|
Name |
Accession |
Description |
Interval |
E-value |
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-420 |
2.11e-127 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 373.90 E-value: 2.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 1 MRKTLFRAATVVAAMSL-LAACGGGDEAPaetqepttaeTSAAPAGATGSLTIWVDENRKPAVQAAVDIYNEtNPDVKVE 79
Cdd:COG2182 1 MKRRLLAALALALALALaLAACGSGSSSS----------GSSSAAGAGGTLTVWVDDDEAEALEEAAAAFEE-EPGIKVK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 80 LVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVDLG-AKAGEFEAVATQAFTYDGQMYGLPYALETIA 158
Cdd:COG2182 70 VVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDlADKDDFLPAALDAVTYDGKLYGVPYAVETLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 159 VVRNAALVDST-PETWDEMIAAGKE--AGTKYPFVINTngttGDAYTYYGLQTSFGAPVFvqNEDGSYTSELGMGGDEGF 235
Cdd:COG2182 150 LYYNKDLVKAEpPKTWDELIAAAKKltAAGKYGLAYDA----GDAYYFYPFLAAFGGYLF--GKDGDDPKDVGLNSPGAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 236 AFADFLAEngMKGEGHFSTDWTYDVANQEFSDGNAPYTIAGPWAIQTFKDA-GIDVAVDPIPS-AGGETAAPFVGVQGFY 313
Cdd:COG2182 224 AALEYLKD--LIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTlAGGKPAKPFVGVKGFG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 314 LSAQSESKLIANDFlVNYVATPEVIKALYDADPRLPAMTSVAD--EVASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWN 391
Cdd:COG2182 302 VSAYSKNKEAAQEF-AEYLTSPEAQKALFEATGRIPANKAAAEdaEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLG 380
|
410 420
....*....|....*....|....*....
gi 336105116 392 AAEASIISGSAKPKDAWTKMLADLESAIG 420
Cdd:COG2182 381 TALQAIASGKADPAEALDAAQKQIEAAIA 409
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
50-413 |
1.38e-101 |
|
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: 306.53 E-value: 1.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 50 LTIWVDEN-RKPAVQAAVDIYNETNpDVKVELVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVDLG- 127
Cdd:cd13586 2 ITVWTDEDgELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 128 AKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAALVDSTPETWDEMIAAGK----EAGTKYPFVINTNgttgDAYTY 203
Cdd:cd13586 81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfndKAGGKYGFAYDQT----NPYFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 204 YGLQTSFGAPVFVQNEDGsyTSELGMGGDEGFAFADFLAENGmKGEGHFSTDWTYDVANQEFSDGNAPYTIAGPWAIQTF 283
Cdd:cd13586 157 YPFLAAFGGYVFGENGGD--PTDIGLNNEGAVKGLKFIKDLK-KKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 284 KDAGIDVAVDPIPS-AGGETAAPFVGVQGFYLSAQSESKLIANDFLVNYVaTPEVIKALYDADPRLPAMTSV--ADEVAS 360
Cdd:cd13586 234 KDAGINFGVAPLPTlPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLT-SDEAQLLLFEKTGRIPALKDAlnDAAVKN 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 336105116 361 DPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDAWTKMLA 413
Cdd:cd13586 313 DPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVA 365
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
50-407 |
1.14e-71 |
|
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: 229.68 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 50 LTIWVDENRKPA-VQAAVDIYNETNpDVKVELVQ----KNFEDIRADflaqVPTGEGPDITIGAHDWLGSFIVNGVAEPV 124
Cdd:cd13658 2 LTVWVDEDKKMAfIKKIAKQYTKKT-GVKVKLVEvdqlDQLEKLSLD----GPAGKGPDVMVAPHDRIGSAVLQGLLSPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 125 DLG-AKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAALVDSTPETWDEMIAAGK----EAGTKYPFVINTNgttgD 199
Cdd:cd13658 77 KLSkDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKdltkEKGKQYGFLADAT----N 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 200 AYTYYGLQTSFGAPVFVQNEDGSYTSELGMGGDEGFAFADFLAEngMKGEGHFSTDWTYDVANQEFSDGNAPYTIAGPWA 279
Cdd:cd13658 153 FYYSYGLLAGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKK--WYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 280 IQTFKDAGIDVAVDPIPS-AGGETAAPFVGVQGFYLSAQSESKLIANDFlVNYVATPEVIKALYDADPRLPAMTSVAD-- 356
Cdd:cd13658 231 IQEYQEAGVNYGVAPLPTlPNGKPMAPFLGVKGWYLSAYSKHKEWAQKF-MEFLTSKENLKKRYDETNEIPPRKDVRSdp 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 336105116 357 EVASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDA 407
Cdd:cd13658 310 EIKNNPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQA 360
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
49-407 |
1.14e-66 |
|
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: 216.47 E-value: 1.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 49 SLTIW--VDENRKPAVQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD- 125
Cdd:cd13657 1 TITIWhaLTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 126 --LGAKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAALVDSTPETWDEMIAAGKE----AGTKYPFVINTNgttgD 199
Cdd:cd13657 81 ylSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDhtdpAAGSYGLAYQVS----D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 200 AYTYYGLQTSFGAPVFVQNedgsyTSELGMGGDEGFAFADFLAENGMKgegHFSTDWTYDVANQEFSDGNAPYTIAGPWA 279
Cdd:cd13657 157 AYFVSAWIFGFGGYYFDDE-----TDKPGLDTPETIKGIQFLKDFSWP---YMPSDPSYNTQTSLFNEGKAAMIINGPWF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 280 IQTFKDAGIDVAVDPIPSAGGETA-APFVGVQGFYLS--AQSESKLIANDFLvNYVATPEVIKALYDADPRLPAMTSVAD 356
Cdd:cd13657 229 IGGIKAAGIDLGVAPLPTVDGTNPpRPYSGVEGIYVTkyAERKNKEAALDFA-KFFTTAEASKILADENGYVPAATNAYD 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 336105116 357 --EVASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDA 407
Cdd:cd13657 308 daEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEA 360
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
48-407 |
3.76e-52 |
|
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: 178.56 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 48 GSLTIWV--DENRKPAVQAAVDIYNETNPDVKVElvqkNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD 125
Cdd:cd13656 1 GKLVIWIngDKGYNGLAEVGKKFEKDTGIKVTVE----HPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 126 LGAK-AGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAALVDSTPETWDEMIAAGKEAGTKYPFVINTNgtTGDAYTYY 204
Cdd:cd13656 77 PDKAfQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFN--LQEPYFTW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 205 GLQTSFGAPVFVQNEDGSYTSELGMGGDEGFAFADFLAEngMKGEGHFSTDWTYDVANQEFSDGNAPYTIAGPWAIQTFK 284
Cdd:cd13656 155 PLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVD--LIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 285 DAGIDVAVDPIPSAGGETAAPFVGVQGFYLSAQSESKLIANDFLVNYVATPEVIKALYDADPR-LPAMTSVADEVASDPI 363
Cdd:cd13656 233 TSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLgAVALKSYEEELAKDPR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 336105116 364 VAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDA 407
Cdd:cd13656 313 IAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEA 356
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
50-411 |
1.89e-51 |
|
The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270240 [Multi-domain] Cd Length: 368 Bit Score: 176.83 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 50 LTIWV--DENRKPAVQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD-L 126
Cdd:cd13522 2 ITVWHqyDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDeY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 127 GAKAGEFEAVATQAFTYDGQMYGLPYALETIAVV-RNAALVDSTPETWDEMIAAGKEAGTK--YPFVINTNgttgDAYTY 203
Cdd:cd13522 82 VSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYyNKKLVPKNPPKTWQELIALAQGLKAKnvWGLVYNQN----EPYFF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 204 YGLQTSFGAPVFVQNeDGSYTSELG-MGGDEGFAFADFLAENgmkgEGHFSTDWTYDVANQEFSDGNAPYTIAGPWAIQT 282
Cdd:cd13522 158 AAWIGGFGGQVFKAN-NGKNNPTLDtPGAVEALQFLVDLKSK----YKIMPPETDYSIADALFKAGKAAMIINGPWDLGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 283 -FKDAGIDVAVDPIPS-AGGETAAPFVGVQGFYLSAQSESKLIANDFlVNYVATPEVIKALYDADPRLPAMTSVADE--V 358
Cdd:cd13522 233 yRQALKINLGVAPLPTfSGTKHAAPFVGGKGFGINKESQNKAAAVEF-VKYLTSYQAQLVLFDDAGDIPANLQAYESpaV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 336105116 359 ASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDAWTKM 411
Cdd:cd13522 312 QNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDA 364
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
39-419 |
5.50e-51 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 176.36 E-value: 5.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 39 TSAAPAGATGSLTIWV--DENRKPAVQAAVDIYNETNPDVKVElvqkNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFI 116
Cdd:PRK09474 22 ASALAKIEEGKLVIWIngDKGYNGLAEVGKKFEKDTGIKVTVE----HPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 117 VNGVAEPVDLGAK-AGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAALVDSTPETWDEMIAAGKE--AGTKYPFVINT 193
Cdd:PRK09474 98 QSGLLAEVTPSKAfKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKElkAKGKSAIMWNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 194 NGTtgdaYTYYGLQTSFGAPVFVQNEDGSYTSELGMGGDEGFAFADFLAEngMKGEGHFSTDWTYDVANQEFSDGNAPYT 273
Cdd:PRK09474 178 QEP----YFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVD--LVKNKHMNADTDYSIAEAAFNKGETAMT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 274 IAGPWAIQTFKDAGIDVAVDPIPSAGGETAAPFVGVQGFYLSAQSESKLIANDFLVNYVATPEVIKALYDADPR-LPAMT 352
Cdd:PRK09474 252 INGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLgAVALK 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336105116 353 SVADEVASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDAwtkmLADLESAI 419
Cdd:PRK09474 332 SFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAA----LDDAAKRI 394
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-341 |
3.54e-47 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 165.60 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 1 MRKTLfrAATVVAAMSLLAACGGGDEAPAETQEPTTaetsaapagatgsLTIW-VDENRKPAVQAAVDIYNETNPDVKVE 79
Cdd:COG1653 1 MRRLA--LALAAALALALAACGGGGSGAAAAAGKVT-------------LTVWhTGGGEAAALEALIKEFEAEHPGIKVE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 80 LVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD-----LGAKAGEFEAVATQAFTYDGQMYGLPYAL 154
Cdd:COG1653 66 VESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDdllddDGLDKDDFLPGALDAGTYDGKLYGVPFNT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 155 ETIAVVRNAALVD----STPETWDEMIAAGK---EAGTKYPFVINTNGTTgdayTYYGLQTSFGAPVFVQNEDGSYTSEL 227
Cdd:COG1653 146 DTLGLYYNKDLFEkaglDPPKTWDELLAAAKklkAKDGVYGFALGGKDGA----AWLDLLLSAGGDLYDEDGKPAFDSPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 228 GMggdEGFAFADFLAENGMKGEGHFSTDWTYdvANQEFSDGNAPYTIAGPWAIQTFKDA--GIDVAVDPIPS-AGGETAA 304
Cdd:COG1653 222 AV---EALEFLKDLVKDGYVPPGALGTDWDD--ARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGgPGGKKPA 296
|
330 340 350
....*....|....*....|....*....|....*..
gi 336105116 305 PFVGVQGFYLSAQSESKLIANDFLvNYVATPEVIKAL 341
Cdd:COG1653 297 SVLGGSGLAIPKGSKNPEAAWKFL-KFLTSPEAQAKW 332
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
50-398 |
7.08e-38 |
|
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: 141.00 E-value: 7.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 50 LTIWV--DENRKPAVQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVDL- 126
Cdd:cd13585 2 LTFWDwgQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 127 ---GAKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRN------AALVDSTPETWDEMIAAGKE----AGTKYPFVInt 193
Cdd:cd13585 82 iekDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNkdlfdkAGPGPKPPWTWDELLEAAKKltdkKGGQYGFAL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 194 NGTTGDAYTYYGLQTSFGAPVFvqNEDGS---YTSElgmGGDEGFAF-ADFLAENGMKGeghfSTDWTYDVANQEFSDGN 269
Cdd:cd13585 160 RGGSGGQTQWYPFLWSNGGDLL--DEDDGkatLNSP---EAVEALQFyVDLYKDGVAPS----SATTGGDEAVDLFASGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 270 APYTIAGPWAIQTFKDAGIDVAVD--PIPSAGGETAAPFVGVQGFYLSAQSESKLIANDFLvNYVATPEVIKALYDADPR 347
Cdd:cd13585 231 VAMMIDGPWALGTLKDSKVKFKWGvaPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFI-KFLTSKENQLKLGGAAGP 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 336105116 348 LPAMTSVADEVASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASII 398
Cdd:cd13585 310 AALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEAL 360
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
49-417 |
1.41e-36 |
|
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: 137.51 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 49 SLTIW---VDENRKPAVQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGPDIT-IGAHDWLGSFIVNGVAEP- 123
Cdd:cd14749 1 TITYWqyfTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 124 ---VDLGAKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRN-----AALVDSTPETWDEMIAAGKE----AGTKYPFVI 191
Cdd:cd14749 81 tdyLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNkdlfeEAGGVKPPKTWDELIEAAKKdkfkAKGQTGFGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 192 NTNGTTGDAYTYYGLQTSFGAPVFVQNEDG-SYTSELGMggdEGFAFADFLAENGMKGEGHFSTDwtYDVANQEFSDGNA 270
Cdd:cd14749 161 LLGAQGGHWYFQYLVRQAGGGPLSDDGSGKaTFNDPAFV---QALQKLQDLVKAGAFQEGFEGID--YDDAGQAFAQGKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 271 PYTIAGPWAIQTFKD--AGIDVAVDPIPS--AGGETAAPFVGVQGFYLSAQSESKLIANDFLvNYVATPEVIKAlYDADP 346
Cdd:cd14749 236 AMNIGGSWDLGAIKAgePGGKIGVFPFPTvgKGAQTSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQ-YLEDV 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336105116 347 RLPAMT---SVADEVASDPIVAGFLSASKNGAPMPSI-PEMGNVWEHWNAAEASIISGSAKPKDAWTKMLADLES 417
Cdd:cd14749 314 GLLPAKevvAKDEDPDPVAILGPFADVLNAAGSTPFLdEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK 388
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
50-419 |
5.11e-36 |
|
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: 135.88 E-value: 5.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 50 LTIW--VDENRKPAVQAAVDIYNETNPDVKVELV-QKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD- 125
Cdd:cd14748 2 ITFWhgMSGPDGKALEELVDEFNKSHPDIKVKAVyQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 126 ----LGAKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAAL-------VDSTPETWDEMIAAGK------EAGTKYP 188
Cdd:cd14748 82 yidkDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLfeeagldPEKPPKTWDELEEAAKklkdkgGKTGRYG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 189 FVINTNGTTGdayTYYGLQTSFGAPVFvqNEDGsytSELGMGGDEGFAFADFLAenGMKGEGHFSTDWTYDVANQEFSDG 268
Cdd:cd14748 162 FALPPGDGGW---TFQALLWQNGGDLL--DEDG---GKVTFNSPEGVEALEFLV--DLVGKDGVSPLNDWGDAQDAFISG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 269 NAPYTIAGPWAIQTFKD--AGIDVAVDPIPSAGGETAAPFVGVQGFYLSAQ-SESKLIANDFlVNYVATPEVIKALYDAD 345
Cdd:cd14748 232 KVAMTINGTWSLAGIRDkgAGFEYGVAPLPAGKGKKGATPAGGASLVIPKGsSKKKEAAWEF-IKFLTSPENQAKWAKAT 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336105116 346 PRLPAMTSVADE----VASDPIVAGFLSASKNGAP-MPSIPEMGNVWEHWNAAEASIISGSAKPKDAwtkmLADLESAI 419
Cdd:cd14748 311 GYLPVRKSAAEDpeefLAENPNYKVAVDQLDYAKPwGPPVPNGAEIRDELNEALEAALLGKKTPEEA----LKEAQEKI 385
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
64-364 |
9.80e-32 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 122.13 E-value: 9.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 64 AAVDIYNETNpDVKVELVQKNFEDIRADFLAQVPTGEGPDITI--GAHDWLGSFIVNGVAEPVDLGAKAGEFEAVATqAF 141
Cdd:pfam13416 1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVvwIAADQLATLAEAGLLADLSDVDNLDDLPDALD-AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 142 TYDGQMYGLPYALET-IAVVRNAALVD---STPETWDEMIAAGKEAGTKYpfvintnGTTGDAYTYYglqtsfgapVFVQ 217
Cdd:pfam13416 79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGKT-------GLTDPATGWL---------LWAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 218 NEDGSYTSELGMGGDEGFAFADFLAEngMKGEGHFStdWTYDVANQEFSDGNAPYTIAGPWAIQTFKDAGIDVAVDPIPS 297
Cdd:pfam13416 143 LADGVDLTDDGKGVEALDEALAYLKK--LKDNGKVY--NTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKD 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 298 aggetaAPFVGVQGFYLSAQS-ESKLIANDFLvNYVATPEVIKALYDADPRLPAMTSVA--DEVASDPIV 364
Cdd:pfam13416 219 ------GSFLGGKGLVVPAGAkDPRLAALDFI-KFLTSPENQAALAEDTGYIPANKSAAlsDEVKADPAL 281
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
49-414 |
3.49e-30 |
|
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: 120.11 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 49 SLTIWVDENRKPA--VQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD- 125
Cdd:cd14747 1 TLTVWAMGNSAEAelLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 126 -LGAKAGEFEAV--ATQAFTYDGQMYGLPYALETIAVVRN-----AALVDSTPETWDEMIAAGK----EAGTKYPFVINT 193
Cdd:cd14747 81 yLEDLGGDKDLFpgLVDTGTVDGKYYGVPWYADTRALFYRtdllkKAGGDEAPKTWDELEAAAKkikaDGPDVSGFAIPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 194 NGTTgdaytyyglqTSFGAPvFVQNEDGSYTSE-------LGMGGDEGFAFADFLAENGMKGEghfSTDWTYDVANQEFS 266
Cdd:cd14747 161 KNDV----------WHNALP-FVWGAGGDLATKdkwkatlDSPEAVAGLEFYTSLYQKGLSPK---STLENSADVEQAFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 267 DGNAPYTIAGPWAIQTFKDAGID----VAVDPIPSAGGETAAPFVGVQGFYLSAQSESKLIANDFlVNYVATPEVIKALY 342
Cdd:cd14747 227 NGKVAMIISGPWEIGAIREAGPDlagkWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKF-IEFLSSPENQAAYA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336105116 343 DADPRLPAMTSVADEV--ASDPIVAGFLSASKNGAPMPSIPEmgnvwehWNAAEASIISGSAKPKDAWTKMLAD 414
Cdd:cd14747 306 KATGMLPANTSAWDDPslANDPLLAVFAEQLKTGKATPATPE-------WGEIEAELVLVLEEVWIGVGADVED 372
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
55-419 |
4.42e-25 |
|
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: 105.84 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 55 DENRKPAVQAAVDIYNETNPDVKVELVQ-KNFEDIRADFLAQVPTGEGPDITIGAHD--WLGSFIVNGVAEPVDLGAKAG 131
Cdd:cd14750 9 DGQEGELLKKAIAAFEKKHPDIKVEIEElPASSDDQRQQLVTALAAGSSAPDVLGLDviWIPEFAEAGWLLPLTEYLKEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 132 E---FEAVATQAFTYDGQMYGLPYALETIAVVRNAALVD----STPETWDEMIAAGKEAGTK----YPFVIN---TNGTT 197
Cdd:cd14750 89 EdddFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGepgiWGYVFQgkqYEGLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 198 GDAYTYYglqTSFGAPVFvqNEDGSYTSELGMGGDEGFAFADFLAENGMKGEGhfSTDWTYDVANQEFSDGNAPYTIAGP 277
Cdd:cd14750 169 CNFLELL---WSNGGDIF--DDDSGKVTVDSPEALEALQFLRDLIGEGISPKG--VLTYGEEEARAAFQAGKAAFMRNWP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 278 WAIQTFKDAGI----DVAVDPIPSAGGETAAPFVGVQGFYLSAQSESKLIANDFlVNYVATPEVIKALYDADPRLPAMTS 353
Cdd:cd14750 242 YAYALLQGPESavagKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEF-VKFLTSPEVQKRRAINGGLPPTRRA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336105116 354 VADE---VASDPIVAGFLSASKNGAPMPSIPEMGNV----WEHWNAAeasiISGSAKPKDAwtkmLADLESAI 419
Cdd:cd14750 321 LYDDpevLEAYPFLPALLEALENAVPRPVTPKYPEVstaiQIALSAA----LSGQATPEEA----LKQAQEKL 385
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
55-337 |
1.22e-20 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 91.32 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 55 DENRKPAVQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGP-DITIGAHDWLGSFIVNGVAEPVDlgakagef 133
Cdd:pfam01547 3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLD-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 134 EAVATQAFTYDGQMYGLPYALETIAVVRNAALVD----STPETWDEMIAAGKEAGTKYPFVINTNGTTG---DAYTYYGL 206
Cdd:pfam01547 75 DYVANYLVLGVPKLYGVPLAAETLGLIYNKDLFKkaglDPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtLGYFTLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 207 QTSFGAPVFVQNEDGsYTSELGMGGDEGFAFADFLAENGMKGEGHFSTDWTYDVANQEFSDGNAPYTIAGPWAIQTFKDA 286
Cdd:pfam01547 155 LASLGGPLFDKDGGG-LDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 287 GIDVA-VDPIPSAGGETAAPFV--------GVQGFYLSAQSESKLIANDFlVNYVATPEV 337
Cdd:pfam01547 234 KLKVAfAAPAPDPKGDVGYAPLpagkggkgGGYGLAIPKGSKNKEAAKKF-LDFLTSPEA 292
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
49-407 |
3.05e-20 |
|
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: 91.67 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 49 SLTIW--VDENRKPAVQAAVDIYNETNPDVKVELVQKNFEDIRADFLAQVPTGEGPDITIGAHDWLGSFIVNGVAEPVD- 125
Cdd:cd14751 1 TITFWhtSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 126 --LGAKAGEFEAVATQAFTYDGQMYGLPYALETIAVVRNAALVD----STPETWDEMIAAGKEAGTK---YPFVINTNGT 196
Cdd:cd14751 81 tpAFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEeagtEVPKTMDELVAAAKAIKKKkgrYGLYISGDGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 197 TGDAYTYYGLQtsfGAPVFVQNEDGSYTSELGMGGDEgfAFADFLAEngmKGEGHFSTDWtYDVANQEFSDGNAPYTIAG 276
Cdd:cd14751 161 YWLLPFLWSFG---GDLTDEKKATGYLNSPESVRALE--TIVDLYDE---GAITPCASGG-YPNMQDGFKSGRYAMIVNG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 277 PWAI------QTFKDAGiDVAVDPIPSAGGETAAPfVGVQGFYLSAQSESKLIANDFlVNYVATPEVIKALYDADPRLPA 350
Cdd:cd14751 232 PWAYadilggKEFKDPD-NLGIAPVPAGPGGSGSP-VGGEDLVIFKGSKNKDAAWKF-VKFMSSAEAQALTAAKLGLLPT 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 336105116 351 MTSVAD--EVASDPIVAGFLSASKNGAPMPSIPEMGNVWEHWNAAEASIISGSAKPKDA 407
Cdd:cd14751 309 RTSAYEspEVANNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREA 367
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
49-411 |
9.29e-20 |
|
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270373 [Multi-domain] Cd Length: 363 Bit Score: 90.10 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 49 SLTIWVDENRKPAVQAAVDIYNETNPDVKVEL-VQKNFEDIRADFLAQVPTgEGPDITIGAHDWLGSFIVNGVAEPVDLG 127
Cdd:cd13655 1 TLTVWGPQEDQEWLKEMVDAFKEKHPEWKITItIGVVGEADAKDEVLKDPS-AAADVFAFANDQLGELVDAGAIYPLTGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 128 A----KAGEFEAVATqAFTYDGQMYGLPYALETIAVVRN-AALVDSTPETWDEMIAAGKEAGTKYPFVINtngttgDAYT 202
Cdd:cd13655 80 AvdkiKNTNSEATVD-AVTYNGKLYGYPFTANTWFMYYDkSKLTEDDVKSLDTMLAKAPDAKGKVSFDLS------NSWY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 203 YYGLQTSFGAPVFVqnEDGSYTSELGMGGDEGFAFADFLAENGMKGEGHFSTDwtyDVANQEFSDGNAPYTIAGPWAIQT 282
Cdd:cd13655 153 LYAFFFGAGCKLFG--NNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDAD---GDAISGLKDGTLGAGVSGPWDAAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 283 FKDA-GIDVAVDPIPSA--GGETA--APFVGVQGFYLSAQSESKLIANDfLVNYVATPEVIKALYDADPRLPAMTSVA-- 355
Cdd:cd13655 228 LKKAlGDNYAVAKLPTYtlGGKDVqmKSFAGYKAIGVNSNTKNPEAAMA-LADYLTNEESQLTRFEKRGIGPTNKEAAes 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 336105116 356 DEVASDPIVAGFLSASKNGA-PMPSIPEMGNVWEHWNAAEASIISGSAKPKDAWTKM 411
Cdd:cd13655 307 DAVKADPAAKALIAQSNEASvVQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQKL 363
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
53-337 |
1.25e-09 |
|
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: 59.78 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 53 WVDENRKPAVQaavDIYNETNpdVKVELVQKNFEDIRADFLAQVPTGEGPDItIGAHDWLGSFIV---NGVAEPVD---- 125
Cdd:cd13521 14 WVDDENWPVAK---EIEKLTN--VKLEIVAVTAATSQQKLNLMLASGDLPDI-VGADYLKDKFIAygmEGAFLPLSkyid 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 126 ----LGAKAGEFEAVATQAFTYDGQMYGLPY----ALETIAVVRNAALVDS----TPETWDEMIAAGKEAGTKYPfviNT 193
Cdd:cd13521 88 qypnLKAFFKQHPDVLRASTASDGKIYLIPYeppkDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKDP---NG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 194 NG--------TTGDAYTYYGLQTSFGAPVFVQNEDGSYTSELGmggdegfAFADFLAE----------NGMKGEGHFSTD 255
Cdd:cd13521 165 NGkadeipfiDRDPLYGAFRLINSWGARSAGGSTDSDWYEDNG-------KFKHPFASeeykdgmkymNKLYTEGLIDKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 256 W---TYDVANQEFSDGNAPYTIAGPWAIQTFKDAGIDVAVD-----PIPSAGG------ETAAPFVGVQGFYLSAQSESK 321
Cdd:cd13521 238 SftqKDDQAEQKFSNGKLGGFTHNWFASDNLFTAQLGKEKPmyillPIAPAGNvkgrreEDSPGYTGPDGVAISKKAKNP 317
|
330
....*....|....*.
gi 336105116 322 LIANDFLvNYVATPEV 337
Cdd:cd13521 318 VAALKFF-DWLASEEG 332
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
66-339 |
1.16e-03 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 41.16 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 66 VDIYNE-TNPDVKVELV-QKNFEDiraDFLAQVPTGEGPDI-TIGAHDWLGSFIVNGVAEPVD--LGAKAGEF----EAV 136
Cdd:cd13580 25 TKYLEEkTNIDVKVKWVpDSSYDE---KLNLALASGDLPDIvVVNDPQLSITLVKQGALWDLTdyLDKYYPNLkkiiEQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 137 ATQAFTYDGQMYGLP----YALETIAVVR-----NAALvdSTPETWDEMIAAGKEAGTKYPfviNTNG---TTGDAYT-- 202
Cdd:cd13580 102 GWDSASVDGKIYGIPrkrpLIGRNGLWIRkdwldKLGL--EVPKTLDELYEVAKAFTEKDP---DGNGkkdTYGLTDTkd 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336105116 203 -----YYGLQTSFGAPV--FVQNEDGSYTselgmGGDEGFAFADFLAE-NGMKGEGHFSTDW---TYDVANQEFSDGNAP 271
Cdd:cd13580 177 ligsgFTGLFGAFGAPPnnWWKDEDGKLV-----PGSIQPEMKEALKFlKKLYKEGLIDPEFavnDGTKANEKFISGKAG 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336105116 272 YTIAGPWAIQTFKDAGID-------VAVDPIPSAGGE-TAAPFVGVQGFYL-SAQSEsKLIANDFLVNYVATPEVIK 339
Cdd:cd13580 252 IFVGNWWDPAWPQASLKKndpdaewVAVPIPSGPDGKyGVWAESGVNGFFViPKKSK-KPEAILKLLDFLSDPEVQK 327
|
|
| |
