|
Name |
Accession |
Description |
Interval |
E-value |
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
1-316 |
1.70e-34 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 128.68 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 1 TDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTI---FQVNGPVGYQNWKGYTADLKDTGIYNELNNKDIALKDGDKVVG 77
Cdd:pfam13416 7 EKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGYDGKLYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 78 IPYVMET-YGIIYNKDLLKKytelpgakikDVKEIDSFDKLKEVADDmqakkdqlgIKGAFTSAgfDSSSDWRFKTHLAn 156
Cdd:pfam13416 87 VPYAASTpTVLYYNKDLLKK----------AGEDPKTWDELLAAAAK---------LKGKTGLT--DPATGWLLWALLA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 157 iplsyefkeDGVTTQPETIKGTYLPNFKNIFDLYLKDSTTApsqlssKTGDDANSEFALGEAAFYQNGTWAWTDLQKAGm 236
Cdd:pfam13416 145 ---------DGVDLTDDGKGVEALDEALAYLKKLKDNGKVY------NTGADAVQLFANGEVAMTVNGTWAAAAAKKAG- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 237 kpDQVGMLPIyigakgeeNQGLATGSENyLCINAKASEADQkASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF---DKV 313
Cdd:pfam13416 209 --KKLGAVVP--------KDGSFLGGKG-LVVPAGAKDPRL-AALDFIKF-LTSPENQAALAEDTGYIPANKSAalsDEV 275
|
...
gi 2060599188 314 KSD 316
Cdd:pfam13416 276 KAD 278
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
4-299 |
5.14e-33 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 126.70 E-value: 5.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 4 TGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPvGYQNW--KGYTADLKDTGIYNELNNKDI------ALKDGDKV 75
Cdd:COG1653 60 PGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSG-WLAEFaaAGALVPLDDLLDDDGLDKDDFlpgaldAGTYDGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 76 VGIPYVMETYGIIYNKDLLKKYtelpgakikDVKEIDSFDKLKEVADDMQAKKDQLGIkgaftsaGFDSSSDWRFKTHLA 155
Cdd:COG1653 139 YGVPFNTDTLGLYYNKDLFEKA---------GLDPPKTWDELLAAAKKLKAKDGVYGF-------ALGGKDGAAWLDLLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 156 NIPLSYeFKEDG--VTTQPETIKGtylpnFKNIFDLYlkDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQK 233
Cdd:COG1653 203 SAGGDL-YDEDGkpAFDSPEAVEA-----LEFLKDLV--KDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKD 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2060599188 234 AGMKPDqVGMLPIYIGAKGEENQGLATGSenYLCINAKASeaDQKASKDFLNWvVTSDEGIKALSE 299
Cdd:COG1653 275 AAPDFD-VGVAPLPGGPGGKKPASVLGGS--GLAIPKGSK--NPEAAWKFLKF-LTSPEAQAKWDA 334
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
4-360 |
1.21e-19 |
|
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: 89.39 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 4 TGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPvGYQNW--KGYTADL-----KDTGIYNELNNKDIALKDGDKVV 76
Cdd:cd13585 28 PGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGP-WVPEFasNGALLDLddyieKDGLDDDFPPGLLDAGTYDGKLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 77 GIPYVMETYGIIYNKDLLKKYTELPgakikdvKEIDSFDKLKEVaddmqAKKDQLGIKGAFtsaGFDSSSDWRFKTHLAN 156
Cdd:cd13585 107 GLPFDADTLVLFYNKDLFDKAGPGP-------KPPWTWDELLEA-----AKKLTDKKGGQY---GFALRGGSGGQTQWYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 157 IPLSY---EFKEDGVT---TQPETIKGtylpnFKNIFDLYlkDSTTAPSQLSSkTGDDANSEFALGEAAFYQNGTWAWTD 230
Cdd:cd13585 172 FLWSNggdLLDEDDGKatlNSPEAVEA-----LQFYVDLY--KDGVAPSSATT-GGDEAVDLFASGKVAMMIDGPWALGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 231 LqKAGMKPDQVGMLPIYIGAKGEENQGLATGSenyLCINAKAseADQKASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF 310
Cdd:cd13585 244 L-KDSKVKFKWGVAPLPAGPGGKRASVLGGWG---LAISKNS--KHPEAAWKFIKF-LTSKENQLKLGGAAGPAALAAAA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2060599188 311 DKVKSDNPLVEEAVEDSNSGKEQVAWNFTMMPSEEWKNQLGQAMLAYAQG 360
Cdd:cd13585 317 ASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLG 366
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
68-300 |
1.13e-05 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 46.93 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 68 ALKDGDKVVGIPYVMETYGIIYNKDLLKKytelPGAKIKDVKEIDsfDKLKEvaddmQAKKDQL-GIKGA-FTSAGFDSS 145
Cdd:PRK09474 122 AVRYNGKLIGYPIAVEALSLIYNKDLVPT----PPKTWEEIPALD--KELKA-----KGKSAIMwNLQEPyFTWPLIAAD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 146 SDWRFKTHLANiplsYEFKEDGVTTqPETIKGTylpNFknIFDLYLKDSTTAPSQLSSktgddANSEFALGEAAFYQNGT 225
Cdd:PRK09474 191 GGYAFKFENGG----YDVKDVGVNN-AGAKAGL---QF--LVDLVKNKHMNADTDYSI-----AEAAFNKGETAMTINGP 255
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2060599188 226 WAWTDLQKAGMkPDQVGMLPIYIGAKGEENQGLATGSenylcINAkASeADQKASKDFL-NWVVTsDEGIKALSED 300
Cdd:PRK09474 256 WAWSNIDKSGI-NYGVTVLPTFNGKPSKPFVGVLSAG-----INA-AS-PNKELAKEFLeNYLLT-DEGLETVNKD 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
1-316 |
1.70e-34 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 128.68 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 1 TDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTI---FQVNGPVGYQNWKGYTADLKDTGIYNELNNKDIALKDGDKVVG 77
Cdd:pfam13416 7 EKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGYDGKLYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 78 IPYVMET-YGIIYNKDLLKKytelpgakikDVKEIDSFDKLKEVADDmqakkdqlgIKGAFTSAgfDSSSDWRFKTHLAn 156
Cdd:pfam13416 87 VPYAASTpTVLYYNKDLLKK----------AGEDPKTWDELLAAAAK---------LKGKTGLT--DPATGWLLWALLA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 157 iplsyefkeDGVTTQPETIKGTYLPNFKNIFDLYLKDSTTApsqlssKTGDDANSEFALGEAAFYQNGTWAWTDLQKAGm 236
Cdd:pfam13416 145 ---------DGVDLTDDGKGVEALDEALAYLKKLKDNGKVY------NTGADAVQLFANGEVAMTVNGTWAAAAAKKAG- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 237 kpDQVGMLPIyigakgeeNQGLATGSENyLCINAKASEADQkASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF---DKV 313
Cdd:pfam13416 209 --KKLGAVVP--------KDGSFLGGKG-LVVPAGAKDPRL-AALDFIKF-LTSPENQAALAEDTGYIPANKSAalsDEV 275
|
...
gi 2060599188 314 KSD 316
Cdd:pfam13416 276 KAD 278
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
4-299 |
5.14e-33 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 126.70 E-value: 5.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 4 TGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPvGYQNW--KGYTADLKDTGIYNELNNKDI------ALKDGDKV 75
Cdd:COG1653 60 PGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSG-WLAEFaaAGALVPLDDLLDDDGLDKDDFlpgaldAGTYDGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 76 VGIPYVMETYGIIYNKDLLKKYtelpgakikDVKEIDSFDKLKEVADDMQAKKDQLGIkgaftsaGFDSSSDWRFKTHLA 155
Cdd:COG1653 139 YGVPFNTDTLGLYYNKDLFEKA---------GLDPPKTWDELLAAAKKLKAKDGVYGF-------ALGGKDGAAWLDLLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 156 NIPLSYeFKEDG--VTTQPETIKGtylpnFKNIFDLYlkDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQK 233
Cdd:COG1653 203 SAGGDL-YDEDGkpAFDSPEAVEA-----LEFLKDLV--KDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKD 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2060599188 234 AGMKPDqVGMLPIYIGAKGEENQGLATGSenYLCINAKASeaDQKASKDFLNWvVTSDEGIKALSE 299
Cdd:COG1653 275 AAPDFD-VGVAPLPGGPGGKKPASVLGGS--GLAIPKGSK--NPEAAWKFLKF-LTSPEAQAKWDA 334
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-376 |
2.30e-20 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 91.93 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 1 TDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQV----------NG-----PVGYQNWKGYTADLKDTGIYNelnnk 65
Cdd:COG2182 61 EEEPGIKVKVVEVPWDDLREKLTTAAPAGKGPDVFVGahdwlgelaeAGllaplDDDLADKDDFLPAALDAVTYD----- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 66 dialkdgDKVVGIPYVMETYGIIYNKDLLKKytELPgakikdvkeiDSFDKLKEVADDMQAKKDQ---LGIKGAFTSAGF 142
Cdd:COG2182 136 -------GKLYGVPYAVETLALYYNKDLVKA--EPP----------KTWDELIAAAKKLTAAGKYglaYDAGDAYYFYPF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 143 DSSSDWrfkthlaniplsYEFKEDGVTTQ------PETIKGTYlpnfknifdlYLKDSTTAPSQLSSKTGDDANSEFALG 216
Cdd:COG2182 197 LAAFGG------------YLFGKDGDDPKdvglnsPGAVAALE----------YLKDLIKDGVLPADADYDAADALFAEG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 217 EAAFYQNGTWAWTDLQKAgmKPDQVGMLPIYIGAKGEENQGLAtGSENYlCINAKAseADQKASKDFLNWvVTSDEGIKA 296
Cdd:COG2182 255 KAAMIINGPWAAADLKKA--LGIDYGVAPLPTLAGGKPAKPFV-GVKGF-GVSAYS--KNKEAAQEFAEY-LTSPEAQKA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 297 LSEDMGFTTPFKTF--DKVKSDNPLVE---EAVEDSnsgkeqvawnfTMMPSE-EWK---NQLGQAMLAYAQGNGS---- 363
Cdd:COG2182 328 LFEATGRIPANKAAaeDAEVKADPLIAafaEQAEYA-----------VPMPNIpEMGavwTPLGTALQAIASGKADpaea 396
|
410
....*....|...
gi 2060599188 364 WDDVQKAFVDNWK 376
Cdd:COG2182 397 LDAAQKQIEAAIA 409
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
4-360 |
1.21e-19 |
|
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: 89.39 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 4 TGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPvGYQNW--KGYTADL-----KDTGIYNELNNKDIALKDGDKVV 76
Cdd:cd13585 28 PGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGP-WVPEFasNGALLDLddyieKDGLDDDFPPGLLDAGTYDGKLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 77 GIPYVMETYGIIYNKDLLKKYTELPgakikdvKEIDSFDKLKEVaddmqAKKDQLGIKGAFtsaGFDSSSDWRFKTHLAN 156
Cdd:cd13585 107 GLPFDADTLVLFYNKDLFDKAGPGP-------KPPWTWDELLEA-----AKKLTDKKGGQY---GFALRGGSGGQTQWYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 157 IPLSY---EFKEDGVT---TQPETIKGtylpnFKNIFDLYlkDSTTAPSQLSSkTGDDANSEFALGEAAFYQNGTWAWTD 230
Cdd:cd13585 172 FLWSNggdLLDEDDGKatlNSPEAVEA-----LQFYVDLY--KDGVAPSSATT-GGDEAVDLFASGKVAMMIDGPWALGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 231 LqKAGMKPDQVGMLPIYIGAKGEENQGLATGSenyLCINAKAseADQKASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF 310
Cdd:cd13585 244 L-KDSKVKFKWGVAPLPAGPGGKRASVLGGWG---LAISKNS--KHPEAAWKFIKF-LTSKENQLKLGGAAGPAALAAAA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2060599188 311 DKVKSDNPLVEEAVEDSNSGKEQVAWNFTMMPSEEWKNQLGQAMLAYAQG 360
Cdd:cd13585 317 ASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLG 366
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
5-371 |
1.41e-15 |
|
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: 77.42 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 5 GVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPVGYQNW--KGYTADLKDTGIYNELNNK------DIALKDGdKVV 76
Cdd:cd14749 30 NIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFvkAGLLLPLTDYLDPNGVDKRflpglaDAVTFNG-KVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 77 GIPYVMETYGIIYNKDLLKKytelpgAKIKDVKEidSFDKLKEVaddmqAKKDQLGIKGA--FTSAGFDSSSDWRFKThl 154
Cdd:cd14749 109 GIPFAARALALFYNKDLFEE------AGGVKPPK--TWDELIEA-----AKKDKFKAKGQtgFGLLLGAQGGHWYFQY-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 155 ANIPLSYEFKEDgVTTQPETIkgTYLPN---FKNIFDLYLKDSTTAPsqLSSKTGDDANSEFALGEAAFYQNGTWAWTDL 231
Cdd:cd14749 174 LVRQAGGGPLSD-DGSGKATF--NDPAFvqaLQKLQDLVKAGAFQEG--FEGIDYDDAGQAFAQGKAAMNIGGSWDLGAI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 232 qKAGMKPDQVGMLPIYIGAKGeeNQGLATGSeNYLCINAKASEADQKASKDFLNWvVTSDEGIKALSEDMGFTTpfKTFD 311
Cdd:cd14749 249 -KAGEPGGKIGVFPFPTVGKG--AQTSTIGG-SDWAIAISANGKKKEAAVKFLKY-LTSPEVMKQYLEDVGLLP--AKEV 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2060599188 312 KVK----SDNPLVEEAVEDSNSGKEQVAWNFTMMP-SEEWKNQLGQAMLAYAQGNGSWDDVQKAF 371
Cdd:cd14749 322 VAKdedpDPVAILGPFADVLNAAGSTPFLDEYWPAaAQVHKDAVQKLLTGKIDPEQVVKQAQSAA 386
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
5-370 |
9.21e-15 |
|
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: 75.02 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 5 GVQVKVQTAASGTYEQT-LKSELAKSDAPTIFQVngpvgYQNWkgyTADLKDTGIY---------NELNNKDI------A 68
Cdd:cd14748 29 DIKVKAVYQGSYDDTLTkLLAALAAGTAPDVAQV-----DASW---VAQLADSGALeplddyidkDGVDDDDFypaaldA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 69 LKDGDKVVGIPYVMETYGIIYNKDLLKKytelpgAKIKDVKEIDSFDKLKEVADDMQAKKDQLGIKGAFTSAGFDsssDW 148
Cdd:cd14748 101 GTYDGKLYGLPFDTSTPVLYYNKDLFEE------AGLDPEKPPKTWDELEEAAKKLKDKGGKTGRYGFALPPGDG---GW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 149 RFKTHLANIPLSYeFKEDGVTTQPETikgtylPNFKNIFDlYLKDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAW 228
Cdd:cd14748 172 TFQALLWQNGGDL-LDEDGGKVTFNS------PEGVEALE-FLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 229 TDLQKAGMKPD-QVGMLPiyigAKGEENQGLATGSeNYLCINAKASEaDQKASKDFLNWvVTSDEGIKALSEDMGFTTPF 307
Cdd:cd14748 244 AGIRDKGAGFEyGVAPLP----AGKGKKGATPAGG-ASLVIPKGSSK-KKEAAWEFIKF-LTSPENQAKWAKATGYLPVR 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2060599188 308 K----TFDKVKSDNPLVEEAVEDSNSGKeqvAWNFTMMPSEEWKNQLGQAMLAYAQGNgswDDVQKA 370
Cdd:cd14748 317 KsaaeDPEEFLAENPNYKVAVDQLDYAK---PWGPPVPNGAEIRDELNEALEAALLGK---KTPEEA 377
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
2-293 |
2.17e-14 |
|
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: 72.83 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 2 DKTGVQVKVQTAASGTYEQTLKSELAKSDAPT-IFQVNGpvgyqnwkGYTADLKDTGIYNELNN--KDIALKDGDKVVGI 78
Cdd:pfam01547 20 EHPGIKVEVESVGSGSLAQKLTTAIAAGDGPAdVFASDN--------DWIAELAKAGLLLPLDDyvANYLVLGVPKLYGV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 79 PYVMETYGIIYNKDLLKKYtelpgakikDVKEIDSFDKLKEVADDMQAKkdqlGIKGAFTSAGFDSSSDWRFKTHLANIP 158
Cdd:pfam01547 92 PLAAETLGLIYNKDLFKKA---------GLDPPKTWDELLEAAKKLKEK----GKSPGGAGGGDASGTLGYFTLALLASL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 159 LSYEFKEDGVTTQPETIKGTyLPNFKNIFDLYLKDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQKAGMKP 238
Cdd:pfam01547 159 GGPLFDKDGGGLDNPEAVDA-ITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2060599188 239 DQV---GMLPIYIGAKGEENQGLATGSENYLCINAKAseADQKASKDFLNWvVTSDEG 293
Cdd:pfam01547 238 AFAapaPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGS--KNKEAAKKFLDF-LTSPEA 292
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
3-375 |
1.91e-12 |
|
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: 67.71 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 3 KTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQvnGP---VGYQNWKGYTADLkDTGIYNELNNKDIALKD---GDKVV 76
Cdd:cd13586 25 KYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFF--GPhdwLGELAAAGLLAPI-PEYLAVKIKNLPVALAAvtyNGKLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 77 GIPYVMETYGIIYNKDLLKkytELPgakikdvkeiDSFDKLKEvaddmQAKKDQLGIKGAFtsaGFDSSSDWRFKTHlan 156
Cdd:cd13586 102 GVPVSVETIALFYNKDLVP---EPP----------KTWEELIA-----LAKKFNDKAGGKY---GFAYDQTNPYFSY--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 157 iPL-----SYEFKEDGVTT------QPETIKGtylpnFKNIFDLYLKDSTTAPSQlsskTGDDANSEFALGEAAFYQNGT 225
Cdd:cd13586 158 -PFlaafgGYVFGENGGDPtdiglnNEGAVKG-----LKFIKDLKKKYKVLPPDL----DYDIADALFKEGKAAMIINGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 226 WAWTDLQKAGMKPDqVGMLPIYIGAKgeenQGLATGSENYLCINAKAseADQKASKDFLNWvVTSDEGIKALSEDMGFTT 305
Cdd:cd13586 228 WDLADYKDAGINFG-VAPLPTLPGGK----QAAPFVGVQGAFVSAYS--KNKEAAVEFAEY-LTSDEAQLLLFEKTGRIP 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2060599188 306 PFKTF--DKVKSDNPLVEEAVEDSNSGkeqvawnfTMMP-----SEEWkNQLGQAMLAYAQGNGSWDDVQKAFVDNW 375
Cdd:cd13586 300 ALKDAlnDAAVKNDPLVKAFAEQAQYG--------VPMPnipemAAVW-DAMGNALNLVASGKATPEEAAKDAVAAI 367
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
1-321 |
3.27e-09 |
|
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: 57.88 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 1 TDKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQV-NGPVGYQNWKGYTADLK-DTGIYNELNNKDI-ALKDGDKVVG 77
Cdd:cd13658 23 TKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVApHDRIGSAVLQGLLSPIKlSKDKKKGFTDQALkALTYDGKLYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 78 IPYVMETYGIIYNKDLLKkytelpgakikdvKEIDSFDKLKEVADDM-QAKKDQLGIKGAFT----SAGFDSSSDwrfkt 152
Cdd:cd13658 103 LPAAVETLALYYNKDLVK-------------NAPKTFDELEALAKDLtKEKGKQYGFLADATnfyySYGLLAGNG----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 153 hlaniplSYEFKEDGVTTQPETIKGTYLPNFKNIfdLYLKDSTTAPSQLSSKTGDDANSEFALGEAAFYQNGTWAWTDLQ 232
Cdd:cd13658 165 -------GYIFKKNGSDLDINDIGLNSPGAVKAV--KFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 233 KAGMkpdQVGMLPIYIGAKGEENQGLATGSENYLcinAKASEaDQKASKDFLNWvVTSDEGIKALSEDMGFTTPFKTF-- 310
Cdd:cd13658 236 EAGV---NYGVAPLPTLPNGKPMAPFLGVKGWYL---SAYSK-HKEWAQKFMEF-LTSKENLKKRYDETNEIPPRKDVrs 307
|
330
....*....|.
gi 2060599188 311 DKVKSDNPLVE 321
Cdd:cd13658 308 DPEIKNNPLTS 318
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
2-361 |
2.15e-08 |
|
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: 55.80 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 2 DKTGVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNGPVGYQNW--KGYTADL--------KDTGIYNELNNKDIALKD 71
Cdd:cd13580 30 EKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLvkQGALWDLtdyldkyyPNLKKIIEQEGWDSASVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 72 GdKVVGIPYVME---TYGIIYNKDLLKKytelpgAKIKDVKEIdsfDKLKEVA-----DDMqakkDQLGIKGAFTSAGFD 143
Cdd:cd13580 110 G-KIYGIPRKRPligRNGLWIRKDWLDK------LGLEVPKTL---DELYEVAkafteKDP----DGNGKKDTYGLTDTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 144 SSSDWRFKTHLA--NIPLSYEFKEDGVTTQPETIkgtyLPNFKN----IFDLY---LKDSTTApsqlsSKTGDDANSEFA 214
Cdd:cd13580 176 DLIGSGFTGLFGafGAPPNNWWKDEDGKLVPGSI----QPEMKEalkfLKKLYkegLIDPEFA-----VNDGTKANEKFI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 215 LGEAAFYQnGTWAWTDLQKAGMKPDQVGM----LPIYIGAKGEENQGLATGSENYLCINAKASEAdqKASKDFLNWVVTS 290
Cdd:cd13580 247 SGKAGIFV-GNWWDPAWPQASLKKNDPDAewvaVPIPSGPDGKYGVWAESGVNGFFVIPKKSKKP--EAILKLLDFLSDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 291 D---------EGIKALSEDMGFTTPFKTFDKVKSDNPLVEEAVEDSNSGKEQVAwNFTMMPSEEWKNQLGQAMLAYAQGN 361
Cdd:cd13580 324 EvqklldygiEGVHYTVKDGGPVNIIPPDKQEVGDATLDYFQGSLALEKYKLTN-NGERKSDAKKEALDERVVNANDEEN 402
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
68-330 |
4.92e-07 |
|
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: 51.06 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 68 ALKDGDKVVGIPYVMETYGIIYNKDLLKKytelPGAKIKDVKEIDSFDKLKEVADDMQAKKDQLgikgaFTSAGFDSSSD 147
Cdd:cd13656 92 AVRYNGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALMFNLQEPY-----FTWPLIAADGG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 148 WRFKTHLAniplSYEFKEDGVTTQPETIKGTYLpnfknifdLYLKDSTTAPSQLSSKTgddANSEFALGEAAFYQNGTWA 227
Cdd:cd13656 163 YAFKYENG----KYDIKDVGVDNAGAKAGLTFL--------VDLIKNKHMNADTDYSI---AEAAFNKGETAMTINGPWA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 228 WTDLQKAGMkPDQVGMLPIYIGAKGEENQGLATGSENylcinakASEADQKASKDFLNWVVTSDEGIKALSEDMGFTTP- 306
Cdd:cd13656 228 WSNIDTSKV-NYGVTVLPTFKGQPSKPFVGVLSAGIN-------AASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVa 299
|
250 260
....*....|....*....|....
gi 2060599188 307 FKTFDKVKSDNPLVEEAVEDSNSG 330
Cdd:cd13656 300 LKSYEEELAKDPRIAATMENAQKG 323
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
50-303 |
1.08e-06 |
|
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: 50.39 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 50 TADLKDTGIYNEL--NNKDIALKDGdKVVGIPYVMETYGIIYNKDLLKK--YTELPgakiKDVKEIDSF-DKLKEVADDM 124
Cdd:cd14747 79 TPYLEDLGGDKDLfpGLVDTGTVDG-KYYGVPWYADTRALFYRTDLLKKagGDEAP----KTWDELEAAaKKIKADGPDV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 125 QA---KKDQLGIKGAFT---SAGFD--SSSDWRfkthlaniplsyefkedGVTTQPETIKGtyLPNFKNIFDLYLKDSTT 196
Cdd:cd14747 154 SGfaiPGKNDVWHNALPfvwGAGGDlaTKDKWK-----------------ATLDSPEAVAG--LEFYTSLYQKGLSPKST 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 197 APSQLssktgdDANSEFALGEAAFYQNGTWAWTDLQKAGMKP-DQVGMLPIYIGAKGeENQGLATGSEnyLCINAKASEA 275
Cdd:cd14747 215 LENSA------DVEQAFANGKVAMIISGPWEIGAIREAGPDLaGKWGVAPLPGGPGG-GSPSFAGGSN--LAVFKGSKNK 285
|
250 260
....*....|....*....|....*...
gi 2060599188 276 DqkASKDFLNWvVTSDEGIKALSEDMGF 303
Cdd:cd14747 286 D--LAWKFIEF-LSSPENQAAYAKATGM 310
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
5-380 |
1.20e-06 |
|
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: 50.07 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 5 GVQVKVQTAASGTYEQTLKSELAKSDAPTIFQVNgpvgyqnwKGYTADLKDTGIYNELNN-------KDI-------ALK 70
Cdd:cd14751 29 KIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRAD--------IAWVPEFAKLGYLQPLDGtpafddiVDYlpgpmetNRY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 71 DGdKVVGIPYVMETYGIIYNKDLLKK-YTELPGakikdvkeidSFDKLKEVADDMQAKKDQLGIKGAFTSAGFDSSSDWR 149
Cdd:cd14751 101 NG-HYYGVPQVTNTLALFYNKRLLEEaGTEVPK----------TMDELVAAAKAIKKKKGRYGLYISGDGPYWLLPFLWS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 150 FKTHLANiplsyEFKEDGVTTQPETIKGTylpnfKNIFDLYLKDSTTaPSQLSSKtgDDANSEFALGEAAFYQNGTWAWT 229
Cdd:cd14751 170 FGGDLTD-----EKKATGYLNSPESVRAL-----ETIVDLYDEGAIT-PCASGGY--PNMQDGFKSGRYAMIVNGPWAYA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 230 DLQKAGM--KPDQVGMLPIYIGAKGeenQGLATGSENYLCINakaSEADQKASKDFLNWvVTSDEGIKALSEDMGfTTPF 307
Cdd:cd14751 237 DILGGKEfkDPDNLGIAPVPAGPGG---SGSPVGGEDLVIFK---GSKNKDAAWKFVKF-MSSAEAQALTAAKLG-LLPT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 308 KT----FDKVKsDNPLVE---EAVEdsnsgkeqVAWNFTMMPS-EEWKNQLGQAMLAYAQGNgswDDVQKAfVDNWKTEY 379
Cdd:cd14751 309 RTsayeSPEVA-NNPMVAafkPALE--------TAVPRPPIPEwGELFEPLTLAFAKVLRGE---KSPREA-LDEAAKQW 375
|
.
gi 2060599188 380 D 380
Cdd:cd14751 376 D 376
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
5-303 |
8.16e-06 |
|
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: 47.29 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 5 GVQVKVQTAASGT--YEQTLKSEL-AKSDAPTIFQVNGPvgyqnWKGYTA----DLKDTGIYNELNNKDI------ALKD 71
Cdd:cd14750 29 DIKVEIEELPASSddQRQQLVTALaAGSSAPDVLGLDVI-----WIPEFAeagwLLPLTEYLKEEEDDDFlpatveANTY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 72 GDKVVGIPYVMETYGIIYNKDLLKKYTELPGAkikdvkeidSFDKLKEVADDMQAKKDqlGIKG---------------- 135
Cdd:cd14750 104 DGKLYALPWFTDAGLLYYRKDLLEKYGPEPPK---------TWDELLEAAKKRKAGEP--GIWGyvfqgkqyeglvcnfl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 136 -AFTSAGFDsssdwrfkthlaniplSYEFKEDGVTT-QPETIKGtylpnFKNIFDLYlkDSTTAPSQLSSKTGDDANSEF 213
Cdd:cd14750 173 eLLWSNGGD----------------IFDDDSGKVTVdSPEALEA-----LQFLRDLI--GEGISPKGVLTYGEEEARAAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 214 ALGEAAFYQNGTWAWTDLQKAGMK-PDQVGMLPIyigAKGEENQGlATGSENY-LCINAKASEadQKASKDFLNWvVTSD 291
Cdd:cd14750 230 QAGKAAFMRNWPYAYALLQGPESAvAGKVGVAPL---PAGPGGGS-ASTLGGWnLAISANSKH--KEAAWEFVKF-LTSP 302
|
330
....*....|..
gi 2060599188 292 EGIKALSEDMGF 303
Cdd:cd14750 303 EVQKRRAINGGL 314
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
73-297 |
1.08e-05 |
|
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: 46.99 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 73 DKVVGIPYVMETYGIIYNKDLLKkytELPgakikdvkeiDSFDKLKEVADDMQAK-KDQLGIKGAFTSAGFDSSSDWRFK 151
Cdd:cd13657 102 GKVYGLPEAYETVALIYNKALVD---QPP----------ETTDELLAIMKDHTDPaAGSYGLAYQVSDAYFVSAWIFGFG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 152 THLANiplsYEFKEDGVTTqPETIKGtylpnFKNIFDLYLKDSTTAPSqlssktGDDANSEFALGEAAFYQNGTWAWTDL 231
Cdd:cd13657 169 GYYFD----DETDKPGLDT-PETIKG-----IQFLKDFSWPYMPSDPS------YNTQTSLFNEGKAAMIINGPWFIGGI 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2060599188 232 QKAGmkpDQVGMLPIyigAKGEENQGLA--TGSEN-YLCINAKASEADqkASKDFLNWvVTSDEGIKAL 297
Cdd:cd13657 233 KAAG---IDLGVAPL---PTVDGTNPPRpySGVEGiYVTKYAERKNKE--AALDFAKF-FTTAEASKIL 292
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
68-300 |
1.13e-05 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 46.93 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 68 ALKDGDKVVGIPYVMETYGIIYNKDLLKKytelPGAKIKDVKEIDsfDKLKEvaddmQAKKDQL-GIKGA-FTSAGFDSS 145
Cdd:PRK09474 122 AVRYNGKLIGYPIAVEALSLIYNKDLVPT----PPKTWEEIPALD--KELKA-----KGKSAIMwNLQEPyFTWPLIAAD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 146 SDWRFKTHLANiplsYEFKEDGVTTqPETIKGTylpNFknIFDLYLKDSTTAPSQLSSktgddANSEFALGEAAFYQNGT 225
Cdd:PRK09474 191 GGYAFKFENGG----YDVKDVGVNN-AGAKAGL---QF--LVDLVKNKHMNADTDYSI-----AEAAFNKGETAMTINGP 255
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2060599188 226 WAWTDLQKAGMkPDQVGMLPIYIGAKGEENQGLATGSenylcINAkASeADQKASKDFL-NWVVTsDEGIKALSED 300
Cdd:PRK09474 256 WAWSNIDKSGI-NYGVTVLPTFNGKPSKPFVGVLSAG-----INA-AS-PNKELAKEFLeNYLLT-DEGLETVNKD 322
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
5-246 |
1.50e-03 |
|
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: 40.47 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 5 GVQVKVQTAASGTYEQTLKSELAKSDAPTIF-QVNGPVGYQNWKGYTADLKDtgiYNELNNKDI-----ALKDGDKVVGI 78
Cdd:cd13522 29 GITVEVTYQDTEARRQFFSTAAAGGKGPDVVfGPSDSLGPFAAAGLLAPLDE---YVSKSGKYApntiaAMKLNGKLYGV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 79 PYVMETYGIIYNKDLLkkyTELPGAKIKDVKEIDSFDKLKEVADDMqakkdqlgikgaftsagFDSSSDWRFKTHLANIP 158
Cdd:cd13522 106 PVSVGAHLMYYNKKLV---PKNPPKTWQELIALAQGLKAKNVWGLV-----------------YNQNEPYFFAAWIGGFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060599188 159 lSYEFKEDGVTTQPETIKGTYLPNFKNIFDLYLKDSTTAPSqlsskTGDD-ANSEFALGEAAFYQNGTWAWTDLQKAgMK 237
Cdd:cd13522 166 -GQVFKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPE-----TDYSiADALFKAGKAAMIINGPWDLGDYRQA-LK 238
|
....*....
gi 2060599188 238 PDqVGMLPI 246
Cdd:cd13522 239 IN-LGVAPL 246
|
|
| |
