|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3502 |
pfam12010 |
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. ... |
365-495 |
5.76e-61 |
|
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 140 amino acids in length. This domain is found associated with pfam01547.
:
Pssm-ID: 463429 Cd Length: 131 Bit Score: 195.91 E-value: 5.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 365 GIEGTHYKKVSDNVIEDLPAMKDGFQMPGFALGNLFLTYMHKEDPADKWEAFKEFNNSAKVAPSFGFNFNPDSVKTEVAS 444
Cdd:pfam12010 1 GIEGVHYEKVGDGKIKLLPDGVDAYNPPGWAWGNQFILYLWEGEPPDKWEEFKEFNESAKASPALGFTFDSSPVKNEIAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516283654 445 ISAIVKEFYPSIMTGAVDPDEHLPKAIEKLKAAGLDKVIAEAQKQYDEWKA 495
Cdd:pfam12010 81 CSNVVNEYKPALNTGAVDPEETLPKFNAKLKAAGIDKVIAEKQKQLDAFLA 131
|
|
| Periplasmic_Binding_Protein_Type_2 super family |
cl21456 |
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ... |
44-492 |
3.09e-33 |
|
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.
The actual alignment was detected with superfamily member cd13580:
Pssm-ID: 473866 [Multi-domain] Cd Length: 471 Bit Score: 131.30 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 44 DKDTVKLKVYMIGGPQRDLPmvQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFTSswAYDYLPNATR 123
Cdd:cd13580 1 EPVTITIVANLGGNPKPDPD--DNPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVN--DPQLSITLVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 124 -GAFLPINDLLDKYGQGIKEQLDPRFLTGSQIDGQNYSVPVNKELASQWVWRFNKQYVDKYNMDITKirTLEDLEPYLQQ 202
Cdd:cd13580 77 qGALWDLTDYLDKYYPNLKKIIEQEGWDSASVDGKIYGIPRKRPLIGRNGLWIRKDWLDKLGLEVPK--TLDELYEVAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 203 IKDNEP-----ADITPLAVPKGFKPYLAFDFLLGDEFPVGINMNGDTGKYVNMLESEELKSSLKTIRKYYQAGYLRKDVA 277
Cdd:cd13580 155 FTEKDPdgngkKDTYGLTDTKDLIGSGFTGLFGAFGAPPNNWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLIDPEFA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 278 TLEG---IDNIKTGK--------WFVDREQT-----QPYAELGWsrsagYEIVTTPMQDPVIFTGSATGAMHAISANSKN 341
Cdd:cd13580 235 VNDGtkaNEKFISGKagifvgnwWDPAWPQAslkknDPDAEWVA-----VPIPSGPDGKYGVWAESGVNGFFVIPKKSKK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 342 PERAMMFLNLLNtDPYLRNLINYGIEGTHYKKVSD--------NVIEDLPAMKDGFQmPGFALGNLFLTYMHKEDPADKW 413
Cdd:cd13580 310 PEAILKLLDFLS-DPEVQKLLDYGIEGVHYTVKDGgpvniippDKQEVGDATLDYFQ-GSLALEKYKLTNNGERKSDAKK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 414 EAFKEFNNSAKVAPSFGFnFNPDSVKTEV-------ASISAIVKEFYPSIMTGAVDPDEhLPKAIEKLKAAGLDKVIAEA 486
Cdd:cd13580 388 EALDERVVNANDEENENI-AVGPPTETLVsptekygATLDKLEDDAFTKIIMGQIPLDE-FDKFVEEWKKSGGDEITKEV 465
|
....*.
gi 516283654 487 QKQYDE 492
Cdd:cd13580 466 NEWYKE 471
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3502 |
pfam12010 |
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. ... |
365-495 |
5.76e-61 |
|
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 140 amino acids in length. This domain is found associated with pfam01547.
Pssm-ID: 463429 Cd Length: 131 Bit Score: 195.91 E-value: 5.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 365 GIEGTHYKKVSDNVIEDLPAMKDGFQMPGFALGNLFLTYMHKEDPADKWEAFKEFNNSAKVAPSFGFNFNPDSVKTEVAS 444
Cdd:pfam12010 1 GIEGVHYEKVGDGKIKLLPDGVDAYNPPGWAWGNQFILYLWEGEPPDKWEEFKEFNESAKASPALGFTFDSSPVKNEIAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516283654 445 ISAIVKEFYPSIMTGAVDPDEHLPKAIEKLKAAGLDKVIAEAQKQYDEWKA 495
Cdd:pfam12010 81 CSNVVNEYKPALNTGAVDPEETLPKFNAKLKAAGIDKVIAEKQKQLDAFLA 131
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
44-492 |
3.09e-33 |
|
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: 131.30 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 44 DKDTVKLKVYMIGGPQRDLPmvQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFTSswAYDYLPNATR 123
Cdd:cd13580 1 EPVTITIVANLGGNPKPDPD--DNPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVN--DPQLSITLVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 124 -GAFLPINDLLDKYGQGIKEQLDPRFLTGSQIDGQNYSVPVNKELASQWVWRFNKQYVDKYNMDITKirTLEDLEPYLQQ 202
Cdd:cd13580 77 qGALWDLTDYLDKYYPNLKKIIEQEGWDSASVDGKIYGIPRKRPLIGRNGLWIRKDWLDKLGLEVPK--TLDELYEVAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 203 IKDNEP-----ADITPLAVPKGFKPYLAFDFLLGDEFPVGINMNGDTGKYVNMLESEELKSSLKTIRKYYQAGYLRKDVA 277
Cdd:cd13580 155 FTEKDPdgngkKDTYGLTDTKDLIGSGFTGLFGAFGAPPNNWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLIDPEFA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 278 TLEG---IDNIKTGK--------WFVDREQT-----QPYAELGWsrsagYEIVTTPMQDPVIFTGSATGAMHAISANSKN 341
Cdd:cd13580 235 VNDGtkaNEKFISGKagifvgnwWDPAWPQAslkknDPDAEWVA-----VPIPSGPDGKYGVWAESGVNGFFVIPKKSKK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 342 PERAMMFLNLLNtDPYLRNLINYGIEGTHYKKVSD--------NVIEDLPAMKDGFQmPGFALGNLFLTYMHKEDPADKW 413
Cdd:cd13580 310 PEAILKLLDFLS-DPEVQKLLDYGIEGVHYTVKDGgpvniippDKQEVGDATLDYFQ-GSLALEKYKLTNNGERKSDAKK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 414 EAFKEFNNSAKVAPSFGFnFNPDSVKTEV-------ASISAIVKEFYPSIMTGAVDPDEhLPKAIEKLKAAGLDKVIAEA 486
Cdd:cd13580 388 EALDERVVNANDEENENI-AVGPPTETLVsptekygATLDKLEDDAFTKIIMGQIPLDE-FDKFVEEWKKSGGDEITKEV 465
|
....*.
gi 516283654 487 QKQYDE 492
Cdd:cd13580 466 NEWYKE 471
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
9-355 |
4.86e-29 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 117.45 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 9 LMVTLLLAFSTVLAGCGGSntndtsgntvSGGEPGDKDTVKLKVYMIGGPQRDlpmVQEEMNKYLMEKI-NATVDITMID 87
Cdd:COG1653 4 LALALAAALALALAACGGG----------GSGAAAAAGKVTLTVWHTGGGEAA---ALEALIKEFEAEHpGIKVEVESVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 88 WGDYSKRMPVITASGENYDIAFT-SSWAYDYlpnATRGAFLPINDLLDKYGQGiKEQLDPRFLTGSQIDGQNYSVPVNke 166
Cdd:COG1653 71 YDDYRTKLLTALAAGNAPDVVQVdSGWLAEF---AAAGALVPLDDLLDDDGLD-KDDFLPGALDAGTYDGKLYGVPFN-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 167 lASQWVWRFNKQYVDKYNMDITKirTLEDLEPYLQQIKDnePADITPLAVpkGFKPYLAFDFLLgdeFPVGINMNGDTGK 246
Cdd:COG1653 145 -TDTLGLYYNKDLFEKAGLDPPK--TWDELLAAAKKLKA--KDGVYGFAL--GGKDGAAWLDLL---LSAGGDLYDEDGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 247 YVnmLESEELKSSLKTIRKYYQAGYLRKDVATL---EGIDNIKTGKWFVDREQTQPYAELgWSRSAGYEIVTTPMqdPVI 323
Cdd:COG1653 215 PA--FDSPEAVEALEFLKDLVKDGYVPPGALGTdwdDARAAFASGKAAMMINGSWALGAL-KDAAPDFDVGVAPL--PGG 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 516283654 324 FTGS-----ATGAMHAISANSKNPERAMMFLNLLNTD 355
Cdd:COG1653 290 PGGKkpasvLGGSGLAIPKGSKNPEAAWKFLKFLTSP 326
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
56-357 |
7.05e-05 |
|
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: 44.71 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 56 GGPQRDLPMVQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGEN-YDIAFTSSWAYDYLpnATRGAFLPINDLLD 134
Cdd:pfam01547 1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGpADVFASDNDWIAEL--AKAGLLLPLDDYVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 135 KYGQGIKEQLdprfltgsqidgqnYSVPVNKElaSQWVWrFNKQYVDKYnmDITKIRTLEDLEPYLQQIKDNEPADI--- 211
Cdd:pfam01547 79 NYLVLGVPKL--------------YGVPLAAE--TLGLI-YNKDLFKKA--GLDPPKTWDELLEAAKKLKEKGKSPGgag 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 212 TPLAVPKGFKPYLAFDFLLGDEFPVGINMNGDTGKYVNMLESEE-LKSSLKTIRKYYQAGYLRKDVATLEG------IDN 284
Cdd:pfam01547 140 GGDASGTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVdLYAKVLLLKKLKNPGVAGADGREALAlfeqgkAAM 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516283654 285 IKTGKWFVDREQTQPYAELGWSRSAGYEIVTTPMQDPVIFTGSATGAMHAISANSKNPERAMMFLNLLNTDPY 357
Cdd:pfam01547 220 GIVGPWAALAANKVKLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3502 |
pfam12010 |
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. ... |
365-495 |
5.76e-61 |
|
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 140 amino acids in length. This domain is found associated with pfam01547.
Pssm-ID: 463429 Cd Length: 131 Bit Score: 195.91 E-value: 5.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 365 GIEGTHYKKVSDNVIEDLPAMKDGFQMPGFALGNLFLTYMHKEDPADKWEAFKEFNNSAKVAPSFGFNFNPDSVKTEVAS 444
Cdd:pfam12010 1 GIEGVHYEKVGDGKIKLLPDGVDAYNPPGWAWGNQFILYLWEGEPPDKWEEFKEFNESAKASPALGFTFDSSPVKNEIAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516283654 445 ISAIVKEFYPSIMTGAVDPDEHLPKAIEKLKAAGLDKVIAEAQKQYDEWKA 495
Cdd:pfam12010 81 CSNVVNEYKPALNTGAVDPEETLPKFNAKLKAAGIDKVIAEKQKQLDAFLA 131
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
44-492 |
3.09e-33 |
|
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: 131.30 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 44 DKDTVKLKVYMIGGPQRDLPmvQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFTSswAYDYLPNATR 123
Cdd:cd13580 1 EPVTITIVANLGGNPKPDPD--DNPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVN--DPQLSITLVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 124 -GAFLPINDLLDKYGQGIKEQLDPRFLTGSQIDGQNYSVPVNKELASQWVWRFNKQYVDKYNMDITKirTLEDLEPYLQQ 202
Cdd:cd13580 77 qGALWDLTDYLDKYYPNLKKIIEQEGWDSASVDGKIYGIPRKRPLIGRNGLWIRKDWLDKLGLEVPK--TLDELYEVAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 203 IKDNEP-----ADITPLAVPKGFKPYLAFDFLLGDEFPVGINMNGDTGKYVNMLESEELKSSLKTIRKYYQAGYLRKDVA 277
Cdd:cd13580 155 FTEKDPdgngkKDTYGLTDTKDLIGSGFTGLFGAFGAPPNNWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLIDPEFA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 278 TLEG---IDNIKTGK--------WFVDREQT-----QPYAELGWsrsagYEIVTTPMQDPVIFTGSATGAMHAISANSKN 341
Cdd:cd13580 235 VNDGtkaNEKFISGKagifvgnwWDPAWPQAslkknDPDAEWVA-----VPIPSGPDGKYGVWAESGVNGFFVIPKKSKK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 342 PERAMMFLNLLNtDPYLRNLINYGIEGTHYKKVSD--------NVIEDLPAMKDGFQmPGFALGNLFLTYMHKEDPADKW 413
Cdd:cd13580 310 PEAILKLLDFLS-DPEVQKLLDYGIEGVHYTVKDGgpvniippDKQEVGDATLDYFQ-GSLALEKYKLTNNGERKSDAKK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 414 EAFKEFNNSAKVAPSFGFnFNPDSVKTEV-------ASISAIVKEFYPSIMTGAVDPDEhLPKAIEKLKAAGLDKVIAEA 486
Cdd:cd13580 388 EALDERVVNANDEENENI-AVGPPTETLVsptekygATLDKLEDDAFTKIIMGQIPLDE-FDKFVEEWKKSGGDEITKEV 465
|
....*.
gi 516283654 487 QKQYDE 492
Cdd:cd13580 466 NEWYKE 471
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
9-355 |
4.86e-29 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 117.45 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 9 LMVTLLLAFSTVLAGCGGSntndtsgntvSGGEPGDKDTVKLKVYMIGGPQRDlpmVQEEMNKYLMEKI-NATVDITMID 87
Cdd:COG1653 4 LALALAAALALALAACGGG----------GSGAAAAAGKVTLTVWHTGGGEAA---ALEALIKEFEAEHpGIKVEVESVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 88 WGDYSKRMPVITASGENYDIAFT-SSWAYDYlpnATRGAFLPINDLLDKYGQGiKEQLDPRFLTGSQIDGQNYSVPVNke 166
Cdd:COG1653 71 YDDYRTKLLTALAAGNAPDVVQVdSGWLAEF---AAAGALVPLDDLLDDDGLD-KDDFLPGALDAGTYDGKLYGVPFN-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 167 lASQWVWRFNKQYVDKYNMDITKirTLEDLEPYLQQIKDnePADITPLAVpkGFKPYLAFDFLLgdeFPVGINMNGDTGK 246
Cdd:COG1653 145 -TDTLGLYYNKDLFEKAGLDPPK--TWDELLAAAKKLKA--KDGVYGFAL--GGKDGAAWLDLL---LSAGGDLYDEDGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 247 YVnmLESEELKSSLKTIRKYYQAGYLRKDVATL---EGIDNIKTGKWFVDREQTQPYAELgWSRSAGYEIVTTPMqdPVI 323
Cdd:COG1653 215 PA--FDSPEAVEALEFLKDLVKDGYVPPGALGTdwdDARAAFASGKAAMMINGSWALGAL-KDAAPDFDVGVAPL--PGG 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 516283654 324 FTGS-----ATGAMHAISANSKNPERAMMFLNLLNTD 355
Cdd:COG1653 290 PGGKkpasvLGGSGLAIPKGSKNPEAAWKFLKFLTSP 326
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
48-492 |
3.12e-28 |
|
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: 117.17 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 48 VKLKVYMIGGPQRDLPMvQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFTSSWAYDYLPNATRGAFL 127
Cdd:cd13521 2 LTLSVLMAFNDNWVDDE-NWPVAKEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKFIAYGMEGAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 128 PINDLLDKY-------GQGIKEQLdprflTGSQIDGQNYSVPVNKELA--SQWVWrFNKQYVDKYNMDItkIRTLEDLEP 198
Cdd:cd13521 81 PLSKYIDQYpnlkaffKQHPDVLR-----ASTASDGKIYLIPYEPPKDvpNQGYF-IRKDWLDKLNLKT--PKTLDELYN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 199 YLQQIKDNEP-----ADITPLAVPKGfkPYLAFDFLLGDEFPVGINMN-----GDTGKYVNMLESEELKSSLKTIRKYYQ 268
Cdd:cd13521 153 VLKAFKEKDPngngkADEIPFIDRDP--LYGAFRLINSWGARSAGGSTdsdwyEDNGKFKHPFASEEYKDGMKYMNKLYT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 269 AGYLRKDVATL------EGIDNIK----TGKWFVDREQTQPYAELGWSRSAGYEIVTTP---MQDPVIFTGSATGAMHAI 335
Cdd:cd13521 231 EGLIDKESFTQkddqaeQKFSNGKlggfTHNWFASDNLFTAQLGKEKPMYILLPIAPAGnvkGRREEDSPGYTGPDGVAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 336 SANSKNPERAMMFLNLLNTDPYlRNLINYGIEGTHYKK-------VSDNVIEDLPAMKDGFQMPGFALGNLFLTYMHK-- 406
Cdd:cd13521 311 SKKAKNPVAALKFFDWLASEEG-RELANFGIEGVHYNKdngkkrtKDPVKKSDQPGDNQLYDLPAFIKGGFWNEYTYPrp 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 407 ------EDPADKWeaFKEFNNSAKVAPSFGFNFNPDSVKTEV----ASISAIVKEFYPSIMTGAVDPDEHLPKAIEKLKA 476
Cdd:cd13521 390 qwgvltGDSARLP--IDMYIKPKYSPPKPEGANLTIEEREQVsidnTELKDIMMEMTQKWIMGTKEKDEEWDAYQEQLKS 467
|
490
....*....|....*.
gi 516283654 477 AGLDKVIAEAQKQYDE 492
Cdd:cd13521 468 AGLYQVTEEVQKAYDR 483
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-477 |
5.17e-22 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 98.10 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 1 MKTRKIALLMVTLLLAfsTVLAGCGGSNTNDTSGntvsggePGDKDTVKLKVYmIGGPQRDlpmVQEEMNKYLMEKINAT 80
Cdd:COG2182 1 MKRRLLAALALALALA--LALAACGSGSSSSGSS-------SAAGAGGTLTVW-VDDDEAE---ALEEAAAAFEEEPGIK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 81 VDITMIDWGDYSKRMPVITASGENYDIAFtssWAYDYLPN-ATRGAFLPINDLLDKygqgiKEQLDPRFLTGSQIDGQNY 159
Cdd:COG2182 68 VKVVEVPWDDLREKLTTAAPAGKGPDVFV---GAHDWLGElAEAGLLAPLDDDLAD-----KDDFLPAALDAVTYDGKLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 160 SVPVNKELASQWVwrfNKQYVDKynmdiTKIRTLEDLEPYLQQIKDnepADITPLAVPkGFKPYLAFDFLL---GDEFPV 236
Cdd:COG2182 140 GVPYAVETLALYY---NKDLVKA-----EPPKTWDELIAAAKKLTA---AGKYGLAYD-AGDAYYFYPFLAafgGYLFGK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 237 GINMNGDTGkyvnmLESEELKSSLKTIRKYYQAGYLRKDVATLEGIDNIKTGK--------WFVdreqtQPYAElgwsrS 308
Cdd:COG2182 208 DGDDPKDVG-----LNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKaamiingpWAA-----ADLKK-----A 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 309 AGYEIVTTPMqdPVIFTGS-----ATGAMHAISANSKNPERAMMFLNLLNTDPYLRnlinygiegTHYKKVSdnvieDLP 383
Cdd:COG2182 273 LGIDYGVAPL--PTLAGGKpakpfVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQK---------ALFEATG-----RIP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 384 AMKDGFQMPGFalgnlfltymhKEDPAdkWEAFKEFNNSAKVAPSFgfnfnpdsvkTEVASISAIVKEFYPSIMTGAVDP 463
Cdd:COG2182 337 ANKAAAEDAEV-----------KADPL--IAAFAEQAEYAVPMPNI----------PEMGAVWTPLGTALQAIASGKADP 393
|
490
....*....|....
gi 516283654 464 DEHLPKAIEKLKAA 477
Cdd:COG2182 394 AEALDAAQKQIEAA 407
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
48-492 |
7.98e-18 |
|
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: 85.84 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 48 VKLKVyMIGGPQRDLPMVQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFTSSWAYDYLPNAT-RGAF 126
Cdd:cd13581 2 VTLTI-FVRKSPLVEDYNENLFFKRLEEKTGIKIEWETVPEDAWAEKKNLMLASGDLPDAFLGAGASDADLMTYGkQGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 127 LPINDLLDKYGQGIKEQLDPRFLTGSQI---DGQNYSVPVNKELAS------QWVwrfNKQYVDKYNMDITKirTLEDLE 197
Cdd:cd13581 81 LPLEDLIDKYAPNLKALFDENPDIKAAItapDGHIYALPSVNECYHcsygqrMWI---NKKWLDKLGLEMPT--TTDELY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 198 PYLQQIKD-----NEPADITPLAVPKGFKPYLAFDFLLGdEF---PVGINMNG---DTGKYVNMLESEELKSSLKTIRKY 266
Cdd:cd13581 156 EVLKAFKEqdpngNGKADEIPLSFSGLNGGTDDPAFLLN-SFginDGGYGGYGfvvKDGKVIYTATDPEYKEALAYLNKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 267 YQAGYLRKDVATLEGIDNIKTGKwfvdreqtQPYAELGWS------------RSAGYEIV---TTPMQDPVIFTGSATGA 331
Cdd:cd13581 235 YKEGLIDPEAFTQDYDQLAAKGK--------ASTAKVGVFfgwdpglffgeeRYEQYVPLpplKGPNGDQLAWVGNSSGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 332 MHA---ISANSKNPERAMMFLNLLnTDPYLRNLINYGIEGTHYKKVSDN---VIEDLPAMKDGFQMPGF---ALGNLFLT 402
Cdd:cd13581 307 GRGgfvITSKNKNPEAAIRWADFL-YSPEGSLQANFGPEGEDWEKNPDGeygVDGPPAAYKILEPSEGEqnvAWADGGPG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 403 YMHKE------DPADKWEAFKEFNNSAKVAPSFgfnFNPDSV------KTEVASISAIVKEFYPSI-------MTGAVDp 463
Cdd:cd13581 386 AIPDEyrlkqvTDEDMDEAEARLDEAKKYYEPY---APPDNSpppallDEEAEKISTIQTDINNYIeqkrakfITGGGD- 461
|
490 500
....*....|....*....|....*....
gi 516283654 464 DEHLPKAIEKLKAAGLDKVIAEAQKQYDE 492
Cdd:cd13581 462 DKEWDAYVKQLEKMGLDEYLEIYQKAYDR 490
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
71-490 |
1.89e-17 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 84.72 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 71 KYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIaFTSSWAYDYLPNATRGAFLPINDLLDK---YGQGI-KEQLDP 146
Cdd:cd13583 24 KEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDI-IPVLYPGEENEFVASGALLPISDYLDYmpnYKKYVeKWGLGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 147 RFLTGSQIDGQNYSVPVNKELA-SQWVWRFNKQYVDKYNMDITKirTLEDLEPYLQQIKDNEPaDITPLAVPKGFKPYLA 225
Cdd:cd13583 103 ELATGRQSDGKYYSLPGLHEDPgVQYSFLYRKDIFEKAGIKIPT--TWDEFYAALKKLKEKYP-DSYPYSDRWNSNALLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 226 FDFLL-------GDEFPvgiNMNGDTGKYVNMLESEELKSSLKTIRKYYQAGYLRKDVATLE---GIDNIKTGKWFVDRE 295
Cdd:cd13583 180 IAAPAfgttagwGFSNY---TYDPDTDKFVYGATTDEYKDMLQYFNKLYAEGLLDPESFTQTddqAKAKFLNGKSFVITT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 296 QTQPYAELGWSRSA----GYEIVTTPMQDP----VIFTGSAT-GAMhaISAN---SKNPERAMMFLNLLnTDPYLRNLIN 363
Cdd:cd13583 257 NPQTVDELQRNLRAadggNYEVVSITPPAGpagkAINGSRLEnGFM--ISSKakdSKNFEALLQFLDWL-YSDEGQELAT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 364 YGIEGTHYKKVSDNVIEDLPAMK-----DGFQMP----GFALGNLFLTYMHKEDPADKWEAFKEFNNS----AKVAPSfg 430
Cdd:cd13583 334 WGVEGETYTKEGDGKVYLADSNTpalnpSGTKLLqkdfGFSDGVFTDGGGTSGKLSEMTPEEAEFNDTmlenRKPVPP-- 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516283654 431 fNFNPDSVKTEVASISAI-------VKEFYPSIMTGaVDPDEHLPKAIEKLKAAGLDKVIAEAQKQY 490
Cdd:cd13583 412 -IPPPPMTEEELEQLSLLetplkdfVDEMTAKFITG-KRSMDEWDAFVAEVKKLGLDQLLDIYNDAY 476
|
|
| PBP2_AlgQ1_2 |
cd13584 |
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ... |
61-491 |
2.99e-13 |
|
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: 71.70 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 61 DLPMVQEemnkyLMEKINATVDitmidwgdySKRMPVITASGENYDIAFTS---------SWAYDYlPNATR----GAFL 127
Cdd:cd13584 19 DLPVYKE-----MERKTNVKLN---------FVANPVAQNSQEQFNLMMASgqlpdiiggDWLKDK-GGFEKygedGAFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 128 PINDLLDKYGQGIKEQLDPRFLTGSQI---DGQNYSVPVNKELASQWVWR---FNKQYVDKYNMDITKirTLEDLEPYLQ 201
Cdd:cd13584 84 PLNDLIDQYAPNLKKFLDEHPDVKKAIttdDGNIYGFPYLPDGDVAKEARgyfIRKDWLDKLGLKTPS--TIDEWYTVLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 202 QIKDNEP-----ADITPLAVPKgfkPYLAFDFLLGDEFpvGINMN--GDTGKYVNMLESEELKSSLKTIRKYYQAGYLRK 274
Cdd:cd13584 162 AFKERDPngngkADEVPLILTK---PGYDETGRLINAW--GAYMDfyQENGKVKYGPLEPGFKDFLKTMNQWYKEGLIDP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 275 DVAT--------LEGIDNIK--TGKWFvdreqTQPYAELGWSRSAGYEIVTTPMQDPVIFTGS----------ATGAMHA 334
Cdd:cd13584 237 DFFTrkakareqNIMNGNIGgfTHDWF-----ASTGTFNLALLKNVPDFKLVAVPPPVLNKGQtpyeedsrqiAKGDGAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 335 ISANSKNPERAMMFLNLLNTDPYlRNLINYGIEGTHYkkvsdNVIEDLPAMKDGFQMPGFALGNLFLTYMHKEDPADKWE 414
Cdd:cd13584 312 ITASNKNPVLAIKWLDYAYSEEG-RLLSNFGVEGESY-----TIKNGKPVFTDDVLKDPQPLVNALSLYYGAQIPGGFWQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 415 AfKEFNNSAKVAPSFGFNFNPDSVKTEV-------------------ASISAIVKEFYPSIMTGAVDPDEHLPKAIEKLK 475
Cdd:cd13584 386 D-YEYEEQWTTPEALESKDIYAKNKYVMplppvtlteeersiydsimTDIDTYVNEMGQKWIMGKEDADDNWDEYQKKLK 464
|
490
....*....|....*.
gi 516283654 476 AAGLDKVIAEAQKQYD 491
Cdd:cd13584 465 SLGLYEALEIQQAAYD 480
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
49-357 |
7.14e-13 |
|
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: 70.13 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 49 KLKVYMIGGPQRDlPMVQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFT-SSWAYDYlpnATRGAFL 127
Cdd:cd13585 1 TLTFWDWGQPAET-AALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVdGPWVPEF---ASNGALL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 128 PINDLLDKYGqgIKEQLDPRFLTGSQIDGQNYSVPVNkelASQWVWRFNKQYVDKYNMDITKIRTLEDLEPYLQQIKDNE 207
Cdd:cd13585 77 DLDDYIEKDG--LDDDFPPGLLDAGTYDGKLYGLPFD---ADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 208 PaDITPLAVP-KGFKPYLAFDFLL--GDEFpvginMNGDTGKYVnmLESEELKSSLKTIRKYYQAGYLRKDVATL--EGI 282
Cdd:cd13585 152 G-GQYGFALRgGSGGQTQWYPFLWsnGGDL-----LDEDDGKAT--LNSPEAVEALQFYVDLYKDGVAPSSATTGgdEAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 283 DNIKTGK--------WFVdREQTQPYAELGWsrsagyEIVTTPMQDPVIFTGSATGAMHAISANSKNPERAMMFLNLLNT 354
Cdd:cd13585 224 DLFASGKvammidgpWAL-GTLKDSKVKFKW------GVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS 296
|
...
gi 516283654 355 DPY 357
Cdd:cd13585 297 KEN 299
|
|
| PBP2_AlgQ_like_3 |
cd13582 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
89-492 |
1.79e-10 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270300 [Multi-domain] Cd Length: 504 Bit Score: 63.11 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 89 GDYSKRMPVITASGENYDIAFTSSwAYDYLPNAtrGAFLPINDLLDKYGQGIKEQLDPRFLTG-SQIDGQNYSVPvnkel 167
Cdd:cd13582 41 GGEKQKIGLMIASGDLPDLIYAKG-DTDKLIEA--GALVPLDDLIEKYGPNIKKWYGDYLLKKlRSEDGHIYYLP----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 168 asqwVWRFNKQYVDKY-----NMDITK------IRTLEDLEPYLQQIKDNEPaDITPL------AVPKGFKPYLAFD--- 227
Cdd:cd13582 113 ----NYRVEDAPWYPNggfwlQHDVLKelgypkIKTLDDYENLIKDYKKKYP-TINGQptigftALTDDWRFLISVTnpa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 228 FLLGDEFPVGINMNGDTGKYVNMLESEELKSSLKTIRKYYQAGYLRKDVATL---EGIDNIKTGK--WFVDREQTQPYAE 302
Cdd:cd13582 188 FLAGYPNDGEVYVDPKTLKAKFHYTRPYYKEYYKWLNELWNEGLLDKESFTQkydQYLAKIASGRvlGFYDAGWDIGNAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 303 LGWSRSAGYEIvtTPMQDPVIFT-----------GSATGAMHAISANSKNPERAMMFLNLLNTDPYLRnLINYGIEGTHY 371
Cdd:cd13582 268 TALKAKGKDER--LYAYYPVAVGvddkdynygdpGYLGGDGIAITKSCKDPERAFKFLDWLASEEAQK-LINWGIEGVDY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 372 KKVSDNVIEDLPAM-----------------------------KDG-FQMPGF-----ALGNLFLTYMHKEDPADKWEAF 416
Cdd:cd13582 345 DVDDGKRVYLTEEMaaknkdpdytkktgigkywyfpprkggkfSDGtGNSPTPdpeeeYIYTAVEKKVKAAYKAELWKDM 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 417 KEFNNSAKVAPSFG---FNFNPDSVKTEVASISAIVKEFYP-SIMTGAVDPDEHLPKAIEKLKAAGLDKVIAEAQKQYDE 492
Cdd:cd13582 425 FPPFEEFPVKPYGYawpIGIPDESIAIINQKASDITRKYIPkAIMAKPDDFDSIWDEYLKDLEKAGYKKLEEYYTKQIKE 504
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
78-355 |
4.07e-07 |
|
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270450 [Multi-domain] Cd Length: 386 Bit Score: 52.32 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 78 NATVDITMIDWGDYSKRMPVITASGENYDIA-FTSSWAYDYlpnATRGAFLPINDLLDKYGQGikEQLDPRFLTGSQIDG 156
Cdd:cd14747 29 GIEVKVQVLPWGDAHTKITTAAASGDGPDVVqLGNTWVAEF---AAMGALEDLTPYLEDLGGD--KDLFPGLVDTGTVDG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 157 QNYSVPvnkelasqWvwrfnkqYVDK----YNMDITK-------IRTLEDLEPYLQQIKDNEPaDITPLAVP-KGFKPYL 224
Cdd:cd14747 104 KYYGVP--------W-------YADTralfYRTDLLKkaggdeaPKTWDELEAAAKKIKADGP-DVSGFAIPgKNDVWHN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 225 AFDFLLGdefpvginmNGdtGKYVNM------LESEELKSSLKTIRKYYQAGYLRKDVATLEG-IDN---------IKTG 288
Cdd:cd14747 168 ALPFVWG---------AG--GDLATKdkwkatLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdVEQafangkvamIISG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516283654 289 KWFVDR-EQTQPYAELGWsrsAGYEIVTTPMQDPVIFTGsatGAMHAISANSKNPERAMMFLNLLNTD 355
Cdd:cd14747 237 PWEIGAiREAGPDLAGKW---GVAPLPGGPGGGSPSFAG---GSNLAVFKGSKNKDLAWKFIEFLSSP 298
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
75-474 |
7.32e-06 |
|
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: 48.06 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 75 EKINATVDITMIDWGDYSKRMPVITA---SGENYDIAF-TSSWAYDYlpnATRGAFLPINDLLDKYGQGIKeQLDPRFLT 150
Cdd:cd14748 24 NKSHPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQvDASWVAQL---ADSGALEPLDDYIDKDGVDDD-DFYPAALD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 151 GSQIDGQNYSVPVNKelaSQWVWRFNKQYVDKYNMDITK-IRTLEDLEPYLQQIKD-NEPADITPLAVPKGFKPYLAFDF 228
Cdd:cd14748 100 AGTYDGKLYGLPFDT---STPVLYYNKDLFEEAGLDPEKpPKTWDELEEAAKKLKDkGGKTGRYGFALPPGDGGWTFQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 229 LLGdefpvginmNGdtGKYVN------MLESEELKSSLKTIRKYYQAGYLRKDVATLEGIDNIKTGK--------WFV-D 293
Cdd:cd14748 177 LWQ---------NG--GDLLDedggkvTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKvamtingtWSLaG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 294 REQTQPYAELGwsrsagyeivTTPMqdPVIFTG----SATGAMHAISAN-SKNPERAMMFLNLLNTDPylrNLINYgIEG 368
Cdd:cd14748 246 IRDKGAGFEYG----------VAPL--PAGKGKkgatPAGGASLVIPKGsSKKKEAAWEFIKFLTSPE---NQAKW-AKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 369 THYkkvsdnviedLPAMKDgfqmpgfALGNLFLTYmhKEDPADKwEAFKEFNNSAKVAPSFGFNfnpdsvktevASISAI 448
Cdd:cd14748 310 TGY----------LPVRKS-------AAEDPEEFL--AENPNYK-VAVDQLDYAKPWGPPVPNG----------AEIRDE 359
|
410 420
....*....|....*....|....*.
gi 516283654 449 VKEFYPSIMTGAVDPDEHLPKAIEKL 474
Cdd:cd14748 360 LNEALEAALLGKKTPEEALKEAQEKI 385
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
56-357 |
7.05e-05 |
|
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: 44.71 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 56 GGPQRDLPMVQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGEN-YDIAFTSSWAYDYLpnATRGAFLPINDLLD 134
Cdd:pfam01547 1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGpADVFASDNDWIAEL--AKAGLLLPLDDYVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 135 KYGQGIKEQLdprfltgsqidgqnYSVPVNKElaSQWVWrFNKQYVDKYnmDITKIRTLEDLEPYLQQIKDNEPADI--- 211
Cdd:pfam01547 79 NYLVLGVPKL--------------YGVPLAAE--TLGLI-YNKDLFKKA--GLDPPKTWDELLEAAKKLKEKGKSPGgag 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 212 TPLAVPKGFKPYLAFDFLLGDEFPVGINMNGDTGKYVNMLESEE-LKSSLKTIRKYYQAGYLRKDVATLEG------IDN 284
Cdd:pfam01547 140 GGDASGTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVdLYAKVLLLKKLKNPGVAGADGREALAlfeqgkAAM 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516283654 285 IKTGKWFVDREQTQPYAELGWSRSAGYEIVTTPMQDPVIFTGSATGAMHAISANSKNPERAMMFLNLLNTDPY 357
Cdd:pfam01547 220 GIVGPWAALAANKVKLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
49-394 |
6.95e-03 |
|
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: 38.62 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 49 KLKVYMIGGPQRDLpmvQEEMNKYLMEKINATVDITMIDWGDYSKRMPVITASGENYDIAFtssWAYDYLPNA-TRGAFL 127
Cdd:cd13658 1 QLTVWVDEDKKMAF---IKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMV---APHDRIGSAvLQGLLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 128 PIndlldKYGQGIKEQLDPRFLTGSQIDGQNYSVPVNKELAsqwVWRFNKQYVDKynmditKIRTLEDLEPYLQQIKDNE 207
Cdd:cd13658 75 PI-----KLSKDKKKGFTDQALKALTYDGKLYGLPAAVETL---ALYYNKDLVKN------APKTFDELEALAKDLTKEK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 208 PADITPLAVPKGFkpYLAFDFLLG-DEFPVGINMNGDTGKYVNmLESEELKSSLKTIRKYYQAGYLRKDvATLEGIDN-- 284
Cdd:cd13658 141 GKQYGFLADATNF--YYSYGLLAGnGGYIFKKNGSDLDINDIG-LNSPGAVKAVKFLKKWYTEGYLPKG-MTGDVIQGlf 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516283654 285 -------IKTGKWfvdreQTQPYAELGwsrsAGYEIVTTP----MQDPVIFTGsatGAMHAISANSKNPERAMMFLNLLN 353
Cdd:cd13658 217 kegkaaaVIDGPW-----AIQEYQEAG----VNYGVAPLPtlpnGKPMAPFLG---VKGWYLSAYSKHKEWAQKFMEFLT 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 516283654 354 TDPYLRnlinygiegTHYKKVSdnvieDLPAMKDGFQMPGF 394
Cdd:cd13658 285 SKENLK---------KRYDETN-----EIPPRKDVRSDPEI 311
|
|
| |
