|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
11-356 |
1.75e-42 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 153.66 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 11 LVAIAAMSLTGLAACGGSS----ADDGKGKVYFLNFKPEAADQWVALAKKYTDKT-GVQVKVQTAASGTYEQTLKSELAK 85
Cdd:COG1653 5 ALALAAALALALAACGGGGsgaaAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYDDYRTKLLTALAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 86 SDAPTIFQVNGPvGYQNW--KGYTADLKDTGIYNELNNKDI------ALKDGDKVVGIPYVMETYGIIYNKDLLKKYtel 157
Cdd:COG1653 85 GNAPDVVQVDSG-WLAEFaaAGALVPLDDLLDDDGLDKDDFlpgaldAGTYDGKLYGVPFNTDTLGLYYNKDLFEKA--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 158 pgakikDVKEIDSFDKLKEVADDMQAKKDQLGIkgaftsaGFDSSSDWRFKTHLANIPLSYeFKEDG--VTTQPETIKGt 235
Cdd:COG1653 161 ------GLDPPKTWDELLAAAKKLKAKDGVYGF-------ALGGKDGAAWLDLLLSAGGDL-YDEDGkpAFDSPEAVEA- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 236 ylpnFKNIFDLYlkDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQKAGMKPDqVGMLPIYIGAKGEENQGL 315
Cdd:COG1653 226 ----LEFLKDLV--KDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFD-VGVAPLPGGPGGKKPASV 298
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 490389709 316 ATGSenYLCINAKASeaDQKASKDFLNWvVTSDEGIKALSE 356
Cdd:COG1653 299 LGGS--GLAIPKGSK--NPEAAWKFLKF-LTSPEAQAKWDA 334
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
52-373 |
2.02e-36 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 135.23 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 52 ALAKKYTDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTI---FQVNGPVGYQNWKGYTADLKDTGIYNELNNKDIALKD 128
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 129 GDKVVGIPYVMET-YGIIYNKDLLKkytelpgakiKDVKEIDSFDKLKEVADDmqakkdqlgIKGAFTSAgfDSSSDWRF 207
Cdd:pfam13416 81 DGKLYGVPYAASTpTVLYYNKDLLK----------KAGEDPKTWDELLAAAAK---------LKGKTGLT--DPATGWLL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 208 KTHLAniplsyefkeDGVTTQPETIKGTYLPNFKNIFDLYLKDSTTApsqlssKTGDDANSEFALGEAAFYQNGTWAWTD 287
Cdd:pfam13416 140 WALLA----------DGVDLTDDGKGVEALDEALAYLKKLKDNGKVY------NTGADAVQLFANGEVAMTVNGTWAAAA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 288 LQKAGmkpDQVGMLPIyigakgeeNQGLATGSENyLCINAKASEADQkASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF 367
Cdd:pfam13416 204 AKKAG---KKLGAVVP--------KDGSFLGGKG-LVVPAGAKDPRL-AALDFIKF-LTSPENQAALAEDTGYIPANKSA 269
|
....*....
gi 490389709 368 ---DKVKSD 373
Cdd:pfam13416 270 alsDEVKAD 278
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-433 |
3.69e-27 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 112.35 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 1 MNRTVKATVGLVAIAAMSLtglAACGG-------SSADDGKGKVYFLNFKPEAADqWVALAKKYTDKTGVQVKVQTAASG 73
Cdd:COG2182 1 MKRRLLAALALALALALAL---AACGSgssssgsSSAAGAGGTLTVWVDDDEAEA-LEEAAAAFEEEPGIKVKVVEVPWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 74 TYEQTLKSELAKSDAPTIFQV----------NG-----PVGYQNWKGYTADLKDTGIYNelnnkdialkdgDKVVGIPYV 138
Cdd:COG2182 77 DLREKLTTAAPAGKGPDVFVGahdwlgelaeAGllaplDDDLADKDDFLPAALDAVTYD------------GKLYGVPYA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 139 METYGIIYNKDLLKKytELPgakikdvkeiDSFDKLKEVADDMQAKKDQ---LGIKGAFTSAGFDSSSDWrfkthlanip 215
Cdd:COG2182 145 VETLALYYNKDLVKA--EPP----------KTWDELIAAAKKLTAAGKYglaYDAGDAYYFYPFLAAFGG---------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 216 lsYEFKEDGVTTQ------PETIKGTYlpnfknifdlYLKDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQ 289
Cdd:COG2182 203 --YLFGKDGDDPKdvglnsPGAVAALE----------YLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 290 KAgmKPDQVGMLPIYIGAKGEENQGLAtGSENYlCINAKAseADQKASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF-- 367
Cdd:COG2182 271 KA--LGIDYGVAPLPTLAGGKPAKPFV-GVKGF-GVSAYS--KNKEAAQEFAEY-LTSPEAQKALFEATGRIPANKAAae 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490389709 368 DKVKSDNPLVE---EAVEDSnsgkeqvawnfTMMPSE-EWK---NQLGQAMLAYAQGNGS----WDDVQKAFVDNWK 433
Cdd:COG2182 344 DAEVKADPLIAafaEQAEYA-----------VPMPNIpEMGavwTPLGTALQAIASGKADpaeaLDAAQKQIEAAIA 409
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
44-417 |
7.68e-21 |
|
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: 93.62 E-value: 7.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 44 PEAADQWVALAKKYTDK-TGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPvGYQNW--KGYTADL-----KDTGI 115
Cdd:cd13585 10 PAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGP-WVPEFasNGALLDLddyieKDGLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 116 YNELNNKDIALKDGDKVVGIPYVMETYGIIYNKDLLKKYTELPgakikdvKEIDSFDKLKEVaddmqAKKDQLGIKGAFt 195
Cdd:cd13585 89 DDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGP-------KPPWTWDELLEA-----AKKLTDKKGGQY- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 196 saGFDSSSDWRFKTHLANIPLSY---EFKEDGVT---TQPETIKGtylpnFKNIFDLYlkDSTTAPSQLSSkTGDDANSE 269
Cdd:cd13585 156 --GFALRGGSGGQTQWYPFLWSNggdLLDEDDGKatlNSPEAVEA-----LQFYVDLY--KDGVAPSSATT-GGDEAVDL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 270 FALGEAAFYQNGTWAWTDLqKAGMKPDQVGMLPIYIGAKGEENQGLATGSenyLCINAKAseADQKASKDFLNWvVTSDE 349
Cdd:cd13585 226 FASGKVAMMIDGPWALGTL-KDSKVKFKWGVAPLPAGPGGKRASVLGGWG---LAISKNS--KHPEAAWKFIKF-LTSKE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490389709 350 GIKALSEDMGFTTPFKTFDKVKSDNPLVEEAVEDSNSGKEQVAWNFTMMPSEEWKNQLGQAMLAYAQG 417
Cdd:cd13585 299 NQLKLGGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLG 366
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
62-428 |
1.61e-15 |
|
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: 77.81 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 62 GVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPVGYQNW--KGYTADLKDTGIYNELNNK------DIALKDGdKVV 133
Cdd:cd14749 30 NIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFvkAGLLLPLTDYLDPNGVDKRflpglaDAVTFNG-KVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 134 GIPYVMETYGIIYNKDLLKKytelpgAKIKDVKEidSFDKLKEVaddmqAKKDQLGIKGA--FTSAGFDSSSDWRFKThl 211
Cdd:cd14749 109 GIPFAARALALFYNKDLFEE------AGGVKPPK--TWDELIEA-----AKKDKFKAKGQtgFGLLLGAQGGHWYFQY-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 212 ANIPLSYEFKEDgVTTQPETIkgTYLPN---FKNIFDLYLKDSTTAPsqLSSKTGDDANSEFALGEAAFYQNGTWAWTDL 288
Cdd:cd14749 174 LVRQAGGGPLSD-DGSGKATF--NDPAFvqaLQKLQDLVKAGAFQEG--FEGIDYDDAGQAFAQGKAAMNIGGSWDLGAI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 289 qKAGMKPDQVGMLPIYIGAKGeeNQGLATGSeNYLCINAKASEADQKASKDFLNWvVTSDEGIKALSEDMGFTTpfKTFD 368
Cdd:cd14749 249 -KAGEPGGKIGVFPFPTVGKG--AQTSTIGG-SDWAIAISANGKKKEAAVKFLKY-LTSPEVMKQYLEDVGLLP--AKEV 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490389709 369 KVK----SDNPLVEEAVEDSNSGKEQVAWNFTMMP-SEEWKNQLGQAMLAYAQGNGSWDDVQKAF 428
Cdd:cd14749 322 VAKdedpDPVAILGPFADVLNAAGSTPFLDEYWPAaAQVHKDAVQKLLTGKIDPEQVVKQAQSAA 386
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
45-350 |
5.46e-15 |
|
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: 75.15 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 45 EAADQWVALAKKYT-DKTGVQVKVQTAASGTYEQTLKSELAKSDAPT-IFQVNGpvgyqnwkGYTADLKDTGIYNELNN- 121
Cdd:pfam01547 5 TEAAALQALVKEFEkEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPAdVFASDN--------DWIAELAKAGLLLPLDDy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 122 -KDIALKDGDKVVGIPYVMETYGIIYNKDLLKKYtelpgakikDVKEIDSFDKLKEVADDMQAKkdqlGIKGAFTSAGFD 200
Cdd:pfam01547 77 vANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKA---------GLDPPKTWDELLEAAKKLKEK----GKSPGGAGGGDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 201 SSSDWRFKTHLANIPLSYEFKEDGVTTQPETIKGTyLPNFKNIFDLYLKDSTTAPSQLSSKTGDDANSEFALGEAAFYQN 280
Cdd:pfam01547 144 SGTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDA-ITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490389709 281 GTWAWTDLQKAGMKPDQV---GMLPIYIGAKGEENQGLATGSENYLCINAKAseADQKASKDFLNWvVTSDEG 350
Cdd:pfam01547 223 GPWAALAANKVKLKVAFAapaPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGS--KNKEAAKKFLDF-LTSPEA 292
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
52-427 |
7.79e-15 |
|
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: 75.79 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 52 ALAKKYTDK-TGVQVKVQTAASGTYEQT-LKSELAKSDAPTIFQVngpvgYQNWkgyTADLKDTGIY---------NELN 120
Cdd:cd14748 18 ELVDEFNKShPDIKVKAVYQGSYDDTLTkLLAALAAGTAPDVAQV-----DASW---VAQLADSGALeplddyidkDGVD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 121 NKDI------ALKDGDKVVGIPYVMETYGIIYNKDLLKKytelpgAKIKDVKEIDSFDKLKEVADDMQAKKDQLGIKGAF 194
Cdd:cd14748 90 DDDFypaaldAGTYDGKLYGLPFDTSTPVLYYNKDLFEE------AGLDPEKPPKTWDELEEAAKKLKDKGGKTGRYGFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 195 TSAGFDsssDWRFKTHLANIPLSYeFKEDGVTTQPETikgtylPNFKNIFDlYLKDSTTAPSQLSSKTGDDANSEFALGE 274
Cdd:cd14748 164 LPPGDG---GWTFQALLWQNGGDL-LDEDGGKVTFNS------PEGVEALE-FLVDLVGKDGVSPLNDWGDAQDAFISGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 275 AAFYQNGTWAWTDLQKAGMKPD-QVGMLPiyigAKGEENQGLATGSeNYLCINAKASEaDQKASKDFLNWvVTSDEGIKA 353
Cdd:cd14748 233 VAMTINGTWSLAGIRDKGAGFEyGVAPLP----AGKGKKGATPAGG-ASLVIPKGSSK-KKEAAWEFIKF-LTSPENQAK 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490389709 354 LSEDMGFTTPFK----TFDKVKSDNPLVEEAVEDSNSGKeqvAWNFTMMPSEEWKNQLGQAMLAYAQGNgswDDVQKA 427
Cdd:cd14748 306 WAKATGYLPVRKsaaeDPEEFLAENPNYKVAVDQLDYAK---PWGPPVPNGAEIRDELNEALEAALLGK---KTPEEA 377
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
52-432 |
1.29e-14 |
|
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: 75.02 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 52 ALAKKYTDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQvnGP---VGYQNWKGYTADLkDTGIYNELNNKDIALKD 128
Cdd:cd13586 17 ELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFF--GPhdwLGELAAAGLLAPI-PEYLAVKIKNLPVALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 129 ---GDKVVGIPYVMETYGIIYNKDLLKkytELPgakikdvkeiDSFDKLKEvaddmQAKKDQLGIKGAFtsaGFDSSSDW 205
Cdd:cd13586 94 vtyNGKLYGVPVSVETIALFYNKDLVP---EPP----------KTWEELIA-----LAKKFNDKAGGKY---GFAYDQTN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 206 RFKTHlaniPL-----SYEFKEDGVTT------QPETIKGtylpnFKNIFDLYLKDSTTAPSQlsskTGDDANSEFALGE 274
Cdd:cd13586 153 PYFSY----PFlaafgGYVFGENGGDPtdiglnNEGAVKG-----LKFIKDLKKKYKVLPPDL----DYDIADALFKEGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 275 AAFYQNGTWAWTDLQKAGMKPDqVGMLPIYIGAKgeenQGLATGSENYLCINAKAseADQKASKDFLNWvVTSDEGIKAL 354
Cdd:cd13586 220 AAMIINGPWDLADYKDAGINFG-VAPLPTLPGGK----QAAPFVGVQGAFVSAYS--KNKEAAVEFAEY-LTSDEAQLLL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 355 SEDMGFTTPFKTF--DKVKSDNPLVEEAVEDSNSGkeqvawnfTMMP-----SEEWkNQLGQAMLAYAQGNGSWDDVQKA 427
Cdd:cd13586 292 FEKTGRIPALKDAlnDAAVKNDPLVKAFAEQAQYG--------VPMPnipemAAVW-DAMGNALNLVASGKATPEEAAKD 362
|
....*
gi 490389709 428 FVDNW 432
Cdd:cd13586 363 AVAAI 367
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
54-378 |
4.50e-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: 64.04 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 54 AKKYTDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQV-NGPVGYQNWKGYTADLK-DTGIYNELNNKDI-ALKDGD 130
Cdd:cd13658 19 AKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVApHDRIGSAVLQGLLSPIKlSKDKKKGFTDQALkALTYDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 131 KVVGIPYVMETYGIIYNKDLLKkytelpgakikdvKEIDSFDKLKEVADDM-QAKKDQLGIKGAFT----SAGFDSSSDw 205
Cdd:cd13658 99 KLYGLPAAVETLALYYNKDLVK-------------NAPKTFDELEALAKDLtKEKGKQYGFLADATnfyySYGLLAGNG- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 206 rfkthlaniplSYEFKEDGVT--------TQPETIKG-TYLPNFknifdlylKDSTTAPSQLsskTGDDANSEFALGEAA 276
Cdd:cd13658 165 -----------GYIFKKNGSDldindiglNSPGAVKAvKFLKKW--------YTEGYLPKGM---TGDVIQGLFKEGKAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 277 FYQNGTWAWTDLQKAGMkpdQVGMLPIYIGAKGEENQGLATGSENYLcinAKASEaDQKASKDFLNWvVTSDEGIKALSE 356
Cdd:cd13658 223 AVIDGPWAIQEYQEAGV---NYGVAPLPTLPNGKPMAPFLGVKGWYL---SAYSK-HKEWAQKFMEF-LTSKENLKKRYD 294
|
330 340
....*....|....*....|....
gi 490389709 357 DMGFTTPFKTF--DKVKSDNPLVE 378
Cdd:cd13658 295 ETNEIPPRKDVrsDPEIKNNPLTS 318
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
55-418 |
1.21e-09 |
|
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: 60.03 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 55 KKYTDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPVGYQNW-------------KGYTADLKDtgiYNELNN 121
Cdd:cd13580 26 KYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLvkqgalwdltdylDKYYPNLKK---IIEQEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 122 KDIALKDGdKVVGIPYVME---TYGIIYNKDLLKKytelpgAKIKDVKEIdsfDKLKEVA-----DDMqakkDQLGIKGA 193
Cdd:cd13580 103 WDSASVDG-KIYGIPRKRPligRNGLWIRKDWLDK------LGLEVPKTL---DELYEVAkafteKDP----DGNGKKDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 194 FTSAGFDSSSDWRFKTHLA--NIPLSYEFKEDGVTTQPETIkgtyLPNFKN----IFDLY---LKDSTTApsqlsSKTGD 264
Cdd:cd13580 169 YGLTDTKDLIGSGFTGLFGafGAPPNNWWKDEDGKLVPGSI----QPEMKEalkfLKKLYkegLIDPEFA-----VNDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 265 DANSEFALGEAAFYQnGTWAWTDLQKAGMKPDQVGM----LPIYIGAKGEENQGLATGSENYLCINAKASEAdqKASKDF 340
Cdd:cd13580 240 KANEKFISGKAGIFV-GNWWDPAWPQASLKKNDPDAewvaVPIPSGPDGKYGVWAESGVNGFFVIPKKSKKP--EAILKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 341 LNWVVTSD---------EGIKALSEDMGFTTPFKTFDKVKSDNPLVEEAVEDSNSGKEQVAwNFTMMPSEEWKNQLGQAM 411
Cdd:cd13580 317 LDFLSDPEvqklldygiEGVHYTVKDGGPVNIIPPDKQEVGDATLDYFQGSLALEKYKLTN-NGERKSDAKKEALDERVV 395
|
....*..
gi 490389709 412 LAYAQGN 418
Cdd:cd13580 396 NANDEEN 402
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
53-387 |
2.31e-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: 55.68 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 53 LAKKYTDKTGVQVKVQ--TAASGTYEQTLkselAKSDAPTI-FQVNGPVGYQNWKGYTADLK-DTGIYNELNNKDI-ALK 127
Cdd:cd13656 19 VGKKFEKDTGIKVTVEhpDKLEEKFPQVA----ATGDGPDIiFWAHDRFGGYAQSGLLAEITpDKAFQDKLYPFTWdAVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 128 DGDKVVGIPYVMETYGIIYNKDLLKKytelPGAKIKDVKEIDSFDKLKEVADDMQAKKDQLgikgaFTSAGFDSSSDWRF 207
Cdd:cd13656 95 YNGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALMFNLQEPY-----FTWPLIAADGGYAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 208 KTHLAniplSYEFKEDGVTTQPETIKGTYLpnfknifdLYLKDSTTAPSQLSSKTgddANSEFALGEAAFYQNGTWAWTD 287
Cdd:cd13656 166 KYENG----KYDIKDVGVDNAGAKAGLTFL--------VDLIKNKHMNADTDYSI---AEAAFNKGETAMTINGPWAWSN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 288 LQKAGMkPDQVGMLPIYIGAKGEENQGLATGSENylcinakASEADQKASKDFLNWVVTSDEGIKALSEDMGFTTP-FKT 366
Cdd:cd13656 231 IDTSKV-NYGVTVLPTFKGQPSKPFVGVLSAGIN-------AASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVaLKS 302
|
330 340
....*....|....*....|.
gi 490389709 367 FDKVKSDNPLVEEAVEDSNSG 387
Cdd:cd13656 303 YEEELAKDPRIAATMENAQKG 323
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
45-360 |
2.90e-07 |
|
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: 52.32 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 45 EAADQWV-ALAKKYTDKT-GVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGpvgyqNWKGY----------TADLKD 112
Cdd:cd14747 10 SAEAELLkELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGN-----TWVAEfaamgaledlTPYLED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 113 TGIYNEL--NNKDIALKDGdKVVGIPYVMETYGIIYNKDLLKK--YTELPgakiKDVKEIDSF-DKLKEVADDMQA---K 184
Cdd:cd14747 85 LGGDKDLfpGLVDTGTVDG-KYYGVPWYADTRALFYRTDLLKKagGDEAP----KTWDELEAAaKKIKADGPDVSGfaiP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 185 KDQLGIKGAFT---SAGFD--SSSDWRfkthlaniplsyefkedGVTTQPETIKGtyLPNFKNIFDLYLKDSTTAPSQLs 259
Cdd:cd14747 160 GKNDVWHNALPfvwGAGGDlaTKDKWK-----------------ATLDSPEAVAG--LEFYTSLYQKGLSPKSTLENSA- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 260 sktgdDANSEFALGEAAFYQNGTWAWTDLQKAGMKP-DQVGMLPIYIGAKGeENQGLATGSEnyLCINAKASEADqkASK 338
Cdd:cd14747 220 -----DVEQAFANGKVAMIISGPWEIGAIREAGPDLaGKWGVAPLPGGPGG-GSPSFAGGSN--LAVFKGSKNKD--LAW 289
|
330 340
....*....|....*....|..
gi 490389709 339 DFLNWvVTSDEGIKALSEDMGF 360
Cdd:cd14747 290 KFIEF-LSSPENQAAYAKATGM 310
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
62-437 |
1.68e-06 |
|
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: 50.07 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 62 GVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNgpvgyqnwKGYTADLKDTGIYNELNN-------KDI-------ALK 127
Cdd:cd14751 29 KIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRAD--------IAWVPEFAKLGYLQPLDGtpafddiVDYlpgpmetNRY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 128 DGdKVVGIPYVMETYGIIYNKDLLKK-YTELPGakikdvkeidSFDKLKEVADDMQAKKDQLGIKGAFTSAGFDSSSDWR 206
Cdd:cd14751 101 NG-HYYGVPQVTNTLALFYNKRLLEEaGTEVPK----------TMDELVAAAKAIKKKKGRYGLYISGDGPYWLLPFLWS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 207 FKTHLANiplsyEFKEDGVTTQPETIKGTylpnfKNIFDLYLKDSTTaPSQLSSKtgDDANSEFALGEAAFYQNGTWAWT 286
Cdd:cd14751 170 FGGDLTD-----EKKATGYLNSPESVRAL-----ETIVDLYDEGAIT-PCASGGY--PNMQDGFKSGRYAMIVNGPWAYA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 287 DLQKAGM--KPDQVGMLPIYIGAKGeenQGLATGSENYLCINakaSEADQKASKDFLNWvVTSDEGIKALSEDMGfTTPF 364
Cdd:cd14751 237 DILGGKEfkDPDNLGIAPVPAGPGG---SGSPVGGEDLVIFK---GSKNKDAAWKFVKF-MSSAEAQALTAAKLG-LLPT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 365 KT----FDKVKsDNPLVE---EAVEdsnsgkeqVAWNFTMMPS-EEWKNQLGQAMLAYAQGNgswDDVQKAfVDNWKTEY 436
Cdd:cd14751 309 RTsayeSPEVA-NNPMVAafkPALE--------TAVPRPPIPEwGELFEPLTLAFAKVLRGE---KSPREA-LDEAAKQW 375
|
.
gi 490389709 437 D 437
Cdd:cd14751 376 D 376
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
45-360 |
2.36e-06 |
|
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: 49.60 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 45 EAADQWvalAKKYTDKTgVQVKVQTAASGTYEQTLKSEL-AKSDAPTIFQVNGPvgyqnWKGYTA----DLKDTGIYNEL 119
Cdd:cd14750 18 KAIAAF---EKKHPDIK-VEIEELPASSDDQRQQLVTALaAGSSAPDVLGLDVI-----WIPEFAeagwLLPLTEYLKEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 120 NNKDI------ALKDGDKVVGIPYVMETYGIIYNKDLLKKYTELPGAkikdvkeidSFDKLKEVADDMQAKKDqlGIKG- 192
Cdd:cd14750 89 EDDDFlpatveANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPK---------TWDELLEAAKKRKAGEP--GIWGy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 193 ----------------AFTSAGFDsssdwrfkthlaniplSYEFKEDGVTT-QPETIKGtylpnFKNIFDLYlkDSTTAP 255
Cdd:cd14750 158 vfqgkqyeglvcnfleLLWSNGGD----------------IFDDDSGKVTVdSPEALEA-----LQFLRDLI--GEGISP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 256 SQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQKAGMK-PDQVGMLPIyigAKGEENQGlATGSENY-LCINAKASEad 333
Cdd:cd14750 215 KGVLTYGEEEARAAFQAGKAAFMRNWPYAYALLQGPESAvAGKVGVAPL---PAGPGGGS-ASTLGGWnLAISANSKH-- 288
|
330 340
....*....|....*....|....*..
gi 490389709 334 QKASKDFLNWvVTSDEGIKALSEDMGF 360
Cdd:cd14750 289 KEAAWEFVKF-LTSPEVQKRRAINGGL 314
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
44-354 |
5.55e-06 |
|
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: 48.14 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 44 PEAADQWVALAKKYTDKTGV-QVKVQTAASGTYEQTLKSELAKSDAPTIFqvngpVGYQNW------KGYTADLKDTGIY 116
Cdd:cd13657 10 GAEEDALQQIIDEFEAKYPVpNVKVPFEKKPDLQNKLLTAIPAGEGPDLF-----IWAHDWigqfaeAGLLVPISDYLSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 117 NELNN-KDIALKDG---DKVVGIPYVMETYGIIYNKDLLKkytELPgakikdvkeiDSFDKLKEVADDMQAK-KDQLGIK 191
Cdd:cd13657 85 DDFENyLPTAVEAVtykGKVYGLPEAYETVALIYNKALVD---QPP----------ETTDELLAIMKDHTDPaAGSYGLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 192 GAFTSAGFDSSSDWRFKTHLANiplsYEFKEDGVTTqPETIKGtylpnFKNIFDLYLKDSTTAPSqlssktGDDANSEFA 271
Cdd:cd13657 152 YQVSDAYFVSAWIFGFGGYYFD----DETDKPGLDT-PETIKG-----IQFLKDFSWPYMPSDPS------YNTQTSLFN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 272 LGEAAFYQNGTWAWTDLQKAGmkpDQVGMLPIyigAKGEENQGLA--TGSEN-YLCINAKASEADqkASKDFLNWvVTSD 348
Cdd:cd13657 216 EGKAAMIINGPWFIGGIKAAG---IDLGVAPL---PTVDGTNPPRpySGVEGiYVTKYAERKNKE--AALDFAKF-FTTA 286
|
....*.
gi 490389709 349 EGIKAL 354
Cdd:cd13657 287 EASKIL 292
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
6-357 |
1.32e-05 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 47.31 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 6 KATVGLVAIAAMSLTGLAACGGSSADDGKGK-VYFLNfkpeaADQ-WVALA---KKYTDKTGVQVKVQT--AASGTYEQT 78
Cdd:PRK09474 2 KIKKGLRTLALSALATLMFSASALAKIEEGKlVIWIN-----GDKgYNGLAevgKKFEKDTGIKVTVEHpdKLEEKFPQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 79 LkselAKSDAPTI-FQVNGPVGYQNWKGYTADLKDTgiyNELNNKDI-----ALKDGDKVVGIPYVMETYGIIYNKDLLK 152
Cdd:PRK09474 77 A----ATGDGPDIiFWAHDRFGGYAQSGLLAEVTPS---KAFKDKLVpftwdAVRYNGKLIGYPIAVEALSLIYNKDLVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 153 KytelPGAKIKDVKEIDsfDKLKEvaddmQAKKDQL-GIKGA-FTSAGFDSSSDWRFKTHLANiplsYEFKEDGVTTqPE 230
Cdd:PRK09474 150 T----PPKTWEEIPALD--KELKA-----KGKSAIMwNLQEPyFTWPLIAADGGYAFKFENGG----YDVKDVGVNN-AG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 231 TIKGTylpNFknIFDLYLKDSTTAPSQLSSktgddANSEFALGEAAFYQNGTWAWTDLQKAGMkPDQVGMLPIYIGAKGE 310
Cdd:PRK09474 214 AKAGL---QF--LVDLVKNKHMNADTDYSI-----AEAAFNKGETAMTINGPWAWSNIDKSGI-NYGVTVLPTFNGKPSK 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490389709 311 ENQGLATGSENylcinakASEADQKASKDFL-NWVVTsDEGIKALSED 357
Cdd:PRK09474 283 PFVGVLSAGIN-------AASPNKELAKEFLeNYLLT-DEGLETVNKD 322
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
50-303 |
5.85e-04 |
|
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: 42.01 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 50 WVALAKKYTDKT-GVQVKVQTAASGTYEQTLKSELAKSDAPTIF-QVNGPVGYQNWKGYTADLKDtgiYNELNNKDI--- 124
Cdd:cd13522 16 VNELIAKFEKAYpGITVEVTYQDTEARRQFFSTAAAGGKGPDVVfGPSDSLGPFAAAGLLAPLDE---YVSKSGKYApnt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 125 --ALKDGDKVVGIPYVMETYGIIYNKDLLkkyTELPGAKIKDVKEIDSFDKLKEVADDMqakkdqlgikgaftsagFDSS 202
Cdd:cd13522 93 iaAMKLNGKLYGVPVSVGAHLMYYNKKLV---PKNPPKTWQELIALAQGLKAKNVWGLV-----------------YNQN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 203 SDWRFKTHLANIPlSYEFKEDGVTTQPETIKGTYLPNFKNIFDLYLKDSTTAPSqlsskTGDD-ANSEFALGEAAFYQNG 281
Cdd:cd13522 153 EPYFFAAWIGGFG-GQVFKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPE-----TDYSiADALFKAGKAAMIING 226
|
250 260
....*....|....*....|..
gi 490389709 282 TWAWTDLQKAgMKPDqVGMLPI 303
Cdd:cd13522 227 PWDLGDYRQA-LKIN-LGVAPL 246
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
54-369 |
1.38e-03 |
|
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: 40.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 54 AKKYTDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIfqvngpVGYQNWKGYTADLKDTGIYNELNN------------ 121
Cdd:cd13521 23 AKEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDI------VGADYLKDKFIAYGMEGAFLPLSKyidqypnlkaff 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 122 -----KDIALKDGD-KVVGIPYVME----TYGIIYNKDLLKKYtelpgakikDVKEIDSFDKLKEVADDMQAK------- 184
Cdd:cd13521 97 kqhpdVLRASTASDgKIYLIPYEPPkdvpNQGYFIRKDWLDKL---------NLKTPKTLDELYNVLKAFKEKdpngngk 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 185 KDQ--LGIKGAFTSAGFDSSSdWRFKTHLANIPlsYEFKEDGVTTQPETIKGTYLPNFKNIFDLYlkDSTTAPSQLSSKT 262
Cdd:cd13521 168 ADEipFIDRDPLYGAFRLINS-WGARSAGGSTD--SDWYEDNGKFKHPFASEEYKDGMKYMNKLY--TEGLIDKESFTQK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 263 GDDANSEFALGEAAFYQNGTWAWTDLQKAGMKPDQVGMLPIYIGAKGE-----ENQGLATGSENYLCINAKAseADQKAS 337
Cdd:cd13521 243 DDQAEQKFSNGKLGGFTHNWFASDNLFTAQLGKEKPMYILLPIAPAGNvkgrrEEDSPGYTGPDGVAISKKA--KNPVAA 320
|
330 340 350
....*....|....*....|....*....|..
gi 490389709 338 KDFLNWvVTSDEGikalSEDMGFTTPFKTFDK 369
Cdd:cd13521 321 LKFFDW-LASEEG----RELANFGIEGVHYNK 347
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
49-153 |
3.21e-03 |
|
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270307 [Multi-domain] Cd Length: 268 Bit Score: 39.13 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 49 QWVALAKKYTDKTGVQVKVQTAASGTYEQTLKselAKSDAPTI--FQVNGPVGYQ-NWKGYTADLKDTGIYNELNNKDIA 125
Cdd:cd13589 15 QRKAVIEPFEKETGIKVVYDTGTSADRLAKLQ---AQAGNPQWdvVDLDDGDAARaIAEGLLEPLDYSKIPNAAKDKAPA 91
|
90 100
....*....|....*....|....*...
gi 490389709 126 LKDGDKvvGIPYVMETYGIIYNKDLLKK 153
Cdd:cd13589 92 ALKTGY--GVGYTLYSTGIAYNTDKFKE 117
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
53-153 |
5.67e-03 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 38.38 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490389709 53 LAKKYTDKTGVQVKVQTAASGTYEQTLKSELAKSDApTIFQVNGPVGYQNWK--GYTADLKDTgiynELNNKDIALKDGD 130
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELLARLKAEGGNPPA-DVVWSGDADALEQLAneGLLQPYKSP----ELDAIPAEFRDPD 75
|
90 100
....*....|....*....|...
gi 490389709 131 KVVgIPYVMETYGIIYNKDLLKK 153
Cdd:COG1840 76 GYW-FGFSVRARVIVYNTDLLKE 97
|
|
| |
