|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
40-413 |
3.32e-175 |
|
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: 493.92 E-value: 3.32e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 40 LTVSVDAGYK-DYVNKIKGDFEKDNDVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVKLGN- 117
Cdd:cd13658 2 LTVWVDEDKKmAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSKd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 118 -KDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKAPATFKDLETLSKDsrfaFTSEKGKNTGFLAKWTDFYFSY 196
Cdd:cd13658 82 kKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKD----LTKEKGKQYGFLADATNFYYSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 197 GLLAGYGGYVFGDEGT--NPKDIGLNNKGSVEGITYATKWFQD-VWPKGMQDnksadDFIQDQFVKGKAAAILGGPWSAA 273
Cdd:cd13658 158 GLLAGNGGYIFKKNGSdlDINDIGLNSPGAVKAVKFLKKWYTEgYLPKGMTG-----DVIQGLFKEGKAAAVIDGPWAIQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 274 NYKEAKINYGVAKIPTLNNGKEYSPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDTAKSK 353
Cdd:cd13658 233 EYQEAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEIK 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 354 NDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVIEDNV 413
Cdd:cd13658 313 NNPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIKENI 372
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-415 |
4.49e-146 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 421.28 E-value: 4.49e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 1 MKRfKKVGIVSAVLVMALSLAACGGGKDTSKSGSSDEK--TLTVSVDAGYKDYVNKIKGDFEKDNDVKVKVVEKDMFETL 78
Cdd:COG2182 1 MKR-RLLAALALALALALALAACGSGSSSSGSSSAAGAggTLTVWVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 79 EALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVKLG--NKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDK 156
Cdd:COG2182 80 EKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDlaDKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 157 -APATFKDLETLSKDSRfaftseKGKNTGFLAKWTDFYFSYGLLAGYGGYVFGDEGTNPKDIGLNNKGSVEGITYATKWF 235
Cdd:COG2182 160 ePPKTWDELIAAAKKLT------AAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGDDPKDVGLNSPGAVAALEYLKDLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 236 QDvwpkGMQDNKSADDFIQDQFVKGKAAAILGGPWSAANYKEA-KINYGVAKIPTLNNGKEYSPFAGGKGWVVSNYSKNK 314
Cdd:COG2182 234 KD----GVLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 315 DVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDTAKSKNDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASG 394
Cdd:COG2182 310 EAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASG 389
|
410 420
....*....|....*....|.
gi 820769411 395 SKTPQQSADDAVKVIEDNVTQ 415
Cdd:COG2182 390 KADPAEALDAAQKQIEAAIAQ 410
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
39-409 |
6.80e-137 |
|
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: 396.28 E-value: 6.80e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTVSVDAG-YKDYVNKIKGDFEKDNDVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVK--L 115
Cdd:cd13586 1 TITVWTDEDgELEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPeyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 116 GNKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKAPATFKDLETLSKDsrfaFTSEKGKNTGFLAKWTDFYFS 195
Cdd:cd13586 81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKK----FNDKAGGKYGFAYDQTNPYFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 196 YGLLAGYGGYVFGDEGTNPKDIGLNNKGSVEGITYATKWFQD--VWPKGMQDnksadDFIQDQFVKGKAAAILGGPWSAA 273
Cdd:cd13586 157 YPFLAAFGGYVFGENGGDPTDIGLNNEGAVKGLKFIKDLKKKykVLPPDLDY-----DIADALFKEGKAAMIINGPWDLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 274 NYKEAKINYGVAKIPTLNNGKEYSPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDTAKSK 353
Cdd:cd13586 232 DYKDAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDALNDAAVK 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 820769411 354 NDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVI 409
Cdd:cd13586 312 NDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
45-409 |
2.34e-66 |
|
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: 215.70 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 45 DAGYKDYVNKIKGDFEKDNDV-KVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVKLGNKDDYDE 123
Cdd:cd13657 9 TGAEEDALQQIIDEFEAKYPVpNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISDYLSEDDFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 124 K----DQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKAPATFKDLETLSKDSRFAFTSekgkNTGFLAKWTDFYFSYGLL 199
Cdd:cd13657 89 NylptAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHTDPAAG----SYGLAYQVSDAYFVSAWI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 200 AGYGGYVFGDEGTNPkdiGLNNKGSVEGITYATKWFQDVWPKgmqdnKSADDFIQDQFVKGKAAAILGGPWSAANYKEAK 279
Cdd:cd13657 165 FGFGGYYFDDETDKP---GLDTPETIKGIQFLKDFSWPYMPS-----DPSYNTQTSLFNEGKAAMIINGPWFIGGIKAAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 280 INYGVAKIPTLNNGKEYSPFAGGKGWVVSNY--SKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDTAKSKNDEL 357
Cdd:cd13657 237 IDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYaeRKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVAADPV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 820769411 358 TNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVI 409
Cdd:cd13657 317 IAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
39-409 |
1.32e-63 |
|
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: 208.81 E-value: 1.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTVSVDAGYKDYVNKIKGDFEKDN-DVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVK--L 115
Cdd:cd13522 3 TVWHQYDTGENQAVNELIAKFEKAYpGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDeyV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 116 GNKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLL-DKAPATFKDLETLSKDSrfaftSEKGKNtGFLAKWTDFYF 194
Cdd:cd13522 83 SKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVpKNPPKTWQELIALAQGL-----KAKNVW-GLVYNQNEPYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 195 SYGLLAGYGGYVFGDEGtNPKDIGLNNKGSVEGITYATKW-FQDVWpkgmqDNKSADDFIQDQ-FVKGKAAAILGGPWSA 272
Cdd:cd13522 157 FAAWIGGFGGQVFKANN-GKNNPTLDTPGAVEALQFLVDLkSKYKI-----MPPETDYSIADAlFKAGKAAMIINGPWDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 273 ANYKEA-KINYGVAKIPTLNNGKEYSPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDTAK 351
Cdd:cd13522 231 GDYRQAlKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAYESPA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 820769411 352 SKNDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVI 409
Cdd:cd13522 311 VQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-365 |
1.30e-58 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 195.65 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 1 MKRFkkvgIVSAVLVMALSLAACGGGKDTSkSGSSDEKTLTV-SVDAGYKDYVNKIKGDFEKDN-DVKVKVVEKDMFETL 78
Cdd:COG1653 1 MRRL----ALALAAALALALAACGGGGSGA-AAAAGKVTLTVwHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYDDYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 79 EALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEV------KLGNKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKD 152
Cdd:COG1653 76 TKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLddllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 153 LLDKA----PATFKDLETLSKdsrfAFTSEKGKnTGFLAKWTDFYFSYGLLAGYGGYVFGDEGTnpkdIGLNNKGSVEGI 228
Cdd:COG1653 156 LFEKAgldpPKTWDELLAAAK----KLKAKDGV-YGFALGGKDGAAWLDLLLSAGGDLYDEDGK----PAFDSPEAVEAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 229 TYATKWFQDVW-PKGMQDNKSADdfIQDQFVKGKAAAILGGPWSAANYKEA--KINYGVAKIPTLNNGKEYSPFAGGKGW 305
Cdd:COG1653 227 EFLKDLVKDGYvPPGALGTDWDD--ARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPGGKKPASVLGGSGL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 306 VVSNYSKNKDVAQKWLDYVTNQKNQETlYDMTNEVPANLKARDTAKSKNDELTNAVIEQY 365
Cdd:COG1653 305 AIPKGSKNPEAAWKFLKFLTSPEAQAK-WDALQAVLLGQKTPEEALDAAQAAANAALARA 363
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-409 |
6.37e-58 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 194.46 E-value: 6.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 1 MKRFKKVGIVSAVLVMALSLAAcgggkdtSKSGSSDEKTLTVSV--DAGYKDyVNKIKGDFEKDNDVKVKVVEKDMFEtl 78
Cdd:PRK09474 1 MKIKKGLRTLALSALATLMFSA-------SALAKIEEGKLVIWIngDKGYNG-LAEVGKKFEKDTGIKVTVEHPDKLE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 79 EALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVKLGN--KDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDK 156
Cdd:PRK09474 71 EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKafKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 157 APATFKDLETLSKDSRfaftsEKGKNtGFLAKWTDFYFSYGLLAGYGGYVFG--DEGTNPKDIGLNNKGSVEGITYATKW 234
Cdd:PRK09474 151 PPKTWEEIPALDKELK-----AKGKS-AIMWNLQEPYFTWPLIAADGGYAFKfeNGGYDVKDVGVNNAGAKAGLQFLVDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 235 F-QDVWPKGMqDNKSADDfiqdQFVKGKAAAILGGPWSAANYKEAKINYGVAKIPTLnNGKEYSPFAGGKGWVVSNYSKN 313
Cdd:PRK09474 225 VkNKHMNADT-DYSIAEA----AFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTF-NGKPSKPFVGVLSAGINAASPN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 314 KDVAQKWL-DYVTnqkNQETLYDMTNEVP---ANLKARDTAKSKnDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMF 389
Cdd:PRK09474 299 KELAKEFLeNYLL---TDEGLETVNKDKPlgaVALKSFQEELAK-DPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAII 374
|
410 420
....*....|....*....|
gi 820769411 390 DAASGSKTPQQSADDAVKVI 409
Cdd:PRK09474 375 NATSGRQTVDAALDDAAKRI 394
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
45-405 |
8.89e-52 |
|
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: 177.79 E-value: 8.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 45 DAGYKDyVNKIKGDFEKDNDVKVKVVEKDMFEtlEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVKLGN--KDDYD 122
Cdd:cd13656 10 DKGYNG-LAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKafQDKLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 123 EKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKAPATFKDLETLSKDsrfafTSEKGKnTGFLAKWTDFYFSYGLLAGY 202
Cdd:cd13656 87 PFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKE-----LKAKGK-SALMFNLQEPYFTWPLIAAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 203 GGYVFG--DEGTNPKDIGLNNKGSVEGITYATkwfqDVWPKGMQDNKSADDFIQDQFVKGKAAAILGGPWSAANYKEAKI 280
Cdd:cd13656 161 GGYAFKyeNGKYDIKDVGVDNAGAKAGLTFLV----DLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 281 NYGVAKIPTLNnGKEYSPFAGGKGWVVSNYSKNKDVAQKWLD-YVTNQKNQETL-YDMTNEVPANlKARDTAKSKnDELT 358
Cdd:cd13656 237 NYGVTVLPTFK-GQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVnKDKPLGAVAL-KSYEEELAK-DPRI 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 820769411 359 NAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDA 405
Cdd:cd13656 314 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 360
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
39-404 |
1.21e-50 |
|
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: 174.46 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTVSVDAGYKDYVNKIKGDFEKDN-DVKVKVvekdmfeTLEALPlDGPAGT--------APDVMMSAFDRIGSLGQQGH 109
Cdd:cd13655 1 TLTVWGPQEDQEWLKEMVDAFKEKHpEWKITI-------TIGVVG-EADAKDevlkdpsaAADVFAFANDQLGELVDAGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 110 LAEVKLGNKDDYDEKDQK----QVTIDDKIYGAPAIIETLVLYYNKDLLDKApaTFKDLETLskdsrFAFTSEKGKNTGF 185
Cdd:cd13655 73 IYPLTGSAVDKIKNTNSEatvdAVTYNGKLYGYPFTANTWFMYYDKSKLTED--DVKSLDTM-----LAKAPDAKGKVSF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 186 laKWTDFYFSYGLLAGYGGYVFGDEGTNPKDIGLNNKGSVEgityATKWFQDVW--PKGMQDNKsaDDFIQdQFVKGKAA 263
Cdd:cd13655 146 --DLSNSWYLYAFFFGAGCKLFGNNGGDTAGCDFNNEKGVA----VTNYLVDLVanPKFVNDAD--GDAIS-GLKDGTLG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 264 AILGGPWSAANYKEA-KINYGVAKIPTLN-NGKEY--SPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNE 339
Cdd:cd13655 217 AGVSGPWDAANLKKAlGDNYAVAKLPTYTlGGKDVqmKSFAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGI 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820769411 340 VPANLKARDTAKSKNDELTNAVIEQYKNAQ-PMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADD 404
Cdd:cd13655 297 GPTNKEAAESDAVKADPAAKALIAQSNEASvVQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQK 362
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
39-413 |
6.56e-49 |
|
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: 170.66 E-value: 6.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTVSV--DAGYKDYVNKIKGDFEKDN-DVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEV-- 113
Cdd:cd13585 1 TLTFWDwgQPAETAALKKLIDAFEKENpGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLdd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 114 ---KLGNKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKA------PATFKDLETLSKdsrfAFTSEKGKNTG 184
Cdd:cd13585 81 yieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAgpgpkpPWTWDELLEAAK----KLTDKKGGQYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 185 FLA--KWTDFYFSYGLLAGYGGYVFGDEGTNPkdiGLNNKGSVEGITYATKWFQDVWPKGMQDNKSADdfIQDQFVKGKA 262
Cdd:cd13585 157 FALrgGSGGQTQWYPFLWSNGGDLLDEDDGKA---TLNSPEAVEALQFYVDLYKDGVAPSSATTGGDE--AVDLFASGKV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 263 AAILGGPWSAANYKEAKI--NYGVAKIPTLNNGKEYSpFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEV 340
Cdd:cd13585 232 AMMIDGPWALGTLKDSKVkfKWGVAPLPAGPGGKRAS-VLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPA 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820769411 341 PANLKARDTAKSKNDELTNAVIEQYKNAQPMPNIPEMSEV-WTGAENLMFDAASGSKTpQQSADDAVKVIEDNV 413
Cdd:cd13585 311 ALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPeVYPILSEALQEALLGAL-GKSPEEALKEAAKEI 383
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
39-410 |
6.98e-46 |
|
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: 162.48 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTV--SVDAGYKDYVNKIKGDFEKDN-DVKVKVVEKDMFETLEALPLDGPAGTAPDVM------MSAFdrigslGQQGH 109
Cdd:cd14747 1 TLTVwaMGNSAEAELLKELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGPDVVqlgntwVAEF------AAMGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 110 LAEV-----KLGNKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKA-----PATFKDLETLSKdsrfAFTSEK 179
Cdd:cd14747 75 LEDLtpyleDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAggdeaPKTWDELEAAAK----KIKADG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 180 GKNTGFL--AKWTDFYFSYGLLAGYGGYVFGDEGTNPKdigLNNKGSVEGITYATKWFQDVWPKGMQDNKSADdfIQDQF 257
Cdd:cd14747 151 PDVSGFAipGKNDVWHNALPFVWGAGGDLATKDKWKAT---LDSPEAVAGLEFYTSLYQKGLSPKSTLENSAD--VEQAF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 258 VKGKAAAILGGPWSAANYKEA----KINYGVAKIPTLNNGKEYSpFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETL 333
Cdd:cd14747 226 ANGKVAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPS-FAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 334 YDMTNEVPANLKARDTAKSKNDELTNAVIEQYKNAQPMPNIPEmsevWTGAEN-----LMFDAASGSKTPQQSADDAVKV 408
Cdd:cd14747 305 AKATGMLPANTSAWDDPSLANDPLLAVFAEQLKTGKATPATPE----WGEIEAelvlvLEEVWIGVGADVEDALDKAAAE 380
|
..
gi 820769411 409 IE 410
Cdd:cd14747 381 IN 382
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
49-409 |
8.62e-46 |
|
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: 162.46 E-value: 8.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 49 KDYVNKIKGDFEKDN-DVKVKVV-EKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEV-KLGNKDDYDEKD 125
Cdd:cd14748 13 GKALEELVDEFNKSHpDIKVKAVyQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLdDYIDKDGVDDDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 126 -----QKQVTIDDKIYGAPAIIETLVLYYNKDLLDKA-------PATFKDLETLSKdsRFAFTSEKGKNTGF-LAKWTDF 192
Cdd:cd14748 93 fypaaLDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldpekpPKTWDELEEAAK--KLKDKGGKTGRYGFaLPPGDGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 193 YFSYGLLAGYGGYVFGDEGTNPKdigLNNKGSVEGITYATKWFQDvwpKGMQDNKSADDfIQDQFVKGKAAAILGGPWSA 272
Cdd:cd14748 171 WTFQALLWQNGGDLLDEDGGKVT---FNSPEGVEALEFLVDLVGK---DGVSPLNDWGD-AQDAFISGKVAMTINGTWSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 273 ANYK--EAKINYGVAKIPTlNNGKEYSPFAGGKGWVV-SNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDT 349
Cdd:cd14748 244 AGIRdkGAGFEYGVAPLPA-GKGKKGATPAGGASLVIpKGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAED 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820769411 350 AKS--KNDELTNAVIEQYKNAQP-MPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVI 409
Cdd:cd14748 323 PEEflAENPNYKVAVDQLDYAKPwGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
49-410 |
1.08e-39 |
|
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: 145.99 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 49 KDYVNKIKGDFEKDN-DVKVKVVEK---DMFETLEALpldGPAGTAPDVMMS-AFDRIGSLGQQGHLAevKLGNKDDYDE 123
Cdd:cd14749 14 KKYMDELIADFEKENpNIKVKVVVFpydNYKTKLKTA---VAAGEGPDVFNLwPGGWLAEFVKAGLLL--PLTDYLDPNG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 124 KDQKQ-------VTIDDKIYGAPAIIETLVLYYNKDLLDKA-----PATFKDLETLSKdsrfAFTSEKGKNTGF----LA 187
Cdd:cd14749 89 VDKRFlpgladaVTFNGKVYGIPFAARALALFYNKDLFEEAggvkpPKTWDELIEAAK----KDKFKAKGQTGFglllGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 188 KWTDFYFSYgLLAGYGGYVFGDEGTNPKDIglNNKGSVEgityATKWFQD-VWPKGMQDN---KSADDFIQDqFVKGKAA 263
Cdd:cd14749 165 QGGHWYFQY-LVRQAGGGPLSDDGSGKATF--NDPAFVQ----ALQKLQDlVKAGAFQEGfegIDYDDAGQA-FAQGKAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 264 AILGGPWSAANYK--EAKINYGVAKIPTLNNGKEYSP-FAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEV 340
Cdd:cd14749 237 MNIGGSWDLGAIKagEPGGKIGVFPFPTVGKGAQTSTiGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820769411 341 PANLKARDTAKSKNDELTNAVIEQYKNAQPMP----NIPEMSEVWTGAENLMFdaaSGSKTPQQSADDAVKVIE 410
Cdd:cd14749 317 PAKEVVAKDEDPDPVAILGPFADVLNAAGSTPfldeYWPAAAQVHKDAVQKLL---TGKIDPEQVVKQAQSAAA 387
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
39-409 |
1.40e-35 |
|
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: 134.73 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTVSVDAGYKDYVNKIKGDFEKDN-DVKVKVVE----KDMFETLEALPLDGpAGTAPDVMMSAFDRIGSLGQQGHLAEV 113
Cdd:cd14750 3 TFAAGSDGQEGELLKKAIAAFEKKHpDIKVEIEElpasSDDQRQQLVTALAA-GSSAPDVLGLDVIWIPEFAEAGWLLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 114 klgnkDDYDEKDQ---------KQVTIDDKIYGAPAIIETLVLYYNKDLLDKA----PATFKDLETLSKDSRfaftSEKG 180
Cdd:cd14750 82 -----TEYLKEEEdddflpatvEANTYDGKLYALPWFTDAGLLYYRKDLLEKYgpepPKTWDELLEAAKKRK----AGEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 181 KNTGFLAKW------TDFYFSYglLAGYGGYVFGDEGTNPkdiGLNNKGSVEGITYATKWFQDVWPKGMQDNKSADDFIQ 254
Cdd:cd14750 153 GIWGYVFQGkqyeglVCNFLEL--LWSNGGDIFDDDSGKV---TVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 255 DqFVKGKAAAILGGPWSAANYKEAKINY----GVAKIPTLnNGKEYSPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQ 330
Cdd:cd14750 228 A-FQAGKAAFMRNWPYAYALLQGPESAVagkvGVAPLPAG-PGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 331 ETLYDMTNEVPANLK-ARDTAKSKNDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVI 409
Cdd:cd14750 306 KRRAINGGLPPTRRAlYDDPEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEKL 385
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
53-410 |
1.27e-32 |
|
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: 126.73 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 53 NKIKGDFEKDN-DVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDRIGSLGQQGHLAEVklgnkDDYDE-KDQKQV- 129
Cdd:cd14751 17 EKLIPAFEKEYpKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPL-----DGTPAfDDIVDYl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 130 -------TIDDKIYGAPAIIETLVLYYNKDLLDKA----PATFKDLETLSKDsrfafTSEKGKNTGFLAKWTDFYFSYGL 198
Cdd:cd14751 92 pgpmetnRYNGHYYGVPQVTNTLALFYNKRLLEEAgtevPKTMDELVAAAKA-----IKKKKGRYGLYISGDGPYWLLPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 199 LAGYGGyVFGDEGTnpKDIGLNNKGSVEGITYATKWF-QDV---WPKGMQDNksaddfIQDQFVKGKAAAILGGPWSAAN 274
Cdd:cd14751 167 LWSFGG-DLTDEKK--ATGYLNSPESVRALETIVDLYdEGAitpCASGGYPN------MQDGFKSGRYAMIVNGPWAYAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 275 YKEAKI-----NYGVAKIPTlNNGKEYSPFaGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDT 349
Cdd:cd14751 238 ILGGKEfkdpdNLGIAPVPA-GPGGSGSPV-GGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYES 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820769411 350 AKSKNDELTNAVIEQYKNAQPMPNIPEMSEVWTGAENLMFDAASGSKTPQQSADDAVKVIE 410
Cdd:cd14751 316 PEVANNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
58-357 |
4.35e-32 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 122.90 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 58 DFEKDNDVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAF--DRIGSLGQQGHLAEvkLGNKDDYDEKDQ--KQVTIDD 133
Cdd:pfam13416 5 AFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWIaaDQLATLAEAGLLAD--LSDVDNLDDLPDalDAAGYDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 134 KIYGAPAIIET-LVLYYNKDLLDKAPATFKDLETLSKdsrfafTSEKGKNTGFLAKWTDFYFSYGLLAgyggyvfgdEGT 212
Cdd:pfam13416 83 KLYGVPYAASTpTVLYYNKDLLKKAGEDPKTWDELLA------AAAKLKGKTGLTDPATGWLLWALLA---------DGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 213 NPKDIGLNNKGSVEGITYATKWFQD--VWPKGmqdnksaDDFIQDqFVKGKAAAILGGPWSAANYKEAKINYGVAKIPTl 290
Cdd:pfam13416 148 DLTDDGKGVEALDEALAYLKKLKDNgkVYNTG-------ADAVQL-FANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKD- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820769411 291 nngkeySPFAGGKGWVVSNYSKNKDV-AQKWLDYVTNQKNQETLYDMTNEVPANLKARDTAKSKNDEL 357
Cdd:pfam13416 219 ------GSFLGGKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKADPA 280
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
51-331 |
1.54e-25 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 105.19 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 51 YVNKIKGDFEKDN-DVKVKVVEKDMFETLEALPLDGPAGTAP-DVMMSAFDRIGSLGQQGHLAEVKlgnkddyDEKDQKQ 128
Cdd:pfam01547 9 ALQALVKEFEKEHpGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLD-------DYVANYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 129 VTIDDKIYGAPAIIETLVLYYNKDLLDKA----PATFKDLETLSKDSRFAfTSEKGKNTGFLAKWTDFYFSYGLLAGYGG 204
Cdd:pfam01547 82 VLGVPKLYGVPLAAETLGLIYNKDLFKKAgldpPKTWDELLEAAKKLKEK-GKSPGGAGGGDASGTLGYFTLALLASLGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 205 YVFGDEGTnpkdiGLNNKGSVEGITYATKWF----QDVWPKGMQDNKSADDFIQDQFVKGKAAAILGGPWSA-------- 272
Cdd:pfam01547 161 PLFDKDGG-----GLDNPEAVDAITYYVDLYakvlLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAAlaankvkl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820769411 273 -----ANYKEAKINYGVAKIPTLNNGKeyspfAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQE 331
Cdd:pfam01547 236 kvafaAPAPDPKGDVGYAPLPAGKGGK-----GGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
11-382 |
1.73e-18 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 86.12 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 11 SAVLVMALSLAACGGGkdtSKSGSSDEKTLTVsvdAGYKDYVNK-IKGDFEKDNDVKVKVVEKDMFETLEALPLDGPAGt 89
Cdd:COG0687 5 SLLGLAAAALAAALAG---GAPAAAAEGTLNV---YNWGGYIDPdVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 90 aPDVMMSAFDRIGSLGQQGHLAEV---KLGNKDDYDEKDQKQVTIDDKIYGAPAIIETLVLYYNKDLLDKAPATFKDLet 166
Cdd:COG0687 78 -YDVVVPSDYFVARLIKAGLLQPLdksKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 167 lsKDSRFaftseKGKnTGFLAKWTDFyfsYGLLAGYGGYVFGDegTNPKDIGlnnkgsvEGITYATKWFQDV---WPkgm 243
Cdd:COG0687 155 --WDPEY-----KGK-VALLDDPREV---LGAALLYLGYDPNS--TDPADLD-------AAFELLIELKPNVrafWS--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 244 qdnkSADDFIQDqFVKGKAAAILGGPWSAANYKEAKINYGVAkIPtlnngKEyspfaGGKGW----VVSNYSKNKDVAQK 319
Cdd:COG0687 212 ----DGAEYIQL-LASGEVDLAVGWSGDALALRAEGPPIAYV-IP-----KE-----GALLWfdnmAIPKGAPNPDLAYA 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 320 WLDYVTNQKNQETLYDMTNEVPANLKARD--TAKSKNDELTNAVIEQYKNAQPMPNIP-----EMSEVWT 382
Cdd:COG0687 276 FINFMLSPEVAAALAEYVGYAPPNKAAREllPPELAANPAIYPPEEVLDKLEFWNPLPpenreLYTRRWT 345
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
58-343 |
4.39e-10 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 60.33 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 58 DFEKDNDVKVKVVEK---DMFETLEAlpldGPAGTAPDVMMS-AFDRIGSLGQQGHLAEVKLGNKDDYDEKDQkqvtiDD 133
Cdd:COG1840 4 AFEKKTGIKVNVVRGgsgELLARLKA----EGGNPPADVVWSgDADALEQLANEGLLQPYKSPELDAIPAEFR-----DP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 134 KIYGAPAIIETLVLYYNKDLLDK--APATFKDLetlsKDSRFaftseKGKNTgfLAKWTDFYFSYGLLAGYggyvfgdeg 211
Cdd:COG1840 75 DGYWFGFSVRARVIVYNTDLLKElgVPKSWEDL----LDPEY-----KGKIA--MADPSSSGTGYLLVAAL--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 212 tnpkdigLNNKGSVEGITYAtkwfqdvwpKGMQDNK----SADDFIQDQFVKGKAAAILGGPWSAANYKEAKINYGVAkI 287
Cdd:COG1840 135 -------LQAFGEEKGWEWL---------KGLAANGarvtGSSSAVAKAVASGEVAIGIVNSYYALRAKAKGAPVEVV-F 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 820769411 288 PtlnngKEYSPFAGGkGWVVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPAN 343
Cdd:COG1840 198 P-----EDGTLVNPS-GAAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVR 247
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
87-359 |
8.41e-10 |
|
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: 60.42 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 87 AGTAPDVMM-SAFDRIGSLGQQGHLAEV------KLGN-KDDYDEKDQKQVTIDDKIYGAP---AIIETLVLYYNKDLLD 155
Cdd:cd13580 56 SGDLPDIVVvNDPQLSITLVKQGALWDLtdyldkYYPNlKKIIEQEGWDSASVDGKIYGIPrkrPLIGRNGLWIRKDWLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 156 K----APATFKDLETLSKdsrfAFTSE----KGKNTGF---LAKWTDFYFSYGLLAGYGGYV---FGDEGTN--PKDIGL 219
Cdd:cd13580 136 KlgleVPKTLDELYEVAK----AFTEKdpdgNGKKDTYgltDTKDLIGSGFTGLFGAFGAPPnnwWKDEDGKlvPGSIQP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 220 NNKgsvEGITYATKWFQD--VWPKGMQDNKSAddfIQDQFVKGKAAAILGGPWSAANYKEAKIN------YGVAKIPTLN 291
Cdd:cd13580 212 EMK---EALKFLKKLYKEglIDPEFAVNDGTK---ANEKFISGKAGIFVGNWWDPAWPQASLKKndpdaeWVAVPIPSGP 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820769411 292 NGKEY--SPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQKNQETL--------YDMTNEVPANLKARDTAKSKNDELTN 359
Cdd:cd13580 286 DGKYGvwAESGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQKLLdygiegvhYTVKDGGPVNIIPPDKQEVGDATLDY 363
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
58-341 |
3.12e-08 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270239 [Multi-domain] Cd Length: 483 Bit Score: 55.54 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 58 DFEKDNDVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAF--DRIGSLGQQGHLAEV-----KLGN-KDDYD---EKDQ 126
Cdd:cd13521 25 EIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYlkDKFIAYGMEGAFLPLskyidQYPNlKAFFKqhpDVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 127 KQVTIDDKIYGAPAIIETLVLYY----NKDLLD----KAPATFKDLETLSKdsrfAFTsEKGKNT-------GFLAKWtD 191
Cdd:cd13521 105 ASTASDGKIYLIPYEPPKDVPNQgyfiRKDWLDklnlKTPKTLDELYNVLK----AFK-EKDPNGngkadeiPFIDRD-P 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 192 FYFSYGLLAGYGGYVFGdeGTNPKDIGLNNkGSV----------EGITYATKWfqdvWPKGMQDNKSA---DDFIQDQFV 258
Cdd:cd13521 179 LYGAFRLINSWGARSAG--GSTDSDWYEDN-GKFkhpfaseeykDGMKYMNKL----YTEGLIDKESFtqkDDQAEQKFS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 259 KGKAAAILGGPWSAANYKEA-----KINYGVAKIPTLNNGK-----EYSPFAGGKGWVVSNYSKNKDVAQKWLDYVTNQK 328
Cdd:cd13521 252 NGKLGGFTHNWFASDNLFTAqlgkeKPMYILLPIAPAGNVKgrreeDSPGYTGPDGVAISKKAKNPVAALKFFDWLASEE 331
|
330 340
....*....|....*....|.
gi 820769411 329 NQE--------TLYDMTNEVP 341
Cdd:cd13521 332 GRElanfgiegVHYNKDNGKK 352
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
58-381 |
3.73e-06 |
|
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: 48.38 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 58 DFEKDNDVKVKVVEKDMFETLEALPLDGPAGTAPDVMMSAFDrIGSLGQQGHLAEV---KLGNKDDYDEKDQKQVTIDDK 134
Cdd:cd13590 18 AFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGYDLVVPSDYM-VERLIKQGLLEPLdhsKLPNLKNLDPQFLNPPYDPGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 135 IYGAPAIIETLVLYYNKDLLDKAPATFKDLETLSKdsrfaftsEKGKnTGFLAKWTDfYFSYGLLagYGGYVFGDegTNP 214
Cdd:cd13590 97 RYSVPYQWGTTGIAYNKDKVKEPPTSWDLDLWDPA--------LKGR-IAMLDDARE-VLGAALL--ALGYSPNT--TDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 215 KDIG------LNNKGSVEGITYatkwfqdvwpkgmqdnksaDDFIQDqFVKGKAAAILG--GPWSAANYKEAKINYgVak 286
Cdd:cd13590 163 AELAaaaellIKQKPNVRAFDS-------------------DSYVQD-LASGEIWLAQAwsGDALQANRENPNLKF-V-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 287 IPtlnngKEyspfaGGKGW----VVSNYSKNKDVAQKWLDYVTNQKNQETLYDMTNEVPANLKARDT--AKSKNDELTNA 360
Cdd:cd13590 220 IP-----KE-----GGLLWvdnmAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELlpPELLDNPALYP 289
|
330 340
....*....|....*....|....*.
gi 820769411 361 VIEQYKNAQPMPNIPE-----MSEVW 381
Cdd:cd13590 290 PIEPLAKLLTFKDVDGealelYDRIW 315
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
39-348 |
4.58e-06 |
|
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: 48.06 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 39 TLTVSVDAGYKDYvnKIKGDFEKDNDVKVKVV----EKDMFetleALPLDGPAGtaPDVMMSAFDRIGSLGQQGHLAEV- 113
Cdd:cd13588 1 ELNVLTWPGYADP--DWVTAFEEATGCKVVVKffgsEDEMV----AKLRSGGGD--YDVVTPSGDALLRLIAAGLVQPId 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 114 --KLGNKDDYDEKDQKQ--VTIDDKIYGAPAIIETLVLYYNKDLLDKAPATFKDLEtlskdsrfaftsEKGKNTGFLAKW 189
Cdd:cd13588 73 tsKIPNYANIDPRLRNLpwLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALL------------WDPKYKGRVAAR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 190 TDFYFSYGLLAGYGGYvfgdegtnpKDIGLNNKGSVEGI------------TYatkWfqdvwpkgmqdnKSADDFIQDqF 257
Cdd:cd13588 141 DDPIDAIADAALYLGQ---------DPPFNLTDEQLDAVkaklreqrplvrKY---W------------SDGAELVQL-F 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 258 VKGkaAAILGGPWSAANYKEAKINYGVA-KIPtlnngKEyspfaGGKGWV----VSNYSKNKDVAQKWLDYVTNQKNQET 332
Cdd:cd13588 196 ANG--EVVAATAWSGQVNALQKAGKPVAyVIP-----KE-----GATGWVdtwmILKDAKNPDCAYKWLNYMLSPKVQAA 263
|
330
....*....|....*.
gi 820769411 333 LYDMTNEVPANLKARD 348
Cdd:cd13588 264 VAEWTGYAPSNPEACA 279
|
|
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
5-71 |
4.86e-06 |
|
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];
Pssm-ID: 441073 [Multi-domain] Cd Length: 270 Bit Score: 47.80 E-value: 4.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820769411 5 KKVGIVSAVLVMALSLAACGGGKdtSKSGSSDEKTLTVSVDAG-YKDYVNKIKGDFEKDNdVKVKVVE 71
Cdd:COG1464 2 KKLLALLLALALALALAACGSSS--AAAAAADKKTIKVGATPGpHAEILEVVKPELAKKG-IDLEIVE 66
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
144-407 |
1.06e-05 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 47.49 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 144 TLVLYYNKDLLDKA-------PATFKDLETLSKDSRFAftsekGKNTGFLAKWT------DFYFSYGLLA-----GYGGY 205
Cdd:PRK10974 146 TPVLYYNKDAFKKAgldpeqpPKTWQDLAAYAAKLRAA-----GMKCGYASGWQgwiqleNFSAWHGLPFasknnGFDGT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 206 VFGDEGTNPKDIG-------LNNKGSvegITYAtkwfqdvwpkGMQDNKSAddfiqdQFVKGKAAAILGGPWSAANYKE- 277
Cdd:PRK10974 221 DAVLEFNKPEQVKhialleeMNKKGD---FTYV----------GRKDESTE------KFYNGDCAITTASSGSLANIRKy 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 278 AKINYGVAKIP---TLNNGKEYSPFAGGKGWVVSNYSKN--KDVAqKWLDYVTNQKNQETLYDMTNEVPANLKARDTAK- 351
Cdd:PRK10974 282 AKFNYGVGMMPydaDVKGAPQNAIIGGASLWVMQGKDKEtyKGVA-KFLDFLAKPENAAEWHQKTGYLPITTAAYDLTRe 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820769411 352 ----SKNDELTNAvIEQYKNAQPMP--------NIP--------EMSEVWTGaenlmfdaasgSKTPQQSADDAVK 407
Cdd:PRK10974 361 qgfyEKNPGADTA-TRQMLNKPPLPftkglrlgNMPqirtivdeELESVWTG-----------KKTPQQALDSAVE 424
|
|
| PRK15046 |
PRK15046 |
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
1-164 |
4.25e-04 |
|
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 41.98 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 1 MKRFKKVGIVSAVLVMALSLAACGGGkdtSKSGSSDEKTLTVSVDAGYKDYVNKIKGDFEKDNDVKVKVVEKDMFETLEA 80
Cdd:PRK15046 1 MRSTNRAAAAAAMKLAAAAAAAAFGG---GAAPAWAADAVTVYSADGLEDWYQDVFPAFTKATGIKVNYVEAGSGEVVNR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 81 LPLDgPAGTAPDVMMSAFDRIGSLGQQGHLAEvklgnkddYDEKDQKQVTIDDKiyGAPAIIETLV-----LYYNKDLLD 155
Cdd:PRK15046 78 AAKE-KSNPQADVLVTLPPFIQQAAAEGLLQP--------YSSVNAKAVPAIAK--DADGTYAPFVnnylsFIYNPKVLK 146
|
....*....
gi 820769411 156 KAPATFKDL 164
Cdd:PRK15046 147 TAPATWADL 155
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
39-419 |
8.54e-04 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270299 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 8.54e-04
10 20 30 40 50 60 70 80
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gi 820769411 39 TLTVSV--DAGYKDYV-NKIKGDFEKDNDVKVK--VVEKDMFETLEALPLdgPAGTAPDVMMSAFDRIGSL---GQQG-- 108
Cdd:cd13581 3 TLTIFVrkSPLVEDYNeNLFFKRLEEKTGIKIEweTVPEDAWAEKKNLML--ASGDLPDAFLGAGASDADLmtyGKQGlf 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 109 ---------HLAEVK--LGNKDDYdekdQKQVT-IDDKIYGAPAIIETL------VLYYNKDLLDKA----PATFKDLET 166
Cdd:cd13581 81 lpledlidkYAPNLKalFDENPDI----KAAITaPDGHIYALPSVNECYhcsygqRMWINKKWLDKLglemPTTTDELYE 156
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 167 LSKdsrfAFtSEKGKN----------TGFLAKWTDFYFSYglLAGYGGYVFGDEGTNPKDIglnNKGSV----------E 226
Cdd:cd13581 157 VLK----AF-KEQDPNgngkadeiplSFSGLNGGTDDPAF--LLNSFGINDGGYGGYGFVV---KDGKViytatdpeykE 226
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 227 GITYATKWFQDvwpkGMQDNKSaddFIQD--QFV-KGKAA-AILGGP--WSAANYKEAKINYGVAKIPTL-------NNG 293
Cdd:cd13581 227 ALAYLNKLYKE----GLIDPEA---FTQDydQLAaKGKAStAKVGVFfgWDPGLFFGEERYEQYVPLPPLkgpngdqLAW 299
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820769411 294 KEYSPFAGGKGWVVSNYSKNKDVAQKWLDY----------------VTNQKNQETLYDMTNEVPANLKARDTAKSKNDEL 357
Cdd:cd13581 300 VGNSSGYGRGGFVITSKNKNPEAAIRWADFlyspegslqanfgpegEDWEKNPDGEYGVDGPPAAYKILEPSEGEQNVAW 379
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410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820769411 358 ----TNAVIEQYKNAQP-MPNIPEMSEVWTGAENLM--FDAASGSKTPQQSADDAVKV------IEDNVTQKYTK 419
Cdd:cd13581 380 adggPGAIPDEYRLKQVtDEDMDEAEARLDEAKKYYepYAPPDNSPPPALLDEEAEKIstiqtdINNYIEQKRAK 454
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