|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
11-365 |
1.54e-37 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 140.18 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 11 LVIAGALGLAISATACGTGDNDGSGKAdspecaayqkyqghGGAEVSIYASiRDAEADLLEQSWEQF-AECTGIEIDYE- 88
Cdd:COG1653 4 LALALAAALALALAACGGGGSGAAAAA--------------GKVTLTVWHT-GGGEAAALEALIKEFeAEHPGIKVEVEs 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 89 -GSGEFEAQLQVRVDGGNAPDIAFVPQPGLlSRFAQAGKLKPAS--AETKAMAEENYAADWLKYSTVAGQFYGAPLGSNV 165
Cdd:COG1653 69 vPYDDYRTKLLTALAAGNAPDVVQVDSGWL-AEFAAAGALVPLDdlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 166 KSFvWYSPKMFQEQGWTVPTTWDDLIKLSDS-AAAGGIKPWCVGiesgdatGWPATDWIEdvLLRTQTPEVYDQWTThgM 244
Cdd:COG1653 148 LGL-YYNKDLFEKAGLDPPKTWDELLAAAKKlKAKDGVYGFALG-------GKDGAAWLD--LLLSAGGDLYDEDGK--P 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 245 PFNDQRVVDAVDRAGTiLRNEKYVNggyggvKSIATTSFQEGGLPILQGECALHRQASFYANQWPADsrvAEDGDVFAFY 324
Cdd:COG1653 216 AFDSPEAVEALEFLKD-LVKDGYVP------PGALGTDWDDARAAFASGKAAMMINGSWALGALKDA---APDFDVGVAP 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 515214725 325 FPAIDPSKGKPVLGGGEFTVAF---DDRPEVQAVQTYLASGEYA 365
Cdd:COG1653 286 LPGGPGGKKPASVLGGSGLAIPkgsKNPEAAWKFLKFLTSPEAQ 329
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
96-444 |
7.04e-18 |
|
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: 85.12 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 96 QLQVRVDGGNAPDIAFVPQPGLLSRFAQAGKLKPASAETKAMAEENYAADWL-KYSTVAGQFYGAPLGSNVKSFVWYSPK 174
Cdd:cd14749 46 KLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNGVDKRFLPGLaDAVTFNGKVYGIPFAARALALFYNKDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 175 MFQEQGWTVPTTWDDLIKLSDSAAAGGIKPwcVGIesGDATGWPATDWIEDVLLRTQTPEVYDQWTTHGMPFNDQRVVDA 254
Cdd:cd14749 126 FEEAGGVKPPKTWDELIEAAKKDKFKAKGQ--TGF--GLLLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFNDPAFVQA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 255 VDRAgTILRNEKYVNGGYGGVKsiattsFQEGGLPILQGECALHRQASFYAnqwpADSRVAEDGDVF-AFYFPAIDPSKG 333
Cdd:cd14749 202 LQKL-QDLVKAGAFQEGFEGID------YDDAGQAFAQGKAAMNIGGSWDL----GAIKAGEPGGKIgVFPFPTVGKGAQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 334 KPVLGGGEFTVAFDDRPEVQ--AVQ--TYLASGEYANSRAKLGNWVSANRKLDVANVANPIDKLSVEILQDES--TVFRF 407
Cdd:cd14749 271 TSTIGGSDWAIAISANGKKKeaAVKflKYLTSPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFADVLNAagSTPFL 350
|
330 340 350
....*....|....*....|....*....|....*....
gi 515214725 408 DgsdlmPAAVGAGTFWKEMVS--WISGKDTKAALDAIES 444
Cdd:cd14749 351 D-----EYWPAAAQVHKDAVQklLTGKIDPEQVVKQAQS 384
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
65-360 |
8.42e-13 |
|
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: 68.60 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 65 AEADLLEQSWEQF-AECTGIEIDYE--GSGEFEAQLQVRVDGGNAPDIAFVPQPGLLSRFAQAGKLKPASAETKamaeeN 141
Cdd:pfam01547 5 TEAAALQALVKEFeKEHPGIKVEVEsvGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVA-----N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 142 YAADWlkystvAGQFYGAPLGSNVkSFVWYSPKMFQEQGWTVPTTWDDLIKLSDSAAAGGIKPWCVgiesGDATGWPATD 221
Cdd:pfam01547 80 YLVLG------VPKLYGVPLAAET-LGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGA----GGGDASGTLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 222 WIEDVLLRTQTPEVYDQWtthGMPFNDQRVVDAVDrAGTILRNEKYVNGGYGGvKSIATTSFQEGGLPILQGECAL---H 298
Cdd:pfam01547 149 YFTLALLASLGGPLFDKD---GGGLDNPEAVDAIT-YYVDLYAKVLLLKKLKN-PGVAGADGREALALFEQGKAAMgivG 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515214725 299 RQASFYANQWPADSRVAEDGDVFAFYFPAIDPSKGKPVLGGGEFTVAFDDRPEVQAVQTYLA 360
Cdd:pfam01547 224 PWAALAANKVKLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLD 285
|
|
| chitin_NgcE |
TIGR03851 |
carbohydrate ABC transporter, N-acetylglucosamine/diacetylchitobiose-binding protein; Members ... |
82-205 |
1.17e-09 |
|
carbohydrate ABC transporter, N-acetylglucosamine/diacetylchitobiose-binding protein; Members of this protein family are the substrate-binding protein, a lipid-anchored protein of Gram-positive bacteria in all examples found so far, that include NgcE of the chitin-degrader, Streptomyces olivaceoviridis, and close homologs from other species likely to share the same function. NgcE binds both N-acetylglucosamine and the chitin dimer, N,N'-diacetylchitobiose. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274816 Cd Length: 450 Bit Score: 60.11 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 82 GIEIDYEGSGEFEAQLQVRVDGGNAPDIAFVPQPGLL--SRFAQAGKLKPASAETKAMAEENYA---ADWLKYSTVA-GQ 155
Cdd:TIGR03851 69 GATVKVSPTQKIAPQLQPRFAGGNPPDLIDNSGADAMdmSALVAEGQLEDLTPLFDAPSWDDPGkkvRDTLLPGVLEpGT 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 515214725 156 FYGAPLGSNVKSFV---WYSPKMFQEQGWTVPTTWDDLIKLSDSAAAGGIKPW 205
Cdd:TIGR03851 149 FDGKPYALNYVYTVyglWYSATLFEENGWTPPKTWDEFLALGEEAKAKGIAPF 201
|
|
| PRK15046 |
PRK15046 |
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
6-191 |
5.37e-04 |
|
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 41.98 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 6 RPRQALVIAGALGLAISATACGTGdndgsgkadspeCAAyqkyqGHGGAEVSIYASirDAEADLLEQSWEQFAECTGIEI 85
Cdd:PRK15046 4 TNRAAAAAAMKLAAAAAAAAFGGG------------AAP-----AWAADAVTVYSA--DGLEDWYQDVFPAFTKATGIKV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 86 DY--EGSGEFEAQLQVRVDGGNAPDIafVPQPGLLSRFAQAGKLKP-ASAETKAMAEENYAADWlKYSTVAGqfygaplg 162
Cdd:PRK15046 65 NYveAGSGEVVNRAAKEKSNPQADVL--VTLPPFIQQAAAEGLLQPySSVNAKAVPAIAKDADG-TYAPFVN-------- 133
|
170 180
....*....|....*....|....*....
gi 515214725 163 sNVKSFVwYSPKMFQEQgwtvPTTWDDLI 191
Cdd:PRK15046 134 -NYLSFI-YNPKVLKTA----PATWADLL 156
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
11-365 |
1.54e-37 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 140.18 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 11 LVIAGALGLAISATACGTGDNDGSGKAdspecaayqkyqghGGAEVSIYASiRDAEADLLEQSWEQF-AECTGIEIDYE- 88
Cdd:COG1653 4 LALALAAALALALAACGGGGSGAAAAA--------------GKVTLTVWHT-GGGEAAALEALIKEFeAEHPGIKVEVEs 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 89 -GSGEFEAQLQVRVDGGNAPDIAFVPQPGLlSRFAQAGKLKPAS--AETKAMAEENYAADWLKYSTVAGQFYGAPLGSNV 165
Cdd:COG1653 69 vPYDDYRTKLLTALAAGNAPDVVQVDSGWL-AEFAAAGALVPLDdlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 166 KSFvWYSPKMFQEQGWTVPTTWDDLIKLSDS-AAAGGIKPWCVGiesgdatGWPATDWIEdvLLRTQTPEVYDQWTThgM 244
Cdd:COG1653 148 LGL-YYNKDLFEKAGLDPPKTWDELLAAAKKlKAKDGVYGFALG-------GKDGAAWLD--LLLSAGGDLYDEDGK--P 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 245 PFNDQRVVDAVDRAGTiLRNEKYVNggyggvKSIATTSFQEGGLPILQGECALHRQASFYANQWPADsrvAEDGDVFAFY 324
Cdd:COG1653 216 AFDSPEAVEALEFLKD-LVKDGYVP------PGALGTDWDDARAAFASGKAAMMINGSWALGALKDA---APDFDVGVAP 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 515214725 325 FPAIDPSKGKPVLGGGEFTVAF---DDRPEVQAVQTYLASGEYA 365
Cdd:COG1653 286 LPGGPGGKKPASVLGGSGLAIPkgsKNPEAAWKFLKFLTSPEAQ 329
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
6-446 |
4.26e-18 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 85.77 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 6 RPRQALVIAGALGLAISATACGTGDNDGSGKADSpecaayqkyqghgGAEVSIYASIRDAEADLLEQSWEQFAECTGIEI 85
Cdd:COG2182 2 KRRLLAALALALALALALAACGSGSSSSGSSSAA-------------GAGGTLTVWVDDDEAEALEEAAAAFEEEPGIKV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 86 DYE--GSGEFEAQLQVRVDGGNAPDIAFVPQPGLlSRFAQAGKLKPASaETKAMAEENYAADWlKYSTVAGQFYGAPLGS 163
Cdd:COG2182 69 KVVevPWDDLREKLTTAAPAGKGPDVFVGAHDWL-GELAEAGLLAPLD-DDLADKDDFLPAAL-DAVTYDGKLYGVPYAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 164 NVkSFVWYSPKMFQEqgwTVPTTWDDLIKLSDSAAAGGIKPWCVGIESG-------DATGWPATDwiedvllrtQTPEVY 236
Cdd:COG2182 146 ET-LALYYNKDLVKA---EPPKTWDELIAAAKKLTAAGKYGLAYDAGDAyyfypflAAFGGYLFG---------KDGDDP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 237 DQWTthgmpFNDQRVVDAVDRAGTiLRNEKYVNGGYGGvkSIATTSFQEGglpilqgecalhrQASFYANqWP---ADSR 313
Cdd:COG2182 213 KDVG-----LNSPGAVAALEYLKD-LIKDGVLPADADY--DAADALFAEG-------------KAAMIIN-GPwaaADLK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 314 VAEDGDVFAFYFPAIDPSK-GKPVLGGGEFTV-AFDDRPEV-QAVQTYLASGEYANSRAKLGNWVSANRKL--DVANVAN 388
Cdd:COG2182 271 KALGIDYGVAPLPTLAGGKpAKPFVGVKGFGVsAYSKNKEAaQEFAEYLTSPEAQKALFEATGRIPANKAAaeDAEVKAD 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515214725 389 PIDKLSVEILQDestvfrfdgSDLMPAAVGAGTFWKEM----VSWISGKDT-KAALDAIESSW 446
Cdd:COG2182 351 PLIAAFAEQAEY---------AVPMPNIPEMGAVWTPLgtalQAIASGKADpAEALDAAQKQI 404
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
96-444 |
7.04e-18 |
|
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: 85.12 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 96 QLQVRVDGGNAPDIAFVPQPGLLSRFAQAGKLKPASAETKAMAEENYAADWL-KYSTVAGQFYGAPLGSNVKSFVWYSPK 174
Cdd:cd14749 46 KLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNGVDKRFLPGLaDAVTFNGKVYGIPFAARALALFYNKDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 175 MFQEQGWTVPTTWDDLIKLSDSAAAGGIKPwcVGIesGDATGWPATDWIEDVLLRTQTPEVYDQWTTHGMPFNDQRVVDA 254
Cdd:cd14749 126 FEEAGGVKPPKTWDELIEAAKKDKFKAKGQ--TGF--GLLLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFNDPAFVQA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 255 VDRAgTILRNEKYVNGGYGGVKsiattsFQEGGLPILQGECALHRQASFYAnqwpADSRVAEDGDVF-AFYFPAIDPSKG 333
Cdd:cd14749 202 LQKL-QDLVKAGAFQEGFEGID------YDDAGQAFAQGKAAMNIGGSWDL----GAIKAGEPGGKIgVFPFPTVGKGAQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 334 KPVLGGGEFTVAFDDRPEVQ--AVQ--TYLASGEYANSRAKLGNWVSANRKLDVANVANPIDKLSVEILQDES--TVFRF 407
Cdd:cd14749 271 TSTIGGSDWAIAISANGKKKeaAVKflKYLTSPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFADVLNAagSTPFL 350
|
330 340 350
....*....|....*....|....*....|....*....
gi 515214725 408 DgsdlmPAAVGAGTFWKEMVS--WISGKDTKAALDAIES 444
Cdd:cd14749 351 D-----EYWPAAAQVHKDAVQklLTGKIDPEQVVKQAQS 384
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
64-446 |
1.12e-14 |
|
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: 75.13 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 64 DAEADLLEQSWEQF-AECTGIEIDYEGSGE--FEAQLQVRVDGGNAPDIAFVPQPGlLSRFAQAGKLKP-ASAETKAMAE 139
Cdd:cd13585 10 PAETAALKKLIDAFeKENPGVKVEVVPVPYddYWTKLTTAAAAGTAPDVFYVDGPW-VPEFASNGALLDlDDYIEKDGLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 140 ENYAADWLKYSTVAGQFYGAPLGSNVkSFVWYSPKMFQEQGW--TVPTTWDDLIKLS--DSAAAGGIKPWCVGIESGDAT 215
Cdd:cd13585 89 DDFPPGLLDAGTYDGKLYGLPFDADT-LVLFYNKDLFDKAGPgpKPPWTWDELLEAAkkLTDKKGGQYGFALRGGSGGQT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 216 GWpatdwieDVLLRTQTPEVYDQWTTHGMpFNDQRVVDAVdragtilrnEKYVNG-GYGGVKSIATTSFQEGGLPILQGE 294
Cdd:cd13585 168 QW-------YPFLWSNGGDLLDEDDGKAT-LNSPEAVEAL---------QFYVDLyKDGVAPSSATTGGDEAVDLFASGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 295 CALHRQASFYANQwpadSRVAEDGDVFAF-YFPAIDPSKGKPVLGGGEFTV-AFDDRPEvQAVQ--TYLASGEyANSRAK 370
Cdd:cd13585 231 VAMMIDGPWALGT----LKDSKVKFKWGVaPLPAGPGGKRASVLGGWGLAIsKNSKHPE-AAWKfiKFLTSKE-NQLKLG 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515214725 371 LGNWVSANRKLDVANVANPIDKLSVEILQDESTVFRFDGSDLMPAAVGAGTFWKEMVSWISG---KDTKAALDAIESSW 446
Cdd:cd13585 305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalgKSPEEALKEAAKEI 383
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
65-360 |
8.42e-13 |
|
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: 68.60 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 65 AEADLLEQSWEQF-AECTGIEIDYE--GSGEFEAQLQVRVDGGNAPDIAFVPQPGLLSRFAQAGKLKPASAETKamaeeN 141
Cdd:pfam01547 5 TEAAALQALVKEFeKEHPGIKVEVEsvGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVA-----N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 142 YAADWlkystvAGQFYGAPLGSNVkSFVWYSPKMFQEQGWTVPTTWDDLIKLSDSAAAGGIKPWCVgiesGDATGWPATD 221
Cdd:pfam01547 80 YLVLG------VPKLYGVPLAAET-LGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGA----GGGDASGTLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 222 WIEDVLLRTQTPEVYDQWtthGMPFNDQRVVDAVDrAGTILRNEKYVNGGYGGvKSIATTSFQEGGLPILQGECAL---H 298
Cdd:pfam01547 149 YFTLALLASLGGPLFDKD---GGGLDNPEAVDAIT-YYVDLYAKVLLLKKLKN-PGVAGADGREALALFEQGKAAMgivG 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515214725 299 RQASFYANQWPADSRVAEDGDVFAFYFPAIDPSKGKPVLGGGEFTVAFDDRPEVQAVQTYLA 360
Cdd:pfam01547 224 PWAALAANKVKLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLD 285
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
55-381 |
8.74e-12 |
|
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: 66.55 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 55 EVSIYASIRDAEADLLEQSWEQFAECTG---IEIDYEG--SGEFEAQLQVRVDGGN-APDIAFVPQPgLLSRFAQAGKLK 128
Cdd:cd14750 1 TITFAAGSDGQEGELLKKAIAAFEKKHPdikVEIEELPasSDDQRQQLVTALAAGSsAPDVLGLDVI-WIPEFAEAGWLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 129 PASAETKAMAEENYAADWLKYSTVAGQFYGAPLGSNVKsFVWYSPKMFQEQGWTVPTTWDDLIKLSDSAAAGGIKPWCVG 208
Cdd:cd14750 80 PLTEYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAG-LLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEPGIWGYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 209 IESGDATGWPaTDWIEdvLLRTQTPEVYD----QWTthgmpFNDQRVVDAVDRAGTiLRNEKYVNGG-YGGVKSIATTSF 283
Cdd:cd14750 159 FQGKQYEGLV-CNFLE--LLWSNGGDIFDddsgKVT-----VDSPEALEALQFLRD-LIGEGISPKGvLTYGEEEARAAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 284 QEGglpilqgecalhrQASFYANqWP--------ADSRVAedgDVFAFY-FPAIDPSKGKPVLGGGEFTV-AFDDRPEV- 352
Cdd:cd14750 230 QAG-------------KAAFMRN-WPyayallqgPESAVA---GKVGVApLPAGPGGGSASTLGGWNLAIsANSKHKEAa 292
|
330 340
....*....|....*....|....*....
gi 515214725 353 QAVQTYLASGEYANSRAKLGNWVSANRKL 381
Cdd:cd14750 293 WEFVKFLTSPEVQKRRAINGGLPPTRRAL 321
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
83-444 |
1.40e-11 |
|
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: 65.78 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 83 IEIDYEGSGEFEAQ-LQVRVDGGNAPDIAFVPqPGLLSRFAQAGKLKPASAETKAMA--EENYAADWLKYSTVAGQFYGA 159
Cdd:cd14748 32 VKAVYQGSYDDTLTkLLAALAAGTAPDVAQVD-ASWVAQLADSGALEPLDDYIDKDGvdDDDFYPAALDAGTYDGKLYGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 160 PLGSNVKSFvWYSPKMFQEQGW---TVPTTWDDLI----KLSDsaAAGGIKPWCVGIESGDATGWPATdwiedvLLRTQT 232
Cdd:cd14748 111 PFDTSTPVL-YYNKDLFEEAGLdpeKPPKTWDELEeaakKLKD--KGGKTGRYGFALPPGDGGWTFQA------LLWQNG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 233 PEVYDQWTTHGMpFNDQRVVDAVdragtilrneKYVNGGYGGVKSIATTSFQEGGLPILQGECALHRQASFYanqWPADS 312
Cdd:cd14748 182 GDLLDEDGGKVT-FNSPEGVEAL----------EFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWS---LAGIR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 313 RVAEDGDVFAFYFPAIDPSKGKPVLGGGEFTVaFDDRPEVQ--AVQ--TYLASGEYANSRAKLGNWVSANRKLDVANV-- 386
Cdd:cd14748 248 DKGAGFEYGVAPLPAGKGKKGATPAGGASLVI-PKGSSKKKeaAWEfiKFLTSPENQAKWAKATGYLPVRKSAAEDPEef 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515214725 387 --ANPIDKLSVEILQdestvfrfDGSDLMPAAVGAGTFWKEMVSWI-----SGKDTKAALDAIES 444
Cdd:cd14748 327 laENPNYKVAVDQLD--------YAKPWGPPVPNGAEIRDELNEALeaallGKKTPEEALKEAQE 383
|
|
| chitin_NgcE |
TIGR03851 |
carbohydrate ABC transporter, N-acetylglucosamine/diacetylchitobiose-binding protein; Members ... |
82-205 |
1.17e-09 |
|
carbohydrate ABC transporter, N-acetylglucosamine/diacetylchitobiose-binding protein; Members of this protein family are the substrate-binding protein, a lipid-anchored protein of Gram-positive bacteria in all examples found so far, that include NgcE of the chitin-degrader, Streptomyces olivaceoviridis, and close homologs from other species likely to share the same function. NgcE binds both N-acetylglucosamine and the chitin dimer, N,N'-diacetylchitobiose. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274816 Cd Length: 450 Bit Score: 60.11 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 82 GIEIDYEGSGEFEAQLQVRVDGGNAPDIAFVPQPGLL--SRFAQAGKLKPASAETKAMAEENYA---ADWLKYSTVA-GQ 155
Cdd:TIGR03851 69 GATVKVSPTQKIAPQLQPRFAGGNPPDLIDNSGADAMdmSALVAEGQLEDLTPLFDAPSWDDPGkkvRDTLLPGVLEpGT 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 515214725 156 FYGAPLGSNVKSFV---WYSPKMFQEQGWTVPTTWDDLIKLSDSAAAGGIKPW 205
Cdd:TIGR03851 149 FDGKPYALNYVYTVyglWYSATLFEENGWTPPKTWDEFLALGEEAKAKGIAPF 201
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
72-280 |
4.86e-09 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 57.03 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 72 QSWEQFAECTGIEIDYE--GSGEFEAQLQVRVDGGNAPDIA-FVPQPGLLSRFAQAGKLKPASAETKAmaeeNYAADWLK 148
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEpqASNDLQAKLLAAAAAGNAPDLDvVWIAADQLATLAEAGLLADLSDVDNL----DDLPDALD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 149 YSTVAGQFYGAPLGSNVKSFVWYSPKMFQEQGwTVPTTWDDLIKLSDSAaaggikPWCVGIeSGDATGW-PATDWIEDVL 227
Cdd:pfam13416 77 AAGYDGKLYGVPYAASTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAKL------KGKTGL-TDPATGWlLWALLADGVD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515214725 228 LrTQTPEVYDQWtthgmpfndqrvVDAVDRAGTILRNEKYVNGGYGGVKSIAT 280
Cdd:pfam13416 149 L-TDDGKGVEAL------------DEALAYLKKLKDNGKVYNTGADAVQLFAN 188
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
64-217 |
6.07e-09 |
|
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: 57.39 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 64 DAEADLLEQSWEQF-AECTGIEIDYEGS--GEFEAQLQVRVDGGNAPD-----IAFVPQpgllsrFAQAGKLKPASAETK 135
Cdd:cd14751 10 DEEKVLYEKLIPAFeKEYPKIKVKAVRVpfDGLHNQIKTAAAGGQAPDvmradIAWVPE------FAKLGYLQPLDGTPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 136 AMAEENYAADWLKYSTVAGQFYGAPLGSNVKSFVwYSPKMFQEQGWTVPTTWDDLIklsdsAAAGGIKpwcvgiESGDAT 215
Cdd:cd14751 84 FDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALF-YNKRLLEEAGTEVPKTMDELV-----AAAKAIK------KKKGRY 151
|
..
gi 515214725 216 GW 217
Cdd:cd14751 152 GL 153
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
74-192 |
3.85e-06 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 48.39 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 74 WEQFAECTGIEIDYE--GSGEFEAQLQVrvDGGNAP-DIAFVPQPGLLSRFAQAGKLKP-ASAETKAMAEENYAADwlky 149
Cdd:COG1840 2 LEAFEKKTGIKVNVVrgGSGELLARLKA--EGGNPPaDVVWSGDADALEQLANEGLLQPyKSPELDAIPAEFRDPD---- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 515214725 150 stvaGQFYGapLGSNVKSFVwYSPKMFQEQGwtVPTTWDDLIK 192
Cdd:COG1840 76 ----GYWFG--FSVRARVIV-YNTDLLKELG--VPKSWEDLLD 109
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
55-196 |
5.00e-06 |
|
The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270375 [Multi-domain] Cd Length: 368 Bit Score: 48.53 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 55 EVSIYASIRDAEADLLEQSWEQFAECTGIE---IDYEGSGEFEAQLQVRVDGGNAPDIAFVPQPGLLsRFAQAGKLKPAS 131
Cdd:cd13657 1 TITIWHALTGAEEDALQQIIDEFEAKYPVPnvkVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIG-QFAEAGLLVPIS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515214725 132 AETKAMAEENYAADWLKYSTVAGQFYGAPLGSNVKSFVwYSPKMFQeqgwTVPTTWDDLIKLSDS 196
Cdd:cd13657 80 DYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALI-YNKALVD----QPPETTDELLAIMKD 139
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
64-194 |
1.74e-05 |
|
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: 46.52 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 64 DAEADLLEQSWEQFAECTGIEIDYE--GSGEFEAQLQVRVDGGNAPDIAFVPQPGLlSRFAQAGKLKP-ASAETKAMAEE 140
Cdd:cd13586 9 DGELEYLKELAEEFEKKYGIKVEVVyvDSGDTREKFITAGPAGKGPDVFFGPHDWL-GELAAAGLLAPiPEYLAVKIKNL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 515214725 141 NYAadwLKYSTVAGQFYGAPLgsNVKSFV-WYSPKMFQEqgwtVPTTWDDLIKLS 194
Cdd:cd13586 88 PVA---LAAVTYNGKLYGVPV--SVETIAlFYNKDLVPE----PPKTWEELIALA 133
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
74-190 |
3.04e-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: 46.20 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 74 WEQFAECTGIEIDYE--GSGEFEAQLQVRVDGGNAPDIAFVPQPGLLSRFAQAGKLKPASAETKAMAeeNYAA------D 145
Cdd:cd13583 23 WKEIEEKTNVKFKRTpiPSSDYETKRSLLIASGDAPDIIPVLYPGEENEFVASGALLPISDYLDYMP--NYKKyvekwgL 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515214725 146 WLKYSTVA---GQFY---GAPLGSNVKSFVWYSPKMFQEQGWTVPTTWDDL 190
Cdd:cd13583 101 GKELATGRqsdGKYYslpGLHEDPGVQYSFLYRKDIFEKAGIKIPTTWDEF 151
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
55-190 |
5.48e-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: 270298 [Multi-domain] Cd Length: 471 Bit Score: 45.40 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 55 EVSIYASIRDAEADLLEQS--WEQFAECTGIEIDYE--GSGEFEAQLQVRVDGGNAPDIAFVPQPGLLSRFAQAGKLKP- 129
Cdd:cd13580 4 TITIVANLGGNPKPDPDDNpyTKYLEEKTNIDVKVKwvPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLVKQGALWDl 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515214725 130 ------ASAETKAMAEENyaadWLKYSTVAGQFYGAPLGSNVKS--FVWYspkmfqEQGW------TVPTTWDDL 190
Cdd:cd13580 84 tdyldkYYPNLKKIIEQE----GWDSASVDGKIYGIPRKRPLIGrnGLWI------RKDWldklglEVPKTLDEL 148
|
|
| PRK15046 |
PRK15046 |
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
6-191 |
5.37e-04 |
|
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 41.98 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 6 RPRQALVIAGALGLAISATACGTGdndgsgkadspeCAAyqkyqGHGGAEVSIYASirDAEADLLEQSWEQFAECTGIEI 85
Cdd:PRK15046 4 TNRAAAAAAMKLAAAAAAAAFGGG------------AAP-----AWAADAVTVYSA--DGLEDWYQDVFPAFTKATGIKV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 86 DY--EGSGEFEAQLQVRVDGGNAPDIafVPQPGLLSRFAQAGKLKP-ASAETKAMAEENYAADWlKYSTVAGqfygaplg 162
Cdd:PRK15046 65 NYveAGSGEVVNRAAKEKSNPQADVL--VTLPPFIQQAAAEGLLQPySSVNAKAVPAIAKDADG-TYAPFVN-------- 133
|
170 180
....*....|....*....|....*....
gi 515214725 163 sNVKSFVwYSPKMFQEQgwtvPTTWDDLI 191
Cdd:PRK15046 134 -NYLSFI-YNPKVLKTA----PATWADLL 156
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
64-217 |
4.80e-03 |
|
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: 39.22 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 64 DAEADLLEQSWEQFAECT-GIEIDYE--GSGEFEAQLQVRVDGGNAPDIA-----FVPQpgllsrFAQAGKLKPASAETK 135
Cdd:cd14747 10 SAEAELLKELADEFEKENpGIEVKVQvlPWGDAHTKITTAAASGDGPDVVqlgntWVAE------FAAMGALEDLTPYLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 136 AMAEENYAADWLKYS-TVAGQFYGAPLGSNVKSFVwYSPKMFQEQGWT-VPTTWDDLIKLSDSAAAGGIKPWCVGIEsGD 213
Cdd:cd14747 84 DLGGDKDLFPGLVDTgTVDGKYYGVPWYADTRALF-YRTDLLKKAGGDeAPKTWDELEAAAKKIKADGPDVSGFAIP-GK 161
|
....
gi 515214725 214 ATGW 217
Cdd:cd14747 162 NDVW 165
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| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
70-201 |
8.93e-03 |
|
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: 38.35 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515214725 70 LEQSWEQFAECTGIEIDYEGSGEFEAQLQVRVDGGNAPDIAFVPQpGLLSRFAQAGKLKPASAEtKAMAEENYAADWLKY 149
Cdd:cd13656 16 LAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAH-DRFGGYAQSGLLAEITPD-KAFQDKLYPFTWDAV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 515214725 150 sTVAGQFYGAPLGSNVKSFVWYspkmfQEQGWTVPTTWDDLIKLSDSAAAGG 201
Cdd:cd13656 94 -RYNGKLIAYPIAVEALSLIYN-----KDLLPNPPKTWEEIPALDKELKAKG 139
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