|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
23-334 |
2.57e-49 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 171.00 E-value: 2.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 23 AQAGEVEVLHWWTSAGEKRAAETLKKLVEAK--GHTWKdfaVAGGGGEAAMTVLKTRAVSGNPPAAAQIKGPDIQEWGEL 100
Cdd:COG1653 28 AAAGKVTLTVWHTGGGEAAALEALIKEFEAEhpGIKVE---VESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 101 GLLADLNAVAAEGKWD-SLLPKQVAQIMKYDGDYVAVPINVHRVNwLYINPEVFKKAGATPPTTLDELFVAADKLKA-AG 178
Cdd:COG1653 105 GALVPLDDLLDDDGLDkDDFLPGALDAGTYDGKLYGVPFNTDTLG-LYYNKDLFEKAGLDPPKTWDELLAAAKKLKAkDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 179 FTPLAHGsqpWQDGTVFENLVLSkMGPEgyrkAFVEQDKATLTGAQMVEVFAALKKLR--GYVDADAAGREWSAATAMVI 256
Cdd:COG1653 184 VYGFALG---GKDGAAWLDLLLS-AGGD----LYDEDGKPAFDSPEAVEALEFLKDLVkdGYVPPGALGTDWDDARAAFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 257 NGKAGMQIMGDWAKSEFTAAGkvPGKDYQCLPFP----GTQKAFDYNIDSLVMFKlsNAENRKAQEDLARSVLDPSFQKD 332
Cdd:COG1653 256 SGKAAMMINGSWALGALKDAA--PDFDVGVAPLPggpgGKKPASVLGGSGLAIPK--GSKNPEAAWKFLKFLTSPEAQAK 331
|
..
gi 489182019 333 FN 334
Cdd:COG1653 332 WD 333
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
71-352 |
6.01e-26 |
|
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: 108.15 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 71 MTVLKTRAVSGNPPAAAQIKGPDIQEWGELGLLADLNA-VAAEGKWDSLLPKQVAQIMKYDGDYVAVPINVH-RVnwLYI 148
Cdd:cd14748 44 LTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDyIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTStPV--LYY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 149 NPEVFKKAG---ATPPTTLDELFVAADKLKAAGFTPLAHG--SQPWQDGTVFENLVLSKMGPegyrkaFVEQD--KATLT 221
Cdd:cd14748 122 NKDLFEEAGldpEKPPKTWDELEEAAKKLKDKGGKTGRYGfaLPPGDGGWTFQALLWQNGGD------LLDEDggKVTFN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 222 GAQMVEVFAALKKLRGyVDADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAGkvPGKDYQCLPFP---GTQKAFDY 298
Cdd:cd14748 196 SPEGVEALEFLVDLVG-KDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIRDKG--AGFEYGVAPLPagkGKKGATPA 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489182019 299 NIDSLVMFKlSNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDADMAPFD 352
Cdd:cd14748 273 GGASLVIPK-GSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEE 325
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
37-331 |
1.07e-17 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 82.85 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 37 AGEKRAAETLKKLVEA--KGHTWKDFAVAGGGGEAAMTVLKTRAVSGNPPAA-AQIKGPDIQEWGELGLLADLNAVAAEG 113
Cdd:pfam01547 1 AASLTEAAALQALVKEfeKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADvFASDNDWIAELAKAGLLLPLDDYVANY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 114 KWDsllpkqvaqimkYDGDYVAVPINVhRVNWLYINPEVFKKAGATPPTTLDELFVAADKLKAAG-FTPLAHGSQPWQDG 192
Cdd:pfam01547 81 LVL------------GVPKLYGVPLAA-ETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGkSPGGAGGGDASGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 193 TVFENLVLSKMGPEGYRKAF--VEQDKATLTGAQMVEVFAALKKLRGYVDADAAGREWSAATAMVINGKAGMQIMGDWA- 269
Cdd:pfam01547 148 GYFTLALLASLGGPLFDKDGggLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAa 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 270 --------KSEFTAAGKVPGKDYQCLPFPGTQKAfDYNIDSLVMFKlsNAENRKAQEDLARSVLDPSFQK 331
Cdd:pfam01547 228 laankvklKVAFAAPAPDPKGDVGYAPLPAGKGG-KGGGYGLAIPK--GSKNKEAAKKFLDFLTSPEAQA 294
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
83-269 |
1.39e-04 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 43.85 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 83 PPAAAQIKGPDI--------QEWGELGLLADLNaVAAEGK-------WDSllpkqvaqiMKYDGDYVAVPINVHRVNWLY 147
Cdd:PRK09474 74 PQVAATGDGPDIifwahdrfGGYAQSGLLAEVT-PSKAFKdklvpftWDA---------VRYNGKLIGYPIAVEALSLIY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 148 iNPEVFKkagaTPPTTLDELFVAADKLKAAG------------FT-PL--AHGsqpwqdGTVFenlvlsKMGPEGYRKAF 212
Cdd:PRK09474 144 -NKDLVP----TPPKTWEEIPALDKELKAKGksaimwnlqepyFTwPLiaADG------GYAF------KFENGGYDVKD 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489182019 213 VEQDKAtltGAQmvevfAALKKLRGYVDAD--AAGREWSAATAMVINGKAGMQIMGDWA 269
Cdd:PRK09474 207 VGVNNA---GAK-----AGLQFLVDLVKNKhmNADTDYSIAEAAFNKGETAMTINGPWA 257
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
23-334 |
2.57e-49 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 171.00 E-value: 2.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 23 AQAGEVEVLHWWTSAGEKRAAETLKKLVEAK--GHTWKdfaVAGGGGEAAMTVLKTRAVSGNPPAAAQIKGPDIQEWGEL 100
Cdd:COG1653 28 AAAGKVTLTVWHTGGGEAAALEALIKEFEAEhpGIKVE---VESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 101 GLLADLNAVAAEGKWD-SLLPKQVAQIMKYDGDYVAVPINVHRVNwLYINPEVFKKAGATPPTTLDELFVAADKLKA-AG 178
Cdd:COG1653 105 GALVPLDDLLDDDGLDkDDFLPGALDAGTYDGKLYGVPFNTDTLG-LYYNKDLFEKAGLDPPKTWDELLAAAKKLKAkDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 179 FTPLAHGsqpWQDGTVFENLVLSkMGPEgyrkAFVEQDKATLTGAQMVEVFAALKKLR--GYVDADAAGREWSAATAMVI 256
Cdd:COG1653 184 VYGFALG---GKDGAAWLDLLLS-AGGD----LYDEDGKPAFDSPEAVEALEFLKDLVkdGYVPPGALGTDWDDARAAFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 257 NGKAGMQIMGDWAKSEFTAAGkvPGKDYQCLPFP----GTQKAFDYNIDSLVMFKlsNAENRKAQEDLARSVLDPSFQKD 332
Cdd:COG1653 256 SGKAAMMINGSWALGALKDAA--PDFDVGVAPLPggpgGKKPASVLGGSGLAIPK--GSKNPEAAWKFLKFLTSPEAQAK 331
|
..
gi 489182019 333 FN 334
Cdd:COG1653 332 WD 333
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
71-352 |
6.01e-26 |
|
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: 108.15 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 71 MTVLKTRAVSGNPPAAAQIKGPDIQEWGELGLLADLNA-VAAEGKWDSLLPKQVAQIMKYDGDYVAVPINVH-RVnwLYI 148
Cdd:cd14748 44 LTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDyIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTStPV--LYY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 149 NPEVFKKAG---ATPPTTLDELFVAADKLKAAGFTPLAHG--SQPWQDGTVFENLVLSKMGPegyrkaFVEQD--KATLT 221
Cdd:cd14748 122 NKDLFEEAGldpEKPPKTWDELEEAAKKLKDKGGKTGRYGfaLPPGDGGWTFQALLWQNGGD------LLDEDggKVTFN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 222 GAQMVEVFAALKKLRGyVDADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAGkvPGKDYQCLPFP---GTQKAFDY 298
Cdd:cd14748 196 SPEGVEALEFLVDLVG-KDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIRDKG--AGFEYGVAPLPagkGKKGATPA 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489182019 299 NIDSLVMFKlSNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDADMAPFD 352
Cdd:cd14748 273 GGASLVIPK-GSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEE 325
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
72-395 |
7.83e-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: 105.15 E-value: 7.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 72 TVLKTRAVSGNPPAAAQIK-GPDIQEWGELGLLADLNAVAAEGKWDSLLPKQVAQIMKYDGDYVAVPINVhRVNWLYINP 150
Cdd:cd14749 45 TKLKTAVAAGEGPDVFNLWpGGWLAEFVKAGLLLPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAA-RALALFYNK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 151 EVFKKAG-ATPPTTLDELFVAADKLKAAGFTPLAHGSQP-WQDGT-VFENLVLSKMGPEgyrKAFVEQDKATLTGAQMVE 227
Cdd:cd14749 124 DLFEEAGgVKPPKTWDELIEAAKKDKFKAKGQTGFGLLLgAQGGHwYFQYLVRQAGGGP---LSDDGSGKATFNDPAFVQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 228 VFAALKKLR--GYVDADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAgkVPGKDYQCLPFPGTQK--------AFD 297
Cdd:cd14749 201 ALQKLQDLVkaGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAIKAG--EPGGKIGVFPFPTVGKgaqtstigGSD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 298 YnidsLVMFKlSNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDADMAPFDSCAQQSMKDFKQASQDGNLVPSMAH 377
Cdd:cd14749 279 W----AIAIS-ANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEY 353
|
330
....*....|....*...
gi 489182019 378 SMAASSYVQGAIFDVVTN 395
Cdd:cd14749 354 WPAAAQVHKDAVQKLLTG 371
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
23-395 |
3.52e-24 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 103.49 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 23 AQAGEVEVLHWWTSAGEKRAAETLKKLVEAKghTWKDFAVAGGGGEAAMTVLKTRAVSGNPPAAAQIKGPDIQEWGELGL 102
Cdd:COG2182 33 SAAGAGGTLTVWVDDDEAEALEEAAAAFEEE--PGIKVKVVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 103 LADLNAVAAEgkWDSLLPKqVAQIMKYDGDYVAVPINV-HRVnwLYINPEVFKkagATPPTTLDELFVAADKLKAAGFTP 181
Cdd:COG2182 111 LAPLDDDLAD--KDDFLPA-ALDAVTYDGKLYGVPYAVeTLA--LYYNKDLVK---AEPPKTWDELIAAAKKLTAAGKYG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 182 LAhgsQPWQDGTVFENLVLSkMGPEGYRKAFVEQDKATLTGAQMVEVFAALKKL--RGYVDADAAgreWSAATAMVINGK 259
Cdd:COG2182 183 LA---YDAGDAYYFYPFLAA-FGGYLFGKDGDDPKDVGLNSPGAVAALEYLKDLikDGVLPADAD---YDAADALFAEGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 260 AGMQIMGDWAKSEFTAAGKVpgkDYQCLPFPG-----TQKAFdynIDSLVMFKLSNAENRKAQEDLARSVLDPSFQKDFN 334
Cdd:COG2182 256 AAMIINGPWAAADLKKALGI---DYGVAPLPTlaggkPAKPF---VGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALF 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182019 335 LNKGSIPVRLDADMAPFDScAQQSMKDFKQASQDGNLVPSMAHSMAASSYVQGAIFDVVTN 395
Cdd:COG2182 330 EATGRIPANKAAAEDAEVK-ADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASG 389
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
74-389 |
9.54e-22 |
|
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: 95.93 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 74 LKTRAVSGNPPAAAQIKGPDIQEWGELGLLADLNAVAAEGKWDSLLPKQVAQIMKYDGDYVAVPINVHrVNWLYINPEVF 153
Cdd:cd13585 46 LTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDAD-TLVLFYNKDLF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 154 KKAGA--TPPTTLDELFVAA--DKLKAAGFTPLAHGSQPWqDGTVFENLVLSkMGPEGYRKafvEQDKATLTGAQMVEVF 229
Cdd:cd13585 125 DKAGPgpKPPWTWDELLEAAkkLTDKKGGQYGFALRGGSG-GQTQWYPFLWS-NGGDLLDE---DDGKATLNSPEAVEAL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 230 AALKKL-RGYVDADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAGkvPGKDYQCLPFP---GTQKAFDYNIDSLVM 305
Cdd:cd13585 200 QFYVDLyKDGVAPSSATTGGDEAVDLFASGKVAMMIDGPWALGTLKDSK--VKFKWGVAPLPagpGGKRASVLGGWGLAI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 306 FKlsNAENRKAQEDLARSVLDPSFQKDFNLNKGS-IPVRLDADMAPFDSCAQQSMKDFKQASQDGNLVPSMAHSMAASSY 384
Cdd:cd13585 278 SK--NSKHPEAAWKFIKFLTSKENQLKLGGAAGPaALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPI 355
|
....*
gi 489182019 385 VQGAI 389
Cdd:cd13585 356 LSEAL 360
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
37-331 |
1.07e-17 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 82.85 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 37 AGEKRAAETLKKLVEA--KGHTWKDFAVAGGGGEAAMTVLKTRAVSGNPPAA-AQIKGPDIQEWGELGLLADLNAVAAEG 113
Cdd:pfam01547 1 AASLTEAAALQALVKEfeKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADvFASDNDWIAELAKAGLLLPLDDYVANY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 114 KWDsllpkqvaqimkYDGDYVAVPINVhRVNWLYINPEVFKKAGATPPTTLDELFVAADKLKAAG-FTPLAHGSQPWQDG 192
Cdd:pfam01547 81 LVL------------GVPKLYGVPLAA-ETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGkSPGGAGGGDASGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 193 TVFENLVLSKMGPEGYRKAF--VEQDKATLTGAQMVEVFAALKKLRGYVDADAAGREWSAATAMVINGKAGMQIMGDWA- 269
Cdd:pfam01547 148 GYFTLALLASLGGPLFDKDGggLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAa 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 270 --------KSEFTAAGKVPGKDYQCLPFPGTQKAfDYNIDSLVMFKlsNAENRKAQEDLARSVLDPSFQK 331
Cdd:pfam01547 228 laankvklKVAFAAPAPDPKGDVGYAPLPAGKGG-KGGGYGLAIPK--GSKNKEAAKKFLDFLTSPEAQA 294
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
71-374 |
4.36e-14 |
|
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: 73.12 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 71 MTVLKTRAVSGNPPAAAQIKGPDIQEWGELGLLADLNAVAAEGKWDSLLPKQVAQIMKYDGDYVAVPinvhrvnW----- 145
Cdd:cd14747 43 HTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLEDLGGDKDLFPGLVDTGTVDGKYYGVP-------Wyadtr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 146 -LYINPEVFKKAG-ATPPTTLDELFVAADKLKAAG--FTPLA-HGSQPWQDGtvFENLVLSKMGpegyrkAFVEQDK--A 218
Cdd:cd14747 116 aLFYRTDLLKKAGgDEAPKTWDELEAAAKKIKADGpdVSGFAiPGKNDVWHN--ALPFVWGAGG------DLATKDKwkA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 219 TLTGAQMVEVFAALKKL--RGYVDADAAGREWSAATAMViNGKAGMQIMGDWAKSEFTAAGKVPGKDYQCLPFPGTQKAF 296
Cdd:cd14747 188 TLDSPEAVAGLEFYTSLyqKGLSPKSTLENSADVEQAFA-NGKVAMIISGPWEIGAIREAGPDLAGKWGVAPLPGGPGGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 297 DYNI---DSLVMFKlsNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDAdMAPFDSCAQQSMKDFKQASQDGNLVP 373
Cdd:cd14747 267 SPSFaggSNLAVFK--GSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSA-WDDPSLANDPLLAVFAEQLKTGKATP 343
|
.
gi 489182019 374 S 374
Cdd:cd14747 344 A 344
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
71-351 |
9.64e-14 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 71.28 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 71 MTVLKTRAVSGNPPAAA--QIKGPDIQEWGELGLLADLNAVAAEGKWDSLLPKQvaqimKYDGDYVAVPINVHRVNWLYI 148
Cdd:pfam13416 25 QAKLLAAAAAGNAPDLDvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAA-----GYDGKLYGVPYAASTPTVLYY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 149 NPEVFKKAGaTPPTTLDELFVAADKLKAAGFTPLahgsqpWQDGTVFENLVLSKMGPEGYRKAFVEQDKAtltgaqmvev 228
Cdd:pfam13416 100 NKDLLKKAG-EDPKTWDELLAAAAKLKGKTGLTD------PATGWLLWALLADGVDLTDDGKGVEALDEA---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 229 FAALKKLRGYVDADAAgreWSAATAMVINGKAGMQIMGDWAKSEFTAAGK----VPGKDYQCLpfpgtqkafdyNIDSLV 304
Cdd:pfam13416 163 LAYLKKLKDNGKVYNT---GADAVQLFANGEVAMTVNGTWAAAAAKKAGKklgaVVPKDGSFL-----------GGKGLV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489182019 305 MFKLSNAENRKAQeDLARSVLDPSFQKDFNLNKGSIPVRLDADMAPF 351
Cdd:pfam13416 229 VPAGAKDPRLAAL-DFIKFLTSPENQAALAEDTGYIPANKSAALSDE 274
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
82-399 |
4.67e-12 |
|
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: 67.05 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 82 NPPAAAQIKGPDIQEW--------GELGLLADLnavaaegkwDSLLPKQVAQI------MKYDGDYVAVPINVHRVNWLY 147
Cdd:cd13522 46 FSTAAAGGKGPDVVFGpsdslgpfAAAGLLAPL---------DEYVSKSGKYApntiaaMKLNGKLYGVPVSVGAHLMYY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 148 INpevfKKAGATPPTTLDELFVAADKLKAAGFTPLAHGSQ------PWQ---DGTVFenlvlskmgpegyrKAFVEQDKA 218
Cdd:cd13522 117 NK----KLVPKNPPKTWQELIALAQGLKAKNVWGLVYNQNepyffaAWIggfGGQVF--------------KANNGKNNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 219 TLTGAQMVEVFAALKKLRGYVDADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAGKVpgkDYQCLP---FPGTQKA 295
Cdd:cd13522 179 TLDTPGAVEALQFLVDLKSKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRQALKI---NLGVAPlptFSGTKHA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 296 FDYnIDSLVMFKLSNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDAdmapFDSCAQQS---MKDFKQASQDGNLV 372
Cdd:cd13522 256 APF-VGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQA----YESPAVQNkpaQKASAEQAAYGVPM 330
|
330 340
....*....|....*....|....*..
gi 489182019 373 PsmahSMAASSYVQGAIFDVVTNFFND 399
Cdd:cd13522 331 P----NIPEMRAVWDAFRIAVNSVLAG 353
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
90-346 |
1.02e-11 |
|
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: 65.86 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 90 KGPD--------IQEWGELGLLADLNAVAAEGKWDSLLPKQVaQIMKYDGDYVAVPINVHRVNwLYINpevfKKAGATPP 161
Cdd:cd13657 54 EGPDlfiwahdwIGQFAEAGLLVPISDYLSEDDFENYLPTAV-EAVTYKGKVYGLPEAYETVA-LIYN----KALVDQPP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 162 TTLDELFVAADKL--KAAGFTPLAhgsqpWQDGTV-FENLVLSKMGPEGYRKafvEQDKATLTGAQMVEVFAALKKL-RG 237
Cdd:cd13657 128 ETTDELLAIMKDHtdPAAGSYGLA-----YQVSDAyFVSAWIFGFGGYYFDD---ETDKPGLDTPETIKGIQFLKDFsWP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 238 YVDADAagrEWSAATAMVINGKAGMQIMGDWAKSEFtaagKVPGKDYQCLPFPGTQKAFD---YNIDSLVMF-KLSNAEN 313
Cdd:cd13657 200 YMPSDP---SYNTQTSLFNEGKAAMIINGPWFIGGI----KAAGIDLGVAPLPTVDGTNPprpYSGVEGIYVtKYAERKN 272
|
250 260 270
....*....|....*....|....*....|...
gi 489182019 314 RKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDA 346
Cdd:cd13657 273 KEAALDFAKFFTTAEASKILADENGYVPAATNA 305
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
85-374 |
1.00e-10 |
|
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: 62.70 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 85 AAAQIKGPDIQEW-----GEL---GLLADL-NAVAAEGKwdsLLPKQVAQiMKYDGDYVAVPINVHRVNwLYINpevfKK 155
Cdd:cd13586 47 AGPAGKGPDVFFGphdwlGELaaaGLLAPIpEYLAVKIK---NLPVALAA-VTYNGKLYGVPVSVETIA-LFYN----KD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 156 AGATPPTTLDEL--FVAADKLKAAGFTPLAHG------SQPWQ---DGTVFenlvlskmGPEGyrkafVEQDKATLTGAQ 224
Cdd:cd13586 118 LVPEPPKTWEELiaLAKKFNDKAGGKYGFAYDqtnpyfSYPFLaafGGYVF--------GENG-----GDPTDIGLNNEG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 225 MVEVFAALKKLRGYVDADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAG------KVP--GKDYQCLPFPGTQkaf 296
Cdd:cd13586 185 AVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGinfgvaPLPtlPGGKQAAPFVGVQ--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 297 dynidslVMFKLSNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDAdmapFDSCAQQS---MKDFKQASQDGNLVP 373
Cdd:cd13586 262 -------GAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDA----LNDAAVKNdplVKAFAEQAQYGVPMP 330
|
.
gi 489182019 374 S 374
Cdd:cd13586 331 N 331
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
94-345 |
1.36e-08 |
|
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: 56.15 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 94 IQEWGELGLLADLNAVAAEGKWDSLLPkQVAQIMKYDGDYVAVPINVHrVNWLYINPEVFKKAGATPPTTLDELFVAADK 173
Cdd:cd14750 69 IPEFAEAGWLLPLTEYLKEEEDDDFLP-ATVEANTYDGKLYALPWFTD-AGLLYYRKDLLEKYGPEPPKTWDELLEAAKK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 174 LKAAGFTPLAHGSQPWQDGTV---FENLVLSKMGpegyrKAFVEQD-KATLTGAQMVEvfaALKKLRGYVDADAAGREWS 249
Cdd:cd14750 147 RKAGEPGIWGYVFQGKQYEGLvcnFLELLWSNGG-----DIFDDDSgKVTVDSPEALE---ALQFLRDLIGEGISPKGVL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 250 A-----ATAMVINGKAGMqiMGDWAKSEFTAAG---KVPGK-DYQCLP-FPGTQKA-----FDYNIdslvmfkLSNAENR 314
Cdd:cd14750 219 TygeeeARAAFQAGKAAF--MRNWPYAYALLQGpesAVAGKvGVAPLPaGPGGGSAstlggWNLAI-------SANSKHK 289
|
250 260 270
....*....|....*....|....*....|.
gi 489182019 315 KAQEDLARSVLDPSFQKDFNLNKGSIPVRLD 345
Cdd:cd14750 290 EAAWEFVKFLTSPEVQKRRAINGGLPPTRRA 320
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
75-365 |
2.22e-08 |
|
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: 55.46 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 75 KTRAVSGNPPAAAQIKGPDIQEWGELGLLADLNAVAAEGKWDSLLPkQVAQIMKYDGDYVAVPINVHRVNWLYiNPEVFK 154
Cdd:cd14751 47 KTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDIVDYLP-GPMETNRYNGHYYGVPQVTNTLALFY-NKRLLE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 155 KAGATPPTTLDELF-VAADKLKAAGFTPLA-HGSQPWQdgtvfenlvlskMGP--EGYRKAFVEQDKATLTGAQmVEVFA 230
Cdd:cd14751 125 EAGTEVPKTMDELVaAAKAIKKKKGRYGLYiSGDGPYW------------LLPflWSFGGDLTDEKKATGYLNS-PESVR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 231 ALKKLRGYVDADAAGR----EWSAATAMVINGKAGMQIMGDWAKSEFTA-AGKVPGKDYQCLPFPGTQKAFDYNI--DSL 303
Cdd:cd14751 192 ALETIVDLYDEGAITPcasgGYPNMQDGFKSGRYAMIVNGPWAYADILGgKEFKDPDNLGIAPVPAGPGGSGSPVggEDL 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489182019 304 VMFKlsNAENRKAQEDLARSVLDPSFQKDFNLNKGSIPVRLDADMAPfdSCAQQSM-KDFKQA 365
Cdd:cd14751 272 VIFK--GSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESP--EVANNPMvAAFKPA 330
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
113-269 |
3.26e-05 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 45.81 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 113 GKWDslLPKQVAQIMKYDGDYVAVP---INVHRVNWLYINPEVFKKAGATPPTTLDELFVAADKLKAAgfTPlahGSQPW 189
Cdd:cd13583 96 EKWG--LGKELATGRQSDGKYYSLPglhEDPGVQYSFLYRKDIFEKAGIKIPTTWDEFYAALKKLKEK--YP---DSYPY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 190 QDGTVFENL----VLSKMGPEGYRKAFVEQDKAT----LTGAQ-----MVEVFAALKKlRGYVDADAAGREWSAATAMVI 256
Cdd:cd13583 169 SDRWNSNALlliaAPAFGTTAGWGFSNYTYDPDTdkfvYGATTdeykdMLQYFNKLYA-EGLLDPESFTQTDDQAKAKFL 247
|
170
....*....|...
gi 489182019 257 NGKaGMQIMGDWA 269
Cdd:cd13583 248 NGK-SFVITTNPQ 259
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
83-291 |
4.43e-05 |
|
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270374 [Multi-domain] Cd Length: 364 Bit Score: 45.28 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 83 PPAAAQIKGPDI--------QEWGELGLLADlnaVAAEGKWDSLLPKQVAQIMKYDGDYVAVPINVHRVNWLYINPEVfk 154
Cdd:cd13656 44 PQVAATGDGPDIifwahdrfGGYAQSGLLAE---ITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 155 kagATPPTTLDELFVAADKLKAAGFTPLAHGSQpwqdGTVFENLVLSKMGpeGYrkAFVEQDKATLTGAQMVEVFAALKK 234
Cdd:cd13656 119 ---PNPPKTWEEIPALDKELKAKGKSALMFNLQ----EPYFTWPLIAADG--GY--AFKYENGKYDIKDVGVDNAGAKAG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489182019 235 LRGYVD-----ADAAGREWSAATAMVINGKAGMQIMGDWAKSEFTAAgkvpGKDYQCLPFPG 291
Cdd:cd13656 188 LTFLVDliknkHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS----KVNYGVTVLPT 245
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
83-269 |
1.39e-04 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 43.85 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 83 PPAAAQIKGPDI--------QEWGELGLLADLNaVAAEGK-------WDSllpkqvaqiMKYDGDYVAVPINVHRVNWLY 147
Cdd:PRK09474 74 PQVAATGDGPDIifwahdrfGGYAQSGLLAEVT-PSKAFKdklvpftWDA---------VRYNGKLIGYPIAVEALSLIY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182019 148 iNPEVFKkagaTPPTTLDELFVAADKLKAAG------------FT-PL--AHGsqpwqdGTVFenlvlsKMGPEGYRKAF 212
Cdd:PRK09474 144 -NKDLVP----TPPKTWEEIPALDKELKAKGksaimwnlqepyFTwPLiaADG------GYAF------KFENGGYDVKD 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489182019 213 VEQDKAtltGAQmvevfAALKKLRGYVDAD--AAGREWSAATAMVINGKAGMQIMGDWA 269
Cdd:PRK09474 207 VGVNNA---GAK-----AGLQFLVDLVKNKhmNADTDYSIAEAAFNKGETAMTINGPWA 257
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
146-189 |
7.77e-03 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 38.24 E-value: 7.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489182019 146 LYINPEVFKKAG---ATPPTTLDELFVAADKLKAAGFT-PLAHGSQPW 189
Cdd:PRK10974 149 LYYNKDAFKKAGldpEQPPKTWQDLAAYAAKLRAAGMKcGYASGWQGW 196
|
|
| |
