|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
91-478 |
3.96e-62 |
|
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: 207.26 E-value: 3.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWAHqGQKSESAALRKAVKSFNSSQHKIKVELKLIPTNDY-TKTITATDASKLPDVMEFDGPTMANFVYNKKLAPMDS 169
Cdd:cd13585 2 LTFWDW-GQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYwTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 170 YVSAKTMSNATDAG-KAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGvkypTNLSDDWTATEFTAALKALGTKDSDGKv 248
Cdd:cd13585 81 YIEKDGLDDDFPPGlLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG----PGPKPPWTWDELLEAAKKLTDKKGGQY- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 249 vdlqensGYA---NEWGTFGFAPVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQSWKPY--------TDPNTDGNAFAN 317
Cdd:cd13585 156 -------GFAlrgGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDgvapssatTGGDEAVDLFAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 318 GRVALSWVGHWMYPAY-SKALGDDLVVLPLPDF-GNGPKTGQGSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANG 395
Cdd:cd13585 229 GKVAMMIDGPWALGTLkDSKVKFKWGVAPLPAGpGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 396 APPATRSALAKSELYQRGGPLQLFADqlakpcrDSDVTKTCVAVTRPVTAGYPTVTAKFSDALNAIYgGADPKGALEKAA 475
Cdd:cd13585 309 PAALAAAAASAAAPDAKPALALAAAA-------DALAAAVPPPVPPPWPEVYPILSEALQEALLGAL-GKSPEEALKEAA 380
|
...
gi 302464743 476 RAI 478
Cdd:cd13585 381 KEI 383
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
72-479 |
2.33e-54 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 187.46 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 72 CGGGSGADVSAEAGSGKGAISVWAHQGqksESAALRKAVKSFNSsQHKIKVELKLIPTNDY-TKTITATDASKLPDVMEF 150
Cdd:COG2182 22 CGSGSSSSGSSSAAGAGGTLTVWVDDD---EAEALEEAAAAFEE-EPGIKVKVVEVPWDDLrEKLTTAAPAGKGPDVFVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 151 DGPTMANFVYNKKLAPMDSYVSAKtmSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAagvKYPTNLSddwtat 230
Cdd:COG2182 98 AHDWLGELAEAGLLAPLDDDLADK--DDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA---EPPKTWD------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 231 EFTAALKALGTKDSDGKVVDLQEnsgyanewgTFGFAPVLWSAGGSLLKDGKAEG---ALDTPAALSAMKTLQSW--KPY 305
Cdd:COG2182 167 ELIAAAKKLTAAGKYGLAYDAGD---------AYYFYPFLAAFGGYLFGKDGDDPkdvGLNSPGAVAALEYLKDLikDGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 306 TDPNTDGN----AFANGRVALSWVGHWMYPAYSKALGDDLVVLPLPDFGNG--PKTGQGSWAWGIGANSKNAKAAGTFLD 379
Cdd:COG2182 238 LPADADYDaadaLFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLAGGkpAKPFVGVKGFGVSAYSKNKEAAQEFAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 380 TLLNDTNVTAMTTANGAPPAtRSALAKSELYQRGGPLQLFADQLAKpcrdsdvtktcvAVTRPVTAGYPTVTAKFSDALN 459
Cdd:COG2182 318 YLTSPEAQKALFEATGRIPA-NKAAAEDAEVKADPLIAAFAEQAEY------------AVPMPNIPEMGAVWTPLGTALQ 384
|
410 420
....*....|....*....|.
gi 302464743 460 AIY-GGADPKGALEKAARAID 479
Cdd:COG2182 385 AIAsGKADPAEALDAAQKQIE 405
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
72-396 |
3.93e-51 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 177.93 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 72 CGGGSGAdvsAEAGSGKGAISVWAHQGQksESAALRKAVKSFNSSQHKIKVELKLIPTNDY-TKTITATDASKLPDVMEF 150
Cdd:COG1653 19 CGGGGSG---AAAAAGKVTLTVWHTGGG--EAAALEALIKEFEAEHPGIKVEVESVPYDDYrTKLLTALAAGNAPDVVQV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 151 DGPTMANFVYNKKLAPMDSYVSAKT--MSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGVKYPtnlsddWT 228
Cdd:COG1653 94 DSGWLAEFAAAGALVPLDDLLDDDGldKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP------KT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 229 ATEFTAALKALgtKDSDGKVvdlqensGYANEWGT-FGFAPVLWSAGGSLL-KDGKAegALDTPAALSAMKTLQSW--KP 304
Cdd:COG1653 168 WDELLAAAKKL--KAKDGVY-------GFALGGKDgAAWLDLLLSAGGDLYdEDGKP--AFDSPEAVEALEFLKDLvkDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 305 YTDPNTDG-------NAFANGRVALSWVGHWMYPAYSKALGD-DLVVLPLPDFGNGPKTGQ--GSWAWGIGANSKNAKAA 374
Cdd:COG1653 237 YVPPGALGtdwddarAAFASGKAAMMINGSWALGALKDAAPDfDVGVAPLPGGPGGKKPASvlGGSGLAIPKGSKNPEAA 316
|
330 340
....*....|....*....|..
gi 302464743 375 GTFLDTLLNDTNVTAMTTANGA 396
Cdd:COG1653 317 WKFLKFLTSPEAQAKWDALQAV 338
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
91-478 |
1.27e-49 |
|
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: 174.40 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWAHQGQKsESAALRKAVKSFNSSQHKIKVELKLIPTNDY--TKTITATDASKLPDVMEFDGPTMANFVYNKKLAPMD 168
Cdd:cd14748 2 ITFWHGMSGP-DGKALEELVDEFNKSHPDIKVKAVYQGSYDDtlTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 169 SYVSAK--TMSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGVKYPtnlSDDWTATEFTAALKALGTKDSDG 246
Cdd:cd14748 81 DYIDKDgvDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPE---KPPKTWDELEEAAKKLKDKGGKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 247 KVVDLqensGYANEWGTFGFAPVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQSW------KPYTDPNTDGNAFANGRV 320
Cdd:cd14748 158 GRYGF----ALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLvgkdgvSPLNDWGDAQDAFISGKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 321 ALSWVGHWMYPAY-SKALGDDLVVLPLPDFGNGPK-TGQGSWAWGIGAN-SKNAKAAGTFLDTLLNDTNVTAMTTANGAP 397
Cdd:cd14748 234 AMTINGTWSLAGIrDKGAGFEYGVAPLPAGKGKKGaTPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 398 PATRSALAKSELYQRGGP-LQLFADQLAKpcrdsdvtktcVAVTRPVTAGYPTVTAKFSDAL-NAIYGGADPKGALEKAA 475
Cdd:cd14748 314 PVRKSAAEDPEEFLAENPnYKVAVDQLDY-----------AKPWGPPVPNGAEIRDELNEALeAALLGKKTPEEALKEAQ 382
|
...
gi 302464743 476 RAI 478
Cdd:cd14748 383 EKI 385
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
93-478 |
7.97e-38 |
|
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: 142.43 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 93 VWAHQGQKSESAALRKAVKSFNSSQHKIKVELKLIP--TNDYTKTITATDASK--LPDVMEFDGPTMANFVYNKKLAPMD 168
Cdd:cd14750 3 TFAAGSDGQEGELLKKAIAAFEKKHPDIKVEIEELPasSDDQRQQLVTALAAGssAPDVLGLDVIWIPEFAEAGWLLPLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 169 SYVSAKTMSNATDAGKAQGEIDGKHYGLGMY-DAGLgVYGNKKLLDAAGVKYPTNlsddWTATEFTAALKALGTKDSDGK 247
Cdd:cd14750 83 EYLKEEEDDDFLPATVEANTYDGKLYALPWFtDAGL-LYYRKDLLEKYGPEPPKT----WDELLEAAKKRKAGEPGIWGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 248 VVdlqenSGYANEWGTFGFAPVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQSWK--PYTDPNTDG-------NAFANG 318
Cdd:cd14750 158 VF-----QGKQYEGLVCNFLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIgeGISPKGVLTygeeearAAFQAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 319 RVALSwvGHWMY-----PAYSKALGDDLVVLPLPDF-GNGPKTGQGSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTT 392
Cdd:cd14750 233 KAAFM--RNWPYayallQGPESAVAGKVGVAPLPAGpGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 393 ANGAPPaTRSALAKSELYQRGGP-LQLFADQLAKpcrdsdvtktcvAVTRPVTAGYPTVTAKFSDALN-AIYGGADPKGA 470
Cdd:cd14750 311 NGGLPP-TRRALYDDPEVLEAYPfLPALLEALEN------------AVPRPVTPKYPEVSTAIQIALSaALSGQATPEEA 377
|
....*...
gi 302464743 471 LEKAARAI 478
Cdd:cd14750 378 LKQAQEKL 385
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
90-480 |
7.00e-35 |
|
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: 134.36 E-value: 7.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 90 AISVWAhQGQKSESAALRKAVKSFNSSQHKIKVELKLIPTND-YTKTITATDASKLPDVMEFDGPTMANFVYNKKLAPMD 168
Cdd:cd14747 1 TLTVWA-MGNSAEAELLKELADEFEKENPGIEVKVQVLPWGDaHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 169 SYV-SAKTMSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGvkyPTNLSDDWTatEFTAALKALgtKDSDGK 247
Cdd:cd14747 80 PYLeDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAG---GDEAPKTWD--ELEAAAKKI--KADGPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 248 VVDLQENSGyANEWgtFGFAPVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQSW--KPYTDPNTDGN------AFANGR 319
Cdd:cd14747 153 VSGFAIPGK-NDVW--HNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLyqKGLSPKSTLENsadveqAFANGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 320 VALSWVGHWMYPA---YSKALGDDLVVLPLPDfgnGPKTGQGSWA----WGIGANSKNAKAAGTFLDTLLNDTNVTAMTT 392
Cdd:cd14747 230 VAMIISGPWEIGAireAGPDLAGKWGVAPLPG---GPGGGSPSFAggsnLAVFKGSKNKDLAWKFIEFLSSPENQAAYAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 393 ANGAPPATRSALAKSELYQRGGpLQLFADQLAKpcrdsdvtktcvAVTRPVTAGYPTVTAKFSDALNAIY--GGADPKGA 470
Cdd:cd14747 307 ATGMLPANTSAWDDPSLANDPL-LAVFAEQLKT------------GKATPATPEWGEIEAELVLVLEEVWigVGADVEDA 373
|
410
....*....|
gi 302464743 471 LEKAARAIDR 480
Cdd:cd14747 374 LDKAAAEINE 383
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
91-479 |
1.76e-31 |
|
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: 124.80 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWAHQGQKSESAALRKAVKSFNSSQHKIKVELKLIPTNDY-TKTITATDASKLPDVME-FDGPTMANFVYNKKLAPMD 168
Cdd:cd14749 2 ITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYkTKLKTAVAAGEGPDVFNlWPGGWLAEFVKAGLLLPLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 169 SYVSAKTMSNATDAGKAQGE-IDGKHYGLGMYDAGLGVYGNKKLLDAAG-VKYPTnlsddwTATEFTAALKALgtkDSDG 246
Cdd:cd14749 82 DYLDPNGVDKRFLPGLADAVtFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPK------TWDELIEAAKKD---KFKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 247 KVVdlqenSGYA----NEWGTFGFAPVLWSAGGSLLKD-GKAEGALDTPAALSAMKTLQS--WKPYTDPN-------TDG 312
Cdd:cd14749 153 KGQ-----TGFGlllgAQGGHWYFQYLVRQAGGGPLSDdGSGKATFNDPAFVQALQKLQDlvKAGAFQEGfegidydDAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 313 NAFANGRVALSWVGHWMYPAY--SKALGD-DLVVLPLPDFGNGPKTGQGS-WAWGIGANSKNAKAAGTFLDTLLNDTNVT 388
Cdd:cd14749 228 QAFAQGKAAMNIGGSWDLGAIkaGEPGGKiGVFPFPTVGKGAQTSTIGGSdWAIAISANGKKKEAAVKFLKYLTSPEVMK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 389 AMTTANGAPPATRSAlAKSELYQRGGPLQLFADQLAKPCRDSDVTKTcvavtrpvtagYPTVTAKFSDALNAIY-GGADP 467
Cdd:cd14749 308 QYLEDVGLLPAKEVV-AKDEDPDPVAILGPFADVLNAAGSTPFLDEY-----------WPAAAQVHKDAVQKLLtGKIDP 375
|
410
....*....|..
gi 302464743 468 KGALEKAARAID 479
Cdd:cd14749 376 EQVVKQAQSAAA 387
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
91-478 |
1.85e-30 |
|
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: 121.63 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWAHQGqkSESAALRKAVKSFNSsQHKIKVELKLIPTNDY-TKTITATDASKLPDVMEFDGPTMANFVYNKKLAPMDS 169
Cdd:cd13586 2 ITVWTDED--GELEYLKELAEEFEK-KYGIKVEVVYVDSGDTrEKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 170 YVsAKTMSNATDAGKAQgEIDGKHYGLGMYDAGLGVYGNKKLldaagVKYPTNLSDDwtateftaaLKALGTKDSDGKvv 249
Cdd:cd13586 79 YL-AVKIKNLPVALAAV-TYNGKLYGVPVSVETIALFYNKDL-----VPEPPKTWEE---------LIALAKKFNDKA-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 250 dlQENSGYANEWG-TFGFAPVLWSAGGSLLK---DGKAEGALDTPAALSAMKTLQSWK---PYTDPNTD----GNAFANG 318
Cdd:cd13586 141 --GGKYGFAYDQTnPYFSYPFLAAFGGYVFGengGDPTDIGLNNEGAVKGLKFIKDLKkkyKVLPPDLDydiaDALFKEG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 319 RVALSWVGHWMYPAYsKALGDDLVVLPLPDFGNG--PKTGQGSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANGA 396
Cdd:cd13586 219 KAAMIINGPWDLADY-KDAGINFGVAPLPTLPGGkqAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 397 PPATRSALAKSELYQRggP-LQLFADQLAkpcrdsdvtktcVAVTRPVTAGYPTVTAKFSDALNAIY-GGADPKGALEKA 474
Cdd:cd13586 298 IPALKDALNDAAVKND--PlVKAFAEQAQ------------YGVPMPNIPEMAAVWDAMGNALNLVAsGKATPEEAAKDA 363
|
....
gi 302464743 475 ARAI 478
Cdd:cd13586 364 VAAI 367
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
93-479 |
2.22e-29 |
|
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: 118.64 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 93 VWAHQGQKSESAALRKAVKSFNSSQHKIKVELKLIPTNDYT-KTITATDASKLPDVMEFDGPTMANFVYNKKLAPMDSYV 171
Cdd:cd14751 3 TFWHTSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHnQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 172 SAKTMSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGVKYPTnlsddwTATEF-TAALKALGTKDSDGKvvd 250
Cdd:cd14751 83 AFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPK------TMDELvAAAKAIKKKKGRYGL--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 251 lqensgYANEWGTFGFAPVLWSAGGSLLKDGKAEGALDTPA---ALSAMKTLQSWKPYTDPNTDG-----NAFANGRVAL 322
Cdd:cd14751 154 ------YISGDGPYWLLPFLWSFGGDLTDEKKATGYLNSPEsvrALETIVDLYDEGAITPCASGGypnmqDGFKSGRYAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 323 SWVGHWMYPAYSKAL----GDDLVVLPLPDFGNGPKTGQGSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANGAPP 398
Cdd:cd14751 228 IVNGPWAYADILGGKefkdPDNLGIAPVPAGPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 399 aTRSALAKSELYQRGGPLQLFADQLAKpcrdsdvtktcvAVTRPVTAGYPTVTAKFSDALNAIY-GGADPKGALEKAARA 477
Cdd:cd14751 308 -TRTSAYESPEVANNPMVAAFKPALET------------AVPRPPIPEWGELFEPLTLAFAKVLrGEKSPREALDEAAKQ 374
|
..
gi 302464743 478 ID 479
Cdd:cd14751 375 WD 376
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
91-478 |
2.53e-27 |
|
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: 112.89 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWaHQGQKSESAALRKAVKSFNSSQHKIKVELKLIPTNDYTK-TITATDASKLPDVMEFDGPTMANFVYNKKLAPMDS 169
Cdd:cd13522 2 ITVW-HQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQfFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 170 YVSaKTMSNATDAGKAQgEIDGKHYGLGMYDAGLGVYGNKKLLdaagVKYPTNLSDdwtatEFTAALKALGTKDSDGKVV 249
Cdd:cd13522 81 YVS-KSGKYAPNTIAAM-KLNGKLYGVPVSVGAHLMYYNKKLV----PKNPPKTWQ-----ELIALAQGLKAKNVWGLVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 250 DLQEnsgyanewgTFGFAPVLWSAGGSLLK--DGKAEGALDTPA---ALSAMKTLQSWKPYTDPNTDGN----AFANGRV 320
Cdd:cd13522 150 NQNE---------PYFFAAWIGGFGGQVFKanNGKNNPTLDTPGaveALQFLVDLKSKYKIMPPETDYSiadaLFKAGKA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 321 ALSWVGHWMYPAYSKALGDDLVVLPLPDFGNG--PKTGQGSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANGAPP 398
Cdd:cd13522 221 AMIINGPWDLGDYRQALKINLGVAPLPTFSGTkhAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 399 ATRSALaKSELYQRGGPLQLFADQLAkpcrdsdvtktcVAVTRPVTAGYPTVTAKFSDALNAIYGG-ADPKGALEKAARA 477
Cdd:cd13522 301 ANLQAY-ESPAVQNKPAQKASAEQAA------------YGVPMPNIPEMRAVWDAFRIAVNSVLAGkVTPEAAAKDAQQE 367
|
.
gi 302464743 478 I 478
Cdd:cd13522 368 A 368
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
91-478 |
1.70e-24 |
|
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: 104.77 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWaHQGQKSESAALRKAVKSFNSSQHKIKVELKL-IPTNDYTKTITATDASKLPDVMEFDGPTMANFVYNKKLAPMDS 169
Cdd:cd13657 2 ITIW-HALTGAEEDALQQIIDEFEAKYPVPNVKVPFeKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 170 YVSAKTMSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAgvkyPTnlsddwTATEFTAALKALGTKDSDgkvv 249
Cdd:cd13657 81 YLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQP----PE------TTDELLAIMKDHTDPAAG---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 250 dlqeNSGYANEWGTFGF-APVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQSW-KPYTDPNTDGN----AFANGRVALS 323
Cdd:cd13657 147 ----SYGLAYQVSDAYFvSAWIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFsWPYMPSDPSYNtqtsLFNEGKAAMI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 324 WVGHWMYpAYSKALGDDLVVLPLPDFG--NGPKTGQGSWAWGI--GANSKNAKAAGTFLDTLLNDTNVTAMTTANGAPPA 399
Cdd:cd13657 223 INGPWFI-GGIKAAGIDLGVAPLPTVDgtNPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 400 TRSALAKSELyqRGGP-LQLFADQLAKpcrdsdvtktcvAVTRPVTagyPTVTAKFS---DALNAIY-GGADPKGALEKA 474
Cdd:cd13657 302 ATNAYDDAEV--AADPvIAAFKAQAEH------------GVPMPNS---PEMASVWGpvtLALAAVYqGGQDPQEALAAA 364
|
....
gi 302464743 475 ARAI 478
Cdd:cd13657 365 QQEI 368
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
98-384 |
6.44e-20 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 90.17 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 98 GQKSESAALRKAVKSFNSSQHKIKVELKLIPTNDY-TKTITATDASKLP-DVMEFDGPTMANFVYNKKLAPMDSYVSAKT 175
Cdd:pfam01547 2 ASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLaQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 176 msnatdagkaqGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGVKYPtnlsddWTATEFTAALKALGTKDSDGKVVDLQENS 255
Cdd:pfam01547 82 -----------VLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP------KTWDELLEAAKKLKEKGKSPGGAGGGDAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 256 GyanEWGTFGFAPVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQS-------WKPYTDPNTDGN----AFANGRVALSW 324
Cdd:pfam01547 145 G---TLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAkvlllkkLKNPGVAGADGRealaLFEQGKAAMGI 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302464743 325 VGHWMYPAYSKALGDDLVVLPLPDFGN---------GPKTGQGSWAWGIGANSKNAKAAGTFLDTLLND 384
Cdd:pfam01547 222 VGPWAALAANKVKLKVAFAAPAPDPKGdvgyaplpaGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
108-405 |
9.16e-20 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 89.39 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 108 KAVKSFNSsQHKIKVELKLIPTNDY-TKTITATDASKLPDVM--EFDGPTMANFVYNKKLAPMDSYVSAKTMSNATDAGK 184
Cdd:pfam13416 1 ALAKAFEK-KTGVTVEVEPQASNDLqAKLLAAAAAGNAPDLDvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 185 aqgeIDGKHYGLG-MYDAGLGVYGNKKLLDAAGvkyptnlSDDWTATEFTAALKALgtkdsDGKVvdlqensGYANeWGT 263
Cdd:pfam13416 80 ----YDGKLYGVPyAASTPTVLYYNKDLLKKAG-------EDPKTWDELLAAAAKL-----KGKT-------GLTD-PAT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 264 FGFAPVLWSAGGSLLKDGKaeGALDTPAALSAMKTLQSWKPYTDPNTDGNA-FANGRVALSWVGHWMYPAYSKAlGDDLV 342
Cdd:pfam13416 136 GWLLWALLADGVDLTDDGK--GVEALDEALAYLKKLKDNGKVYNTGADAVQlFANGEVAMTVNGTWAAAAAKKA-GKKLG 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302464743 343 VLPLPDfgngpKTGQGSWAWGIGANSKNA-KAAGTFLDTLLNDTNVTAMTTANGAPPATRSALA 405
Cdd:pfam13416 213 AVVPKD-----GSFLGGKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSAAL 271
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
120-386 |
3.33e-17 |
|
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: 83.92 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 120 IKVELKLIPTNDYTKTITATDAS-KLPDVM-EFDGPTMANFVYNKKLAPMDSYV---SAKTMSNATDAGKAQGEIDGKHY 194
Cdd:cd13580 34 IDVKVKWVPDSSYDEKLNLALASgDLPDIVvVNDPQLSITLVKQGALWDLTDYLdkyYPNLKKIIEQEGWDSASVDGKIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 195 GLGMYDA---GLGVYGNKKLLDAAGVKYPTNLsddwtaTEFTAALKALGTKDSDGKvvDLQENSGYA--NEWGTFGFAPV 269
Cdd:cd13580 114 GIPRKRPligRNGLWIRKDWLDKLGLEVPKTL------DELYEVAKAFTEKDPDGN--GKKDTYGLTdtKDLIGSGFTGL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 270 LWSAGGS-----LLKDGKAEGALDTPAALSAMKTLQSW--KPYTDP----NTDGNA---FANGRVALsWVGHWMYPAY-- 333
Cdd:cd13580 186 FGAFGAPpnnwwKDEDGKLVPGSIQPEMKEALKFLKKLykEGLIDPefavNDGTKAnekFISGKAGI-FVGNWWDPAWpq 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302464743 334 ----SKALGDDLVVLPLP-----DFGNGPKTGQGSWaWGIGANSKNAKAAGTFLDTLLNDTN 386
Cdd:cd13580 265 aslkKNDPDAEWVAVPIPsgpdgKYGVWAESGVNGF-FVIPKKSKKPEAILKLLDFLSDPEV 325
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
91-478 |
2.07e-13 |
|
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270376 [Multi-domain] Cd Length: 372 Bit Score: 71.75 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWAHQGQKSESaaLRKAVKSFnSSQHKIKVELKLIPTNDYTKTITATD-ASKLPDVMEFDGPTMANFVYNKKLAPMDs 169
Cdd:cd13658 2 LTVWVDEDKKMAF--IKKIAKQY-TKKTGVKVKLVEVDQLDQLEKLSLDGpAGKGPDVMVAPHDRIGSAVLQGLLSPIK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 170 yVSAKTMSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAgvkyPTNLsDDWTAteftaalKALGTKDSDGKvv 249
Cdd:cd13658 78 -LSKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA----PKTF-DELEA-------LAKDLTKEKGK-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 250 dlqeNSGYANEWGTFGFA-PVLWSAGGSLLKDGKAEG-----ALDTPAALSAMKTLQSW--KPYTDPNTDGNA----FAN 317
Cdd:cd13658 143 ----QYGFLADATNFYYSyGLLAGNGGYIFKKNGSDLdindiGLNSPGAVKAVKFLKKWytEGYLPKGMTGDViqglFKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 318 GRVALSWVGHWMYPAYsKALGDDLVVLPLPDFGNG--PKTGQGSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANG 395
Cdd:cd13658 219 GKAAAVIDGPWAIQEY-QEAGVNYGVAPLPTLPNGkpMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 396 APPAtRSALAKSELYQRGGPLQLFADQLAKpcrdsdvtktcvAVTRPvtaGYPTVTAKFSDALNAIY----GGADPKGAL 471
Cdd:cd13658 298 EIPP-RKDVRSDPEIKNNPLTSAFAKQASR------------AVPMP---NIPEMGAVWEPANNALFfilsGKKTPKQAL 361
|
....*..
gi 302464743 472 EKAARAI 478
Cdd:cd13658 362 NDAVNDI 368
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
91-408 |
6.47e-11 |
|
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: 63.90 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 91 ISVWAHQGQKsesAALRKAVKSFNSSQHKIKVELKLIPTNDYT-KTITATDASKLPDVMEFDGPTMANFVYNKKLAPMDS 169
Cdd:cd13655 2 LTVWGPQEDQ---EWLKEMVDAFKEKHPEWKITITIGVVGEADaKDEVLKDPSAAADVFAFANDQLGELVDAGAIYPLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 170 YVSAKTMSNATDAGKAQGEIDGKHYGLGMYDAGLGVYGNKKLLDAAGVKyptnlsddwTATEFTAALKALGTKdsdgkvV 249
Cdd:cd13655 79 SAVDKIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVK---------SLDTMLAKAPDAKGK------V 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 250 DLQENSGYAnewgtfgFAPVLWSAGGSL-LKDGKAEGALDT-----PAALSAMKTLQSWKPYTDpNTDGNA---FANGRV 320
Cdd:cd13655 144 SFDLSNSWY-------LYAFFFGAGCKLfGNNGGDTAGCDFnnekgVAVTNYLVDLVANPKFVN-DADGDAisgLKDGTL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 321 ALSWVGHWMYPAYSKALGDDLVVLPLPDFGNGPKTGQ-----GSWAWGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANG 395
Cdd:cd13655 216 GAGVSGPWDAANLKKALGDNYAVAKLPTYTLGGKDVQmksfaGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRG 295
|
330
....*....|...
gi 302464743 396 APPATRSALAKSE 408
Cdd:cd13655 296 IGPTNKEAAESDA 308
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
117-405 |
1.23e-04 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 44.13 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 117 QHKIKVELKLIPTND--YTKtITATDASklPDVMEFDGPTMANFVYNKKLAPMDsyVSA-KTMSNATDAGKAQGEIDGKH 193
Cdd:COG0687 51 ETGIKVVYDTYDSNEemLAK-LRAGGSG--YDVVVPSDYFVARLIKAGLLQPLD--KSKlPNLANLDPRFKDPPFDPGNV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 194 YGLG-MYDA-GLGVygNKKLLDAAgvkyPTNLSDDWTAteftaALKalgtkdsdGKVvdlqenSGYANEWGTFGFApvLW 271
Cdd:COG0687 126 YGVPyTWGTtGIAY--NTDKVKEP----PTSWADLWDP-----EYK--------GKV------ALLDDPREVLGAA--LL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 272 SAGGSLLKDGKAEgaLDTpaalsAMKTLQSWKP-----YTDPNTDGNAFANGRVALSWVghWMYPAYS-KALGDDLVVLP 345
Cdd:COG0687 179 YLGYDPNSTDPAD--LDA-----AFELLIELKPnvrafWSDGAEYIQLLASGEVDLAVG--WSGDALAlRAEGPPIAYVI 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302464743 346 lpdfgngPKTGQGSWA--WGIGANSKNAKAAGTFLDTLLNDTNVTAMTTANGAPPATRSALA 405
Cdd:COG0687 250 -------PKEGALLWFdnMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARE 304
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
120-302 |
1.21e-03 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270299 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 120 IKVELKLIPTNDYTKTITATDASK-LPDVMEFDGPTMANFVYNKK---LAPMDSYVSAKT------MSNATDAGKAQGEI 189
Cdd:cd13581 32 IKIEWETVPEDAWAEKKNLMLASGdLPDAFLGAGASDADLMTYGKqglFLPLEDLIDKYApnlkalFDENPDIKAAITAP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302464743 190 DGKHYGLGMYDA-GLGVYG-----NKKLLDAAGVKYPTnlsddwTATEFTAALKALGTKDSDGK-VVDLQENSGYANEWG 262
Cdd:cd13581 112 DGHIYALPSVNEcYHCSYGqrmwiNKKWLDKLGLEMPT------TTDELYEVLKAFKEQDPNGNgKADEIPLSFSGLNGG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 302464743 263 T---------FGFAPVLWSAGGSLLKDGKAEGALDTPAALSAMKTLQSW 302
Cdd:cd13581 186 TddpafllnsFGINDGGYGGYGFVVKDGKVIYTATDPEYKEALAYLNKL 234
|
|
| |
