATGDG---PDIIFWAHDRFGGYAQSGLLAEITPD------KAFQDKL---YPFTWDAVRYNGKLIAYPIAVEALSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 163 FYNKKLMSqyniSMPKTWADFAADQDKLKG*DINAIELD-QSYDVALEGMAYGAGSQLitpKLKANLNAPK--------T 233
Cdd:cd13656 112 IYNKDLLP----NPPKTWEEIPALDKELKAKGKSALMFNlQEPYFTWPLIAADGGYAF---KYENGKYDIKdvgvdnagA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 234 LAAVNQILDLRKSGALKTAGEDQYFSVPFANGKAVFGIGSsatvPVLLQQAPKS-LDWGTAVIPEYEGKRSNPLNGNYNV 312
Cdd:cd13656 185 KAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTING----PWAWSNIDTSkVNYGVTVLPTFKGQPSKPFVGVLSA 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 313 LFKGASKAQQAGAWAFQKFLLKSENAAQWAKDsgyVPVTKSASNSatFKAYLEKNPQYKA 372
Cdd:cd13656 261 GINAASPNKELAKEFLENYLLTDEGLEAVNKD---KPLGAVALKS--YEEELAKDPRIAA 315
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
56-354 |
8.32e-08 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. 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: 270308 [Multi-domain] Cd Length: 315 Bit Score: 53.39 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 56 KLITKFnnsQKKY--KVVATSQGSYNALQQKIMAAGKSK---TLPTMAQspytnIGDYVKNQLLLPFDSEmlngsnKLSN 130
Cdd:cd13590 14 EVLKAF---EKETgvKVNYDTYDSNEEMLAKLRAGGGSGydlVVPSDYM-----VERLIKQGLLEPLDHS------KLPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 131 rqLKDIYPSFLAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYnismPKTWADFAaDQDKLKG*diNAIELDQSYDV---A 207
Cdd:cd13590 80 --LKNLDPQFLNPPYDPGNRYSVPYQWGTTGIAYNKDKVKEP----PTSWDLDL-WDPALKG---RIAMLDDAREVlgaA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 208 LEGMAYGAGSqlITPklkANLNApktlaAVNQILDLRKSgaLKTAGEDQYFSvPFANGKAVFGIGSSATVPVLLQQAPKs 287
Cdd:cd13590 150 LLALGYSPNT--TDP---AELAA-----AAELLIKQKPN--VRAFDSDSYVQ-DLASGEIWLAQAWSGDALQANRENPN- 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 913907246 288 LDWgtaVIPEyEGkrsNPLNGNYNVLFKGAskAQQAGAWAFQKFLLKSENAAQWAKDSGYVPVTKSA 354
Cdd:cd13590 216 LKF---VIPK-EG---GLLWVDNMAIPKGA--PNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAA 273
|
|
| bind_CPR_0540 |
TIGR03850 |
carbohydrate ABC transporter substrate-binding protein, CPR_0540 family; Members of this ... |
108-423 |
1.29e-07 |
|
carbohydrate ABC transporter substrate-binding protein, CPR_0540 family; Members of this protein are the substrate-binding protein of a predicted carbohydrate transporter operon, together with permease subunits of ABC transporter homology families. This substrate-binding protein frequently co-occurs in genomes with a family of disaccharide phosphorylases, TIGR02336, suggesting that the molecule transported will include beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine and related carbohydrates. Members of this family are sporadically strain by strain, often in species with a human host association, including Propionibacterium acnes and Clostridium perfringens, and Bacillus cereus. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274815 [Multi-domain] Cd Length: 437 Bit Score: 53.54 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 108 YVKNQLLLPFdSEMLNGSNKLSNRQLKD-IYPSFLAAGK---Y-DGKYYGLPFSVSTSVLFYNKKLMSQYNISMPKTWAD 182
Cdd:TIGR03850 105 LIKDKALADL-TDVLDMKVPGEDVTVKDkILPGFVGSSAtnpYgDGKTYLAPMFYSPTGLFYNKTLFEEKGWEVPTTWDE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 183 FAADQDKLKG*DINAIELDQS--YDVALEGMAYGA-GSQLITPKLKANLNAPKTlAAVNQILDLrkSGALKTAGEDQyfS 259
Cdd:TIGR03850 184 MFALGDKAKAEGISLFTYPTTgyFDAFFYALLAEAgGDDFFNKAMNYEEGIWDT-EEAKKAFDT--VGKLATYTEPT--T 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 260 VPFAN-------------GKAVFgIGSSATVPVLLQQAPKS--LDWGTAVIPEYEGKRSNPLNGNYNVLFKGASKAQQAG 324
Cdd:TIGR03850 259 VANANnqdftknqqlvldNKALF-MPNGTWVVGEMKDAPRAdgFEWGMTALPAVKEGGDRYSYTFFEQMWIPAAAKNKDL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 325 AWAFQKFLLkSENAAQWAKDSGYVPVTKSASNsatfkaYLEKNPQ-----YKAAVSAVPQSFASTVFAGYTDYRNDLMST 399
Cdd:TIGR03850 338 AKEFIAFLY-SDEAAKIFAKSGAVQPVKGIAD------KLSGENKvfysiYDNGAKAVIGGFAATKAVEGVDMKDTLYGT 410
|
330 340
....*....|....*....|....
gi 913907246 400 VDSTLTKNVSGETAFNKLQKQTDK 423
Cdd:TIGR03850 411 VNSVVSGDKTVEEWQDSVEEASDK 434
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
143-372 |
1.03e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 50.40 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 143 AGKYDGKYYGLPFSVSTSVLFYNKKLMSqyniSMPKTWADFAADQDKLKG*DINAIE--LDQSY-----DVALEGMAYGA 215
Cdd:PRK09474 122 AVRYNGKLIGYPIAVEALSLIYNKDLVP----TPPKTWEEIPALDKELKAKGKSAIMwnLQEPYftwplIAADGGYAFKF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 216 GSQLITPKlKANLNAPKTLAAVNQILDLRKSGALkTAGEDqyFSVpfanGKAVFGIGSSATV---PVLLQQAPKS-LDWG 291
Cdd:PRK09474 198 ENGGYDVK-DVGVNNAGAKAGLQFLVDLVKNKHM-NADTD--YSI----AEAAFNKGETAMTingPWAWSNIDKSgINYG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 292 TAVIPEYEGKRSNPLNGNYNVLFKGASKAQQAGAWAFQKFLLKSENAAQWAKDsgyVPVTKSASNSatFKAYLEKNPQYK 371
Cdd:PRK09474 270 VTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKD---KPLGAVALKS--FQEELAKDPRIA 344
|
.
gi 913907246 372 A 372
Cdd:PRK09474 345 A 345
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
142-362 |
1.50e-05 |
|
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270373 [Multi-domain] Cd Length: 363 Bit Score: 46.95 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 142 AAGKYDGKYYGLPFSVSTSVLFYNKKLMSQYNIsmpKTWADFAADQDKLKG*diNAIELDQSYdvALEGMAYGAGSQLI- 220
Cdd:cd13655 94 DAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDV---KSLDTMLAKAPDAKGK--VSFDLSNSW--YLYAFFFGAGCKLFg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 221 ---TPKLKANLNAPKTLAAVNQILDLRKSGALkTAGEDQYFSVPFANGKAVFGIgSSATVPVLLQQAPKSlDWGTAVIPE 297
Cdd:cd13655 167 nngGDTAGCDFNNEKGVAVTNYLVDLVANPKF-VNDADGDAISGLKDGTLGAGV-SGPWDAANLKKALGD-NYAVAKLPT 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 298 YE--GKRSnPLNGNYNVLFKG---ASKAQQAgAWAFQKFLLKSENAAQWAKDSGYVPVTKSASNSATFKA 362
Cdd:cd13655 244 YTlgGKDV-QMKSFAGYKAIGvnsNTKNPEA-AMALADYLTNEESQLTRFEKRGIGPTNKEAAESDAVKA 311
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
108-354 |
3.15e-05 |
|
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270306 [Multi-domain] Cd Length: 279 Bit Score: 45.36 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 108 YVKNQLLLPFDSemlngsNKLSNrqLKDIYPSF--LAAGKYDGKYYGLPFSVSTSVLFYNKKLMSQynisMPKTWADFAA 185
Cdd:cd13588 62 LIAAGLVQPIDT------SKIPN--YANIDPRLrnLPWLTVDGKVYGVPYDWGANGLAYNTKKVKT----PPTSWLALLW 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 186 DQdKLKG*dinaielDQSYDVALEGMAYGAgsqLITPKLKANLNAPKTLAAVNQIldLRKSGAL-----KTAGEDQYFsv 260
Cdd:cd13588 130 DP-KYKGR-------VAARDDPIDAIADAA---LYLGQDPPFNLTDEQLDAVKAK--LREQRPLvrkywSDGAELVQL-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 261 pFANGKAVFGIGSSATVpVLLQQA--PKSLdwgtaVIPEyEGkrsnpLNG--NYNVLFKGAskAQQAGAWAFQKFLLKSE 336
Cdd:cd13588 195 -FANGEVVAATAWSGQV-NALQKAgkPVAY-----VIPK-EG-----ATGwvDTWMILKDA--KNPDCAYKWLNYMLSPK 259
|
250
....*....|....*...
gi 913907246 337 NAAQWAKDSGYVPVTKSA 354
Cdd:cd13588 260 VQAAVAEWTGYAPSNPEA 277
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
57-363 |
3.67e-05 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 45.31 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 57 LITKFnnsQKKYKV-VATSQGSYNALQQKIMAAGKSktlPT----MAQSPyTNIGDYVKNQLLLPFDSEmlngsnklsnr 131
Cdd:COG1840 1 LLEAF---EKKTGIkVNVVRGGSGELLARLKAEGGN---PPadvvWSGDA-DALEQLANEGLLQPYKSP----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 132 QLKDIYPSFLAAgkyDGKYYGlpFSVSTSVLFYNKKLMSQYNIsmPKTWADFAadQDKLKG*dInaieldQSYDVALEGM 211
Cdd:COG1840 63 ELDAIPAEFRDP---DGYWFG--FSVRARVIVYNTDLLKELGV--PKSWEDLL--DPEYKGK-I------AMADPSSSGT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 212 AYGAGSQLItpklkANLNAPKTLAAVNQildLRKSGALKTAGE-DQYFSVpfANGKAVFGIGSSATVpvlLQQAPKSLDW 290
Cdd:COG1840 127 GYLLVAALL-----QAFGEEKGWEWLKG---LAANGARVTGSSsAVAKAV--ASGEVAIGIVNSYYA---LRAKAKGAPV 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 913907246 291 GTaVIPEyEGkrsNPLNGNYNVLFKGASKAQQAGawAFQKFLLKSENAAQWAKDSGYVPVTKSASNSATFKAY 363
Cdd:COG1840 194 EV-VFPE-DG---TLVNPSGAAILKGAPNPEAAK--LFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGLPPL 259
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
37-185 |
3.76e-05 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 45.78 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 37 PVKIT--YWHRMTGTYDKSLNKLITKFN-NSQKKYKVVATSQGSYNalqQKIMAAGKSKTLPTMAQSPYTNIG-DYVKNQ 112
Cdd:cd13580 2 PVTITivANLGGNPKPDPDDNPYTKYLEeKTNIDVKVKWVPDSSYD---EKLNLALASGDLPDIVVVNDPQLSiTLVKQG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913907246 113 LLLPFDsEMLN--GSNklsnrqLKDIYPSF-LAAGKYDGKYYGLPFSVSTS---VLFYNKKLMSQYNISMPKTWADFAA 185
Cdd:cd13580 79 ALWDLT-DYLDkyYPN------LKKIIEQEgWDSASVDGKIYGIPRKRPLIgrnGLWIRKDWLDKLGLEVPKTLDELYE 150
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
105-367 |
5.70e-03 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 38.11 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 105 IGDYVKNQLLLPFDSEML-NGSNKLSNRQLKDIypsflaagkyDGKYYglPFSVSTSVLFYNKKLMSQYNIsmPKTWADF 183
Cdd:pfam13343 20 LEKFIEEGLFQPLDSANLpNVPKDFDDEGLRDP----------DGYYT--PYGVGPLVIAYNKERLGGRPV--PRSWADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 184 AAD--QDKLKg*dINAIELDQSYDVALEGMAYGAGSQLITPKLKAnlnapktLAAVNQILDLRKSGALKTAGEDQYFSVP 261
Cdd:pfam13343 86 LDPeyKGKVA---LPGPNVGDLFNALLLALYKDFGEDGVRKLARN-------LKANLHPAQMVKAAGRLESGEPAVYLMP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 262 FANGKAVFGIGSSATVPVllqqaPKSldwGTAVIPEYEGKRsnplngnynvlfkgasKAQQAGAWAFQKFLLKSENAAQW 341
Cdd:pfam13343 156 YFFADILPRKKKNVEVVW-----PED---GALVSPIFMLVK----------------KGKKELADPLIDFLLSPEVQAIL 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 913907246 342 AKDSGYVPVT------KSASNSATFK----AYLEKN 367
Cdd:pfam13343 212 AKAGLVFPVVlnpavdNPLPEGAPFKwlgwDYIRKN 247
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
104-191 |
5.71e-03 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 38.88 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913907246 104 NIGDYVKnqlllpfdsEMLNGSNKLSNRQLKDIYPSflaAGKYDGKYYGLP----FSVSTSVLFYNKKLMSQYNISMPKT 179
Cdd:cd13583 80 PISDYLD---------YMPNYKKYVEKWGLGKELAT---GRQSDGKYYSLPglheDPGVQYSFLYRKDIFEKAGIKIPTT 147
|
90
....*....|..
gi 913907246 180 WADFAADQDKLK 191
Cdd:cd13583 148 WDEFYAALKKLK 159
|
|
| |
