|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
44-342 |
2.49e-55 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 187.94 E-value: 2.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 44 TGTPSASAKGEITIWNRSGDLFKVFDAAIDAFRKAYPDIKVNHQAV---DIDAKLANTLISGtDLPDGSFWDDAKIG--G 118
Cdd:COG1653 24 SGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVpydDYRTKLLTALAAG-NAPDVVQVDSGWLAefA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 119 QAEHLYDLTDLIAPYRDKTSAYK---LSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPAglKTYDDLLAAARSLRE 195
Cdd:COG1653 103 AAGALVPLDDLLDDDGLDKDDFLpgaLDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--KTWDELLAAAKKLKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 196 KNPKArPLHMEKDPflGQLWLEMLAgQQGTSLADADGQVRLDSKEYRNILNWVRDAVDDDLV--THAEYLKQADLAALEN 273
Cdd:COG1653 181 KDGVY-GFALGGKD--GAAWLDLLL-SAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDGYVppGALGTDWDDARAAFAS 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389008600 274 GQQALVPWAVWwsFAPQQLLKKGKGKWRAAPLPAWTPGGARSGAMGGSSFIIPAKAKNPELAWLLYEFL 342
Cdd:COG1653 257 GKAAMMINGSW--ALGALKDAAPDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFL 323
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
54-445 |
1.33e-53 |
|
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: 183.76 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWNRSGDLF-KVFDAAIDAFRKAYPDIKVNHQAVD---IDAKLaNTLISGTDLPDGSFWDDAKIGGQAE--HLYDLT 127
Cdd:cd13585 1 TLTFWDWGQPAEtAALKKLIDAFEKENPGVKVEVVPVPyddYWTKL-TTAAAAGTAPDVFYVDGPWVPEFASngALLDLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 128 DLIAPYRDKTSAYK--LSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPAGLKTYDDLLAAARSLREKNPKARPLHM 205
Cdd:cd13585 80 DYIEKDGLDDDFPPglLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 206 EKDPFLGQLWLEMLAGQQGTSLADADGQVRLDSKEYRNILNWVRDAVDDDLVTHAEYLKQAD-LAALENGQQALVPWAVW 284
Cdd:cd13585 160 RGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEaVDLFASGKVAMMIDGPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 285 wsFAPQQLLKKGKGKWRAAPLPAWtPGGARSGAMGGSSFIIPAKAKNPELAWLLYEFLCFKEPGYSAVYGPSEVYPGGLT 364
Cdd:cd13585 240 --ALGTLKDSKVKFKWGVAPLPAG-PGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 365 TSVPSYGPArrpdkplfepvaalggQDLWKVAVDAADTIPSAAPIPAWWAKSVDYLGNNLQRLIEGKMA--PDDVIDDST 442
Cdd:cd13585 317 ASAAAPDAK----------------PALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGksPEEALKEAA 380
|
...
gi 1389008600 443 KKI 445
Cdd:cd13585 381 KEI 383
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
54-445 |
6.87e-39 |
|
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: 144.74 E-value: 6.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWN-RSGDLFKVFDAAIDAFRKAYPDIKVNHQAVDIDAKLANTL---ISGTDLPDGSFWDDAKIGGQAE--HLYDLT 127
Cdd:cd14748 1 EITFWHgMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLlaaLAAGTAPDVAQVDASWVAQLADsgALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 128 DLIAPYRDKTSAY---KLSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPAGL-KTYDDLLAAARSLREKNPKARPL 203
Cdd:cd14748 81 DYIDKDGVDDDDFypaALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPpKTWDELEEAAKKLKDKGGKTGRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 204 HMEKDPFLGQLWLEMLAGQQGTSLADAD-GQVRLDSKEYRNILNWVRDAVDDDLVTHAEYLKQADlAALENGQQALV--- 279
Cdd:cd14748 161 GFALPPGDGGWTFQALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQ-DAFISGKVAMTing 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 280 PWAVwwsfapQQLLKKGKG-KWRAAPLPAWTpGGARSGAMGGSSFIIPAK-AKNPELAWLLYEFLCFKEpgysavygpse 357
Cdd:cd14748 240 TWSL------AGIRDKGAGfEYGVAPLPAGK-GKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPE----------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 358 vypGGLTTSVPSYGPARRPDkPLFEPVAALGGQDLWKVAVDAADTIPSAAPIPAWWAKSVDYLGNNLQRLIEGKMAPDDV 437
Cdd:cd14748 302 ---NQAKWAKATGYLPVRKS-AAEDPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEA 377
|
....*...
gi 1389008600 438 IDDSTKKI 445
Cdd:cd14748 378 LKEAQEKI 385
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
66-342 |
2.79e-37 |
|
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: 140.12 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 66 KVFDAAIDAFRKAYPDIKVNHQAVDIDA-----KLANTLISGTDLPDGSFWDDAKIGGQAEHLY--DLTDLIAP-YRDKT 137
Cdd:cd14750 14 ELLKKAIAAFEKKHPDIKVEIEELPASSddqrqQLVTALAAGSSAPDVLGLDVIWIPEFAEAGWllPLTEYLKEeEDDDF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 138 SAYKLSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPagLKTYDDLLAAARSLREKNPKARPLHMEKDPFLG--QLW 215
Cdd:cd14750 94 LPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEP--PKTWDELLEAAKKRKAGEPGIWGYVFQGKQYEGlvCNF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 216 LEMLAGQQGTSLADADGQVRLDSKEYRNILNWVRDAVDDDLVTHA--EYLKQADLAALENGQQALV---PWAVWwsfAPQ 290
Cdd:cd14750 172 LELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPKGvlTYGEEEARAAFQAGKAAFMrnwPYAYA---LLQ 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1389008600 291 QLLKKGKGKWRAAPLPAWtPGGARSGAMGGSSFIIPAKAKNPELAWLLYEFL 342
Cdd:cd14750 249 GPESAVAGKVGVAPLPAG-PGGGSASTLGGWNLAISANSKHKEAAWEFVKFL 299
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
54-449 |
5.98e-31 |
|
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: 122.81 E-value: 5.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWNRSGDLF-KVFDAAIDAFRKAYPDIKVNHQAV---DIDAKLAnTLISGTDLPD----GSFW--DDAKIGGqaehL 123
Cdd:cd14747 1 TLTVWAMGNSAEaELLKELADEFEKENPGIEVKVQVLpwgDAHTKIT-TAAASGDGPDvvqlGNTWvaEFAAMGA----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 124 YDLTDLIAPYRDKTSAYKLSVN--TVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPAgLKTYDDLLAAARSLREKNPKAR 201
Cdd:cd14747 76 EDLTPYLEDLGGDKDLFPGLVDtgTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEA-PKTWDELEAAAKKIKADGPDVS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 202 PLHMEKDPFLGQLWLEMLAGQQGTSLADADGQVRLDSKEYRNILNWVRDAVDDDLVTHAEYLKQADL-AALENGQQALVP 280
Cdd:cd14747 155 GFAIPGKNDVWHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVeQAFANGKVAMII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 281 WAVWWSFAPQQLLKKGKGKWRAAPLPAwTPGGARSGAMGGSSFIIPAKAKNPELAWLLYEFLCFKEpGYSAVYGPSEVYP 360
Cdd:cd14747 235 SGPWEIGAIREAGPDLAGKWGVAPLPG-GPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPE-NQAAYAKATGMLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 361 GglTTSVpsygparrPDKPLFEPvaalggQDLWKVAVDAADTIPSAAPIPAwWAKSVDYLGNNLQRLIEGKMA-PDDVID 439
Cdd:cd14747 313 A--NTSA--------WDDPSLAN------DPLLAVFAEQLKTGKATPATPE-WGEIEAELVLVLEEVWIGVGAdVEDALD 375
|
410
....*....|
gi 1389008600 440 DSTKKIQRNL 449
Cdd:cd14747 376 KAAAEINEIL 385
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
37-449 |
3.90e-27 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 112.35 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 37 GSEPRKLTGTPSASAKGEITIWNRSGDLfKVFDAAIDAFRKAyPDIKVNHQAV---DIDAKLANTLISGtDLPDGSFWDD 113
Cdd:COG2182 23 GSGSSSSGSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEE-PGIKVKVVEVpwdDLREKLTTAAPAG-KGPDVFVGAH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 114 AKIGG--QAEHLYDLTDLIAPyRDKTSAYKLSVNTVDGRIYGVPWDLDPGLLWYREDLLEDagvDPAglKTYDDLLAAAR 191
Cdd:COG2182 100 DWLGElaEAGLLAPLDDDLAD-KDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA---EPP--KTWDELIAAAK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 192 SLREKNPKarPLHME-KDPFlgqlWLEMLAGQQGTSLADADG----QVRLDSKEYRNILNWVRDAVDDDLV-------TH 259
Cdd:COG2182 174 KLTAAGKY--GLAYDaGDAY----YFYPFLAAFGGYLFGKDGddpkDVGLNSPGAVAALEYLKDLIKDGVLpadadydAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 260 AEYLKQADLAALENGqqalvPWAVwwsfapqQLLKKGKG-KWRAAPLPAwTPGGARSGAM-GGSSFIIPAKAKNPELAWL 337
Cdd:COG2182 248 DALFAEGKAAMIING-----PWAA-------ADLKKALGiDYGVAPLPT-LAGGKPAKPFvGVKGFGVSAYSKNKEAAQE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 338 LYEFLCFKEpGYSAVYgpsEVYPgglttsvpsYGPARrpdKPLFEpVAALGGQDLWKVAVDAADTipsAAPIPAW--WAK 415
Cdd:COG2182 315 FAEYLTSPE-AQKALF---EATG---------RIPAN---KAAAE-DAEVKADPLIAAFAEQAEY---AVPMPNIpeMGA 374
|
410 420 430
....*....|....*....|....*....|....
gi 1389008600 416 SVDYLGNNLQRLIEGKMAPDDVIDDSTKKIQRNL 449
Cdd:COG2182 375 VWTPLGTALQAIASGKADPAEALDAAQKQIEAAI 408
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
54-446 |
5.18e-25 |
|
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: 105.92 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWNRS--GDLFKVFDAAIDAFRKAYPDIKVNHQAV--DIDAKLANTLISGTDLPD------GSFWDDAKIGGQaehL 123
Cdd:cd14749 1 TITYWQYFtgDTKKKYMDELIADFEKENPNIKVKVVVFpyDNYKTKLKTAVAAGEGPDvfnlwpGGWLAEFVKAGL---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 124 YDLTDLIAPYRDKTSAYKLSVN--TVDGRIYGVPWDLDPGLLWYREDLLEDAG-VDPAglKTYDDLLAAARSLREKNPKA 200
Cdd:cd14749 78 LPLTDYLDPNGVDKRFLPGLADavTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPP--KTWDELIEAAKKDKFKAKGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 201 RPLHMEKDPFLGQLWLEMLAGQQGTSLADADGQVRLDSKEYRNI--LNWVRDAVDDDLVTHA--EYLKQADLAALENGQQ 276
Cdd:cd14749 156 TGFGLLLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFNDPAFVqaLQKLQDLVKAGAFQEGfeGIDYDDAGQAFAQGKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 277 ALVPWAVWWSFApqqlLKKG--KGKWRAAPLPAwTPGGARSGAMGGSSFI--IPAKAKNPELAWLLYEFLCFKEPG--YS 350
Cdd:cd14749 236 AMNIGGSWDLGA----IKAGepGGKIGVFPFPT-VGKGAQTSTIGGSDWAiaISANGKKKEAAVKFLKYLTSPEVMkqYL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 351 AVYGPSEVYPGGLTTSVPSygparrpdkplfePVAALGGQDLWkvavdaadtIPSAAPIPAW---WAKSVDYLGNNLQRL 427
Cdd:cd14749 311 EDVGLLPAKEVVAKDEDPD-------------PVAILGPFADV---------LNAAGSTPFLdeyWPAAAQVHKDAVQKL 368
|
410
....*....|....*....
gi 1389008600 428 IEGKMAPDDVIDDSTKKIQ 446
Cdd:cd14749 369 LTGKIDPEQVVKQAQSAAA 387
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
68-342 |
1.49e-22 |
|
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: 97.10 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 68 FDAAIDAFRKAYPDIKVNHQAVDIDA---KLANTLISGTDLPDGSFWDDAKIGGQAE--HLYDLTDLIAPYrdktsaykl 142
Cdd:pfam01547 10 LQALVKEFEKEHPGIKVEVESVGSGSlaqKLTTAIAAGDGPADVFASDNDWIAELAKagLLLPLDDYVANY--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 143 sVNTVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPAglKTYDDLLAAARSLREKNPKARPLHMEKDPFLGQLWLEMLAGQ 222
Cdd:pfam01547 81 -LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP--KTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 223 QGTSLADADGQvRLDSKEYRNILNWVRDAVDDDLVTH-------AEYLKQADLAALENGQQALVPWAVWWSFAPQQLLKK 295
Cdd:pfam01547 158 LGGPLFDKDGG-GLDNPEAVDAITYYVDLYAKVLLLKklknpgvAGADGREALALFEQGKAAMGIVGPWAALAANKVKLK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389008600 296 G---------KGKWRAAPLPAWTPGGArsgamGGSSFIIPAKAKNPELAWLLYEFL 342
Cdd:pfam01547 237 VafaapapdpKGDVGYAPLPAGKGGKG-----GGYGLAIPKGSKNKEAAKKFLDFL 287
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
55-445 |
1.04e-19 |
|
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: 90.52 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 55 ITIWNRSGDLFKV-FDAAIDAFRKAYPDIKVNHQAVDIDaKLAN---TLISGTDLPD----GSFW--DDAKIGgqaeHLY 124
Cdd:cd14751 2 ITFWHTSSDEEKVlYEKLIPAFEKEYPKIKVKAVRVPFD-GLHNqikTAAAGGQAPDvmraDIAWvpEFAKLG----YLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 125 DLTDLiaPYRDKTSAY---KLSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAGVDPAglKTYDDLLAAARSLREKNPKAR 201
Cdd:cd14751 77 PLDGT--PAFDDIVDYlpgPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIKKKKGRYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 202 PLHMEKDP--FLGQLWLEmlagqqGTSLADADGQ-VRLDSKE----YRNILNWVRDAV-----DDDLVTHAEYLKQADLA 269
Cdd:cd14751 153 LYISGDGPywLLPFLWSF------GGDLTDEKKAtGYLNSPEsvraLETIVDLYDEGAitpcaSGGYPNMQDGFKSGRYA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 270 ALENGqqalvPWAV-----WWSFAPqqllkkgKGKWRAAPLPAwTPGGARSgAMGGSSFIIPAKAKNPELAWLLYEFLCF 344
Cdd:cd14751 227 MIVNG-----PWAYadilgGKEFKD-------PDNLGIAPVPA-GPGGSGS-PVGGEDLVIFKGSKNKDAAWKFVKFMSS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 345 KEPGYSAVYGpsevyPGGLTTSVPSYGPARRPDKPLFEPVaalggqdlwkvaVDAADTIPSAAPIPAwWAKSVDYLGNNL 424
Cdd:cd14751 293 AEAQALTAAK-----LGLLPTRTSAYESPEVANNPMVAAF------------KPALETAVPRPPIPE-WGELFEPLTLAF 354
|
410 420
....*....|....*....|.
gi 1389008600 425 QRLIEGKMAPDDVIDDSTKKI 445
Cdd:cd14751 355 AKVLRGEKSPREALDEAAKQW 375
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
55-342 |
2.53e-17 |
|
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: 83.23 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 55 ITIWNRSGDL-FKVFDAAIDAFRKAYPDIKVN--HQAVDIDAKLANTLISGTDLPDGSFWDDAKIGGQAEH--LYDLTDL 129
Cdd:cd13522 2 ITVWHQYDTGeNQAVNELIAKFEKAYPGITVEvtYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAglLAPLDEY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 130 IAPYRDKTSAYKLSVnTVDGRIYGVPWDLDPGLLWYREDLLEDagvDPAglKTYDDLLAAArsLREKNPKARPL-HMEKD 208
Cdd:cd13522 82 VSKSGKYAPNTIAAM-KLNGKLYGVPVSVGAHLMYYNKKLVPK---NPP--KTWQELIALA--QGLKAKNVWGLvYNQNE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 209 PFLGQLWLEMLAGQQGTSlADADGQVRLDSKEYRNILNWVRDAVDDDLVTHAE-YLKQADlAALENGQQALV---PWAvw 284
Cdd:cd13522 154 PYFFAAWIGGFGGQVFKA-NNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPEtDYSIAD-ALFKAGKAAMIingPWD-- 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389008600 285 WSFAPQQLlkkgKGKWRAAPLPAWtPGGARSGAM-GGSSFIIPAKAKNPELAWLLYEFL 342
Cdd:cd13522 230 LGDYRQAL----KINLGVAPLPTF-SGTKHAAPFvGGKGFGINKESQNKAAAVEFVKYL 283
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
82-354 |
4.37e-14 |
|
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: 73.90 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 82 IKVNHQAVDIDA---KLANTLISGtDLPDGSFWDDAKIGGQAEH---LYDLTDLIAPYRDKTSAY-----KLSVnTVDGR 150
Cdd:cd13580 34 IDVKVKWVPDSSydeKLNLALASG-DLPDIVVVNDPQLSITLVKqgaLWDLTDYLDKYYPNLKKIieqegWDSA-SVDGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 151 IYGVP--WDL-DPGLLWYREDLLEDAGVDPagLKTYDDLLAAARSLREKNP----KARP--LHMEKDPFLGqlWLEMLAG 221
Cdd:cd13580 112 IYGIPrkRPLiGRNGLWIRKDWLDKLGLEV--PKTLDELYEVAKAFTEKDPdgngKKDTygLTDTKDLIGS--GFTGLFG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 222 QQGTS----LADADGQVRLDS--KEYRNILNWVRDAVDDDLVTHaEYL--KQADL-AALENGQQALV--PWavWWSFAPQ 290
Cdd:cd13580 188 AFGAPpnnwWKDEDGKLVPGSiqPEMKEALKFLKKLYKEGLIDP-EFAvnDGTKAnEKFISGKAGIFvgNW--WDPAWPQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389008600 291 QLLKKG--KGKWRAAPLPAWTPG--GARSGAMGGSSFIIPAKAKNPELAWLLYEFLCFKEPGYSAVYG 354
Cdd:cd13580 265 ASLKKNdpDAEWVAVPIPSGPDGkyGVWAESGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQKLLDYG 332
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
54-342 |
4.54e-13 |
|
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: 70.40 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWNRSGDLFKVFDAAIDAFRKAYpDIKVNHQAVDIDAKLANTLI--SGTDLPDGSFW--DDAKIGGQAEHLYDLTDL 129
Cdd:cd13586 1 TITVWTDEDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITagPAGKGPDVFFGphDWLGELAAAGLLAPIPEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 130 IAPyRDKTSAYKLSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAgvdPaglKTYDDLLAAARSLREKNPKARPLHME-KD 208
Cdd:cd13586 80 LAV-KIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEP---P---KTWEELIALAKKFNDKAGGKYGFAYDqTN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 209 PFLGQLWLemlaGQQGTSLADADG----QVRLDSKEYRNILNWVRDAVDDDLVTHAEYLKQADLAALENGQQALV---PW 281
Cdd:cd13586 153 PYFSYPFL----AAFGGYVFGENGgdptDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKAAMIingPW 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389008600 282 AVwwsfapqQLLKKGKGKWRAAPLPAwTPGGARSGAMGGS-SFIIPAKAKNPELAWLLYEFL 342
Cdd:cd13586 229 DL-------ADYKDAGINFGVAPLPT-LPGGKQAAPFVGVqGAFVSAYSKNKEAAVEFAEYL 282
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
70-346 |
9.16e-13 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 68.59 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 70 AAIDAFRKAYpDIKVNHQAV---DIDAKLANTLISGTDLPDGSFW---DDAKIGGQAEHLYDLTDLiaPYRDKTSAYKLS 143
Cdd:pfam13416 1 ALAKAFEKKT-GVTVEVEPQasnDLQAKLLAAAAAGNAPDLDVVWiaaDQLATLAEAGLLADLSDV--DNLDDLPDALDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 144 VnTVDGRIYGVPWDLD-PGLLWYREDLLEDAGVDPaglKTYDDLLAAArslrEKNPKARPLHmekDPFLGqlWLEMLAGQ 222
Cdd:pfam13416 78 A-GYDGKLYGVPYAAStPTVLYYNKDLLKKAGEDP---KTWDELLAAA----AKLKGKTGLT---DPATG--WLLWALLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 223 QGTSLaDADGQVRLDSKEYRNILNWVRDAVD----DDLVTHAeyLKQADLAALENGqqalvPWAVwwsfapqQLLKKGKG 298
Cdd:pfam13416 145 DGVDL-TDDGKGVEALDEALAYLKKLKDNGKvyntGADAVQL--FANGEVAMTVNG-----TWAA-------AAAKKAGK 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1389008600 299 KWRAAPLpawtPGGARSgamGGSSFIIPAKAKNPEL-AWLLYEFLCFKE 346
Cdd:pfam13416 210 KLGAVVP----KDGSFL---GGKGLVVPAGAKDPRLaALDFIKFLTSPE 251
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
81-451 |
2.94e-11 |
|
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: 65.03 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 81 DIKVNHQAVDIDA---KLANTLISGtDLPD---GSFW--DDAKIGGQAEHLYDLTDLIAPYR-------DKTSAYKLSVN 145
Cdd:cd13581 31 GIKIEWETVPEDAwaeKKNLMLASG-DLPDaflGAGAsdADLMTYGKQGLFLPLEDLIDKYApnlkalfDENPDIKAAIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 146 TVDGRIYGVPWD------LDPGLLWYREDLLEDAGVD-PaglKTYDDLLAAARSLREKNP------KARPLHMEKDPFLG 212
Cdd:cd13581 110 APDGHIYALPSVnecyhcSYGQRMWINKKWLDKLGLEmP---TTTDELYEVLKAFKEQDPngngkaDEIPLSFSGLNGGT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 213 QL--WL-----EMLAGQQGTSLADADGQVR--LDSKEYRNILNWVRDAVDDDLVtHAEYLKQAD--LAALENGQQALVPW 281
Cdd:cd13581 187 DDpaFLlnsfgINDGGYGGYGFVVKDGKVIytATDPEYKEALAYLNKLYKEGLI-DPEAFTQDYdqLAAKGKASTAKVGV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 282 AVWWSfapqQLLKKGKGKWRA-APLPAWT-PGGAR------SGAMGGSSFIIPAKAKNPELA--WLLYeflcFKEPGYSA 351
Cdd:cd13581 266 FFGWD----PGLFFGEERYEQyVPLPPLKgPNGDQlawvgnSSGYGRGGFVITSKNKNPEAAirWADF----LYSPEGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 352 -----VYGPSEVYPGGlttsvpsyGPARRPDKPLFEPVAALGGqdlWKVAVDAADTIPSAAP-------IPAWWAKSVDY 419
Cdd:cd13581 338 qanfgPEGEDWEKNPD--------GEYGVDGPPAAYKILEPSE---GEQNVAWADGGPGAIPdeyrlkqVTDEDMDEAEA 406
|
410 420 430
....*....|....*....|....*....|....*..
gi 1389008600 420 LGNNLQRLIEGKMAPDDV-----IDDSTKKIQRNLVD 451
Cdd:cd13581 407 RLDEAKKYYEPYAPPDNSpppalLDEEAEKISTIQTD 443
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
54-449 |
3.14e-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: 64.81 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWNRSGDLFKVFDAAIDAFRKAYpDIKVNHQAVDIDAKLANTLISGT--DLPDGSFWDDAKIGGQAE--HLYDltdl 129
Cdd:cd13658 1 QLTVWVDEDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPagKGPDVMVAPHDRIGSAVLqgLLSP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 130 IAPYRDKTSAY---KLSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAgvdpagLKTYDDLLAAARSLREKNPKARPLHME 206
Cdd:cd13658 76 IKLSKDKKKGFtdqALKALTYDGKLYGLPAAVETLALYYNKDLVKNA------PKTFDELEALAKDLTKEKGKQYGFLAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 207 KDPFLGQLWLemLAG-------QQGTSLadADGQVRLDSKEYRNILNWVR---------DAVDDDLVThaEYLKQADLAA 270
Cdd:cd13658 150 ATNFYYSYGL--LAGnggyifkKNGSDL--DINDIGLNSPGAVKAVKFLKkwytegylpKGMTGDVIQ--GLFKEGKAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 271 LENGqqalvPWAvwwsFAPQQLLKKGKGkwrAAPLPAWTPGGARSGAMGGSSFIIPAKAKNPELAWLLYEFLCFKEPGYS 350
Cdd:cd13658 224 VIDG-----PWA----IQEYQEAGVNYG---VAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 351 AVYGPSEVypgglttsvpsygPARRP--DKPLFEpvaalGGQDLWKVAVDAADTIPSAApIP---AWWaksvDYLGNNLQ 425
Cdd:cd13658 292 RYDETNEI-------------PPRKDvrSDPEIK-----NNPLTSAFAKQASRAVPMPN-IPemgAVW----EPANNALF 348
|
410 420
....*....|....*....|....
gi 1389008600 426 RLIEGKMAPDDVIDDSTKKIQRNL 449
Cdd:cd13658 349 FILSGKKTPKQALNDAVNDIKENI 372
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
54-346 |
3.37e-09 |
|
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: 58.16 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 54 EITIWN--RSGDLfKVFDAAIDAFRKAYPDIKVNhqaVDIDAKLA-----NTLISGTDLPDGSFWDDAKIGGQAE--HLY 124
Cdd:cd13657 1 TITIWHalTGAEE-DALQQIIDEFEAKYPVPNVK---VPFEKKPDlqnklLTAIPAGEGPDLFIWAHDWIGQFAEagLLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 125 DLTDLIAPyrDKTSAYK---LSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAgvdPaglKTYDDLLAAARSLREKNPKAR 201
Cdd:cd13657 77 PISDYLSE--DDFENYLptaVEAVTYKGKVYGLPEAYETVALIYNKALVDQP---P---ETTDELLAIMKDHTDPAAGSY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 202 PLHME-KDPFLGQLWLEMLAGqqgtSLADADG-QVRLDSKEYRNILNWVRDAVDDDLVTHAEYLKQadLAALENGQQALV 279
Cdd:cd13657 149 GLAYQvSDAYFVSAWIFGFGG----YYFDDETdKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQ--TSLFNEGKAAMI 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389008600 280 ---PWAVwwsfapqQLLKKGKGKWRAAPLPAWTPGGARSGAMGGSSFII--PAKAKNPELAWLLYEFLCFKE 346
Cdd:cd13657 223 ingPWFI-------GGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAE 287
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
94-350 |
5.04e-07 |
|
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: 51.69 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 94 KLANTLISGtDLPD---GSFWDDAKIG-GQAEHLYDLTDLIAPY------RDKTSAYKLSVNTVDGRIYGVPW--DLDP- 160
Cdd:cd13521 47 KLNLMLASG-DLPDivgADYLKDKFIAyGMEGAFLPLSKYIDQYpnlkafFKQHPDVLRASTASDGKIYLIPYepPKDVp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 161 -GLLWYREDLLEDAGVDPagLKTYDDLLAAARSLREKNPKA---RPLHMEKDPFLGQLWLEMLAGQQGTSLAD------- 229
Cdd:cd13521 126 nQGYFIRKDWLDKLNLKT--PKTLDELYNVLKAFKEKDPNGngkADEIPFIDRDPLYGAFRLINSWGARSAGGstdsdwy 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 230 -ADGQVRLD--SKEYRNILNWVRDAVDDDLVTHAEYLKQADLAA--LENGqQALVPWAVWWSFAPQQLLKKGKGKWRAAP 304
Cdd:cd13521 204 eDNGKFKHPfaSEEYKDGMKYMNKLYTEGLIDKESFTQKDDQAEqkFSNG-KLGGFTHNWFASDNLFTAQLGKEKPMYIL 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1389008600 305 LPAWTPGGA-------RSGAMGGSSFIIPAKAKNPELAWLLYEFLcFKEPGYS 350
Cdd:cd13521 283 LPIAPAGNVkgrreedSPGYTGPDGVAISKKAKNPVAALKFFDWL-ASEEGRE 334
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
45-342 |
3.03e-04 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 42.59 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 45 GTPSASAKGEITIWNRSGDlfkVFDAAIDAFRKAYpDIKVNHQAVDIDAKLANTLISGT---DL--PDGSFwddAKIGGQ 119
Cdd:COG0687 21 GAPAAAAEGTLNVYNWGGY---IDPDVLEPFEKET-GIKVVYDTYDSNEEMLAKLRAGGsgyDVvvPSDYF---VARLIK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 120 AehlydltDLIAPY-RDKTSAYK------LSVNTVDGRIYGVPWDLDPGLLWYREDLLEDAgvdpagLKTYDDLLaaars 192
Cdd:COG0687 94 A-------GLLQPLdKSKLPNLAnldprfKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEP------PTSWADLW----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 193 lrekNPK-ARPLHMEKDPflgQLWLEMLAGQQGTSLADadgqvrLDSKEYRNILNWVRDAVDDDLVTHAEYLKQADLaaL 271
Cdd:COG0687 156 ----DPEyKGKVALLDDP---REVLGAALLYLGYDPNS------TDPADLDAAFELLIELKPNVRAFWSDGAEYIQL--L 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389008600 272 ENGQQALvpwAVWWSFAPQQLLKKGKgKWRAAplpawTPggaRSGAMGGS-SFIIPAKAKNPELAwllYEFL 342
Cdd:COG0687 221 ASGEVDL---AVGWSGDALALRAEGP-PIAYV-----IP---KEGALLWFdNMAIPKGAPNPDLA---YAFI 277
|
|
| PBP2_AlgQ1_2 |
cd13584 |
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ... |
97-453 |
4.99e-04 |
|
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. 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 includes 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: 270302 [Multi-domain] Cd Length: 481 Bit Score: 42.42 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 97 NTLISGTDLPD--GSFWDDAKIG----GQAEHLYDLTDLI---AP----YRDKTSAYKLSVNTVDGRIYGVPW--DLDPG 161
Cdd:cd13584 50 NLMMASGQLPDiiGGDWLKDKGGfekyGEDGAFLPLNDLIdqyAPnlkkFLDEHPDVKKAITTDDGNIYGFPYlpDGDVA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 162 LLWY----REDLLEDAGVDPAglKTYDDLLAAARSLREKNPKARPLHMEKdPFLGQLWlemlAGQQGTSLADA------- 230
Cdd:cd13584 130 KEARgyfiRKDWLDKLGLKTP--STIDEWYTVLKAFKERDPNGNGKADEV-PLILTKP----GYDETGRLINAwgaymdf 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 231 ---DGQVRLDSKE--YRNIL----NWVRDA-VDDDLVTHAEYLKQADLAAlENGQQALVPWAVWWSFAPQQLLKKGKG-K 299
Cdd:cd13584 203 yqeNGKVKYGPLEpgFKDFLktmnQWYKEGlIDPDFFTRKAKAREQNIMN-GNIGGFTHDWFASTGTFNLALLKNVPDfK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 300 WRAAPLP----AWTPGGARSGAMG-GSSFIIPAKAKNPELA--WLLYEflcFKEPGYSAV-YG-PSEVY----------- 359
Cdd:cd13584 282 LVAVPPPvlnkGQTPYEEDSRQIAkGDGAAITASNKNPVLAikWLDYA---YSEEGRLLSnFGvEGESYtikngkpvftd 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 360 -----PGGLTTSVPSYGPARRP-----DKPLFEPVA---ALGGQDLW------KVAVDAADTIPSAAPIPAWWAKSVDYL 420
Cdd:cd13584 359 dvlkdPQPLVNALSLYYGAQIPggfwqDYEYEEQWTtpeALESKDIYaknkyvMPLPPVTLTEEERSIYDSIMTDIDTYV 438
|
410 420 430
....*....|....*....|....*....|...
gi 1389008600 421 GNNLQRLIEGKMAPDDVIDDSTKKIQRNLVDRA 453
Cdd:cd13584 439 NEMGQKWIMGKEDADDNWDEYQKKLKSLGLYEA 471
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
81-340 |
1.16e-03 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 41.19 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 81 DIKVNHQAV---DIDAKLaNTLISGTDLPD--GSFWDDAKI----GGQAEHLYDLTDLIAPYRDKTSAYKL-----SVNT 146
Cdd:cd13583 31 NVKFKRTPIpssDYETKR-SLLIASGDAPDiiPVLYPGEENefvaSGALLPISDYLDYMPNYKKYVEKWGLgkelaTGRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 147 VDGRIYGVP-WDLDPGL---LWYREDLLEDAGVDPAglKTYDDLLAAARSLREKNPKARPLH--MEKDPFLGQLWLEM-- 218
Cdd:cd13583 110 SDGKYYSLPgLHEDPGVqysFLYRKDIFEKAGIKIP--TTWDEFYAALKKLKEKYPDSYPYSdrWNSNALLLIAAPAFgt 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 219 --LAGQQGTSLADADGQVRL--DSKEYRNILNWVRDAVDDDLVThAEYLKQADLAALE---NGqQALVPWAVWWSFA--P 289
Cdd:cd13583 188 taGWGFSNYTYDPDTDKFVYgaTTDEYKDMLQYFNKLYAEGLLD-PESFTQTDDQAKAkflNG-KSFVITTNPQTVDelQ 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389008600 290 QQLLKKGKGKWRAAPLP--------AWTPGGARSGAMGGSSfiiPAKAKNPE-----LAWLLYE 340
Cdd:cd13583 266 RNLRAADGGNYEVVSITppagpagkAINGSRLENGFMISSK---AKDSKNFEallqfLDWLYSD 326
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
48-342 |
7.56e-03 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 38.45 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 48 SASAK---GEITIWNRSGDLFKVFDAAIDAFRKAyPDIKVNHQAVD-IDAKLANTLISGtDLPDGSFWDDAKIGGQAEhl 123
Cdd:PRK09474 23 SALAKieeGKLVIWINGDKGYNGLAEVGKKFEKD-TGIKVTVEHPDkLEEKFPQVAATG-DGPDIIFWAHDRFGGYAQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 124 ydlTDLIAP------YRDKTSAYKLSVNTVDGRIYGVPWDLDPGLLWYREDLLedagvdPAGLKTYDDLLAAARSLREKN 197
Cdd:PRK09474 99 ---SGLLAEvtpskaFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLV------PTPPKTWEEIPALDKELKAKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389008600 198 PKARPLHMeKDPFLGqlWlEMLAGQQGTSLADADG-----QVRLDSKEYRNILNWVRDAVDDDLVThaeylKQADL---- 268
Cdd:PRK09474 170 KSAIMWNL-QEPYFT--W-PLIAADGGYAFKFENGgydvkDVGVNNAGAKAGLQFLVDLVKNKHMN-----ADTDYsiae 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389008600 269 AALENGQQALV---PWAvwWSFapqqlLKKGKGKWRAAPLPAWT--PGGARSGAMGGSsfiIPAKAKNPELAwllYEFL 342
Cdd:PRK09474 241 AAFNKGETAMTingPWA--WSN-----IDKSGINYGVTVLPTFNgkPSKPFVGVLSAG---INAASPNKELA---KEFL 306
|
|
| |
