|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
16-361 |
6.47e-36 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 135.94 E-value: 6.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 16 LVSVAALSFGALAACG---NTTAVDSSKGRVYYLNKKAEEQEKWEALAQAFQDET-GIE-TQIQLSATDYDQTLRSEMAK 90
Cdd:COG1653 5 ALALAAALALALAACGgggSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKvEVESVPYDDYRTKLLTALAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 91 DEAPTMFQADGPSFM-YSWLDYAADMSDS-KIYGELTDSYKDRTLKNA--DGKPVGIPYAVESYGIIYNKSLLKKYfdas 166
Cdd:COG1653 85 GNAPDVVQVDSGWLAeFAAAGALVPLDDLlDDDGLDKDDFLPGALDAGtyDGKLYGVPFNTDTLGLYYNKDLFEKA---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 167 wssvkSIDGLNNFKALKTVADEIQEHKDDMGvkgaFTSAGMDSSAFrynfhlpsLPLFYE-----YRDDG-VDMNSvPES 240
Cdd:COG1653 161 -----GLDPPKTWDELLAAAKKLKAKDGVYG----FALGGKDGAAW--------LDLLLSaggdlYDEDGkPAFDS-PEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 241 VKGtyVDYMQNIYDlyitDATVPASSLsGKTMDDATSEFALGEAVFFQDGVWIYSALQDQGfPDEDLGVLPIYMGVDGEE 320
Cdd:COG1653 223 VEA--LEFLKDLVK----DGYVPPGAL-GTDWDDARAAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKK 294
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1143275849 321 KQGLnqVISNYWCVNSKSsqKDQEATQQFLEWLVTSDAARE 361
Cdd:COG1653 295 PASV--LGGSGLAIPKGS--KNPEAAWKFLKFLTSPEAQAK 331
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
58-388 |
6.39e-26 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 106.34 E-value: 6.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 58 ALAQAFQDETGIETQIQLSAT-DYDQTLRSEMAKDEAPT--MFQADGPSFM-YSWLDYAADMSDSKIYGELTDSYKDRTL 133
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEPQASnDLQAKLLAAAAAGNAPDldVVWIAADQLAtLAEAGLLADLSDVDNLDDLPDALDAAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 134 knaDGKPVGIPYAVES-YGIIYNKSLLKKyfdaSWSSVKSIDGLNNFKAlktvadeiqehkddmGVKGAFTSAgMDSSAF 212
Cdd:pfam13416 81 ---DGKLYGVPYAASTpTVLYYNKDLLKK----AGEDPKTWDELLAAAA---------------KLKGKTGLT-DPATGW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 213 RYNFhlpslpLFYEYRDDGVDMNSVPESVKgtYVDYMQNIYDlyitDATVPASSlsgktmDDATSEFALGEAVFFQDGVW 292
Cdd:pfam13416 138 LLWA------LLADGVDLTDDGKGVEALDE--ALAYLKKLKD----NGKVYNTG------ADAVQLFANGEVAMTVNGTW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 293 IYSALQDQGFPdedLGVLPIYMG--VDGEekqglnqvisnYWCVNSKSSqKDQEATQQFLEWLvTSDAARESISQDMGLV 370
Cdd:pfam13416 200 AAAAAKKAGKK---LGAVVPKDGsfLGGK-----------GLVVPAGAK-DPRLAALDFIKFL-TSPENQAALAEDTGYI 263
|
330
....*....|....*...
gi 1143275849 371 TPFKTFDEEAYTVKNPLV 388
Cdd:pfam13416 264 PANKSAALSDEVKADPAL 281
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
50-361 |
1.40e-17 |
|
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: 83.99 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 50 AEEQEKWEALAQAFQDE-TGIETQ-IQLSATDYDQTLRSEMAKDEAPTMFQADGPSF-MYSWLDYAADMSDSKIYGELTD 126
Cdd:cd13585 10 PAETAALKKLIDAFEKEnPGVKVEvVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVpEFASNGALLDLDDYIEKDGLDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 127 SYKDRTLK--NADGKPVGIPYAVESYGIIYNKSLLKKYFDASwssvksidglnnfKALKTVADEI---QEHKDDMGVKGA 201
Cdd:cd13585 90 DFPPGLLDagTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGP-------------KPPWTWDELLeaaKKLTDKKGGQYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 202 FTSAGMDSSAFRYnfhlpsLPLFYEY------RDDG-VDMNSvPESVKGtyvdyMQNIYDLYiTDATVPASSLSGKtmDD 274
Cdd:cd13585 157 FALRGGSGGQTQW------YPFLWSNggdlldEDDGkATLNS-PEAVEA-----LQFYVDLY-KDGVAPSSATTGG--DE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 275 ATSEFALGEAVFFQDGVWIYSALQDQGfPDEDLGVLPIYMGVDGEEKQGLNqviSNYWCVNSKSsqKDQEATQQFLEWLV 354
Cdd:cd13585 222 AVDLFASGKVAMMIDGPWALGTLKDSK-VKFKWGVAPLPAGPGGKRASVLG---GWGLAISKNS--KHPEAAWKFIKFLT 295
|
....*..
gi 1143275849 355 TSDAARE 361
Cdd:cd13585 296 SKENQLK 302
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
13-398 |
4.01e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 48.85 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 13 AIGLVSVAALSFGALAAC--GNTTA-VDSSKGrvyYlNKKAEEQEKWEAlaqafqdETGIETQIQL--SATD-YDQTlrs 86
Cdd:PRK09474 11 ALSALATLMFSASALAKIeeGKLVIwINGDKG---Y-NGLAEVGKKFEK-------DTGIKVTVEHpdKLEEkFPQV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 87 emakdeAPTmfqADGPSFMYSWLDYAADMSDSKIYGELTDS--YKDRTLKNA------DGKPVGIPYAVESYGIIYNKSL 158
Cdd:PRK09474 77 ------AAT---GDGPDIIFWAHDRFGGYAQSGLLAEVTPSkaFKDKLVPFTwdavryNGKLIGYPIAVEALSLIYNKDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 159 LKKYfDASWSSVKSIDglnnfKALKTvadeiqehkddmgvKGaftsagmdSSAFRYNFHLP--SLPLF-------YEYRD 229
Cdd:PRK09474 148 VPTP-PKTWEEIPALD-----KELKA--------------KG--------KSAIMWNLQEPyfTWPLIaadggyaFKFEN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 230 DGVDMNSVPESVKGTyVDYMQNIYDLyITDATVPAsslsgkTMDDATSE--FALGEAVFFQDGVWIYSALQDQGFpdeDL 307
Cdd:PRK09474 200 GGYDVKDVGVNNAGA-KAGLQFLVDL-VKNKHMNA------DTDYSIAEaaFNKGETAMTINGPWAWSNIDKSGI---NY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 308 GVLPIyMGVDGEEKQGLNQVISNywCVNSKSSQKDqeATQQFLEWLVTSDAARESISQDMGL-VTPFKTFDEEayTVKNP 386
Cdd:PRK09474 269 GVTVL-PTFNGKPSKPFVGVLSA--GINAASPNKE--LAKEFLENYLLTDEGLETVNKDKPLgAVALKSFQEE--LAKDP 341
|
410
....*....|..
gi 1143275849 387 LVEANREYQENG 398
Cdd:PRK09474 342 RIAATMDNAQNG 353
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
16-361 |
6.47e-36 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 135.94 E-value: 6.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 16 LVSVAALSFGALAACG---NTTAVDSSKGRVYYLNKKAEEQEKWEALAQAFQDET-GIE-TQIQLSATDYDQTLRSEMAK 90
Cdd:COG1653 5 ALALAAALALALAACGgggSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKvEVESVPYDDYRTKLLTALAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 91 DEAPTMFQADGPSFM-YSWLDYAADMSDS-KIYGELTDSYKDRTLKNA--DGKPVGIPYAVESYGIIYNKSLLKKYfdas 166
Cdd:COG1653 85 GNAPDVVQVDSGWLAeFAAAGALVPLDDLlDDDGLDKDDFLPGALDAGtyDGKLYGVPFNTDTLGLYYNKDLFEKA---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 167 wssvkSIDGLNNFKALKTVADEIQEHKDDMGvkgaFTSAGMDSSAFrynfhlpsLPLFYE-----YRDDG-VDMNSvPES 240
Cdd:COG1653 161 -----GLDPPKTWDELLAAAKKLKAKDGVYG----FALGGKDGAAW--------LDLLLSaggdlYDEDGkPAFDS-PEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 241 VKGtyVDYMQNIYDlyitDATVPASSLsGKTMDDATSEFALGEAVFFQDGVWIYSALQDQGfPDEDLGVLPIYMGVDGEE 320
Cdd:COG1653 223 VEA--LEFLKDLVK----DGYVPPGAL-GTDWDDARAAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKK 294
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1143275849 321 KQGLnqVISNYWCVNSKSsqKDQEATQQFLEWLVTSDAARE 361
Cdd:COG1653 295 PASV--LGGSGLAIPKGS--KNPEAAWKFLKFLTSPEAQAK 331
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
12-443 |
4.44e-27 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 112.35 E-value: 4.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 12 KAIGLVSVAALSFGALAACGNTTAVDSSKG--------RVYYlnkKAEEQEKWEALAQAFQDETGIETQIQ-LSATDYDQ 82
Cdd:COG2182 4 RLLAALALALALALALAACGSGSSSSGSSSaagaggtlTVWV---DDDEAEALEEAAAAFEEEPGIKVKVVeVPWDDLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 83 TLRSEMAKDEAPTMFQADGPsFMYSWLD--YAADMSDSKiygELTDSYKDRTLKNA--DGKPVGIPYAVESYGIIYNKSL 158
Cdd:COG2182 81 KLTTAAPAGKGPDVFVGAHD-WLGELAEagLLAPLDDDL---ADKDDFLPAALDAVtyDGKLYGVPYAVETLALYYNKDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 159 LKKyfdaswSSVKSIDGLnnFKALKTVADEiqehkddmGVKGaFTSAGMDSsafrynFHLPSL------PLFYEYRDDG- 231
Cdd:COG2182 157 VKA------EPPKTWDEL--IAAAKKLTAA--------GKYG-LAYDAGDA------YYFYPFlaafggYLFGKDGDDPk 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 232 -VDMNSvPESVKGtyVDYMQNIYDlyitDATVPASSlsgkTMDDATSEFALGEAVFFQDGVWIYSALQDQGfpDEDLGVL 310
Cdd:COG2182 214 dVGLNS-PGAVAA--LEYLKDLIK----DGVLPADA----DYDAADALFAEGKAAMIINGPWAAADLKKAL--GIDYGVA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 311 PIYMGVDGEEKQGLNQVISnyWCVNSKSsqKDQEATQQFLEWLVTSDAAREsISQDMGLVTPFKTFDEEAYTVKNPLVEA 390
Cdd:COG2182 281 PLPTLAGGKPAKPFVGVKG--FGVSAYS--KNKEAAQEFAEYLTSPEAQKA-LFEATGRIPANKAAAEDAEVKADPLIAA 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1143275849 391 NREYQENGYYdVISVSTVSHQWEkDLGSAELNYAQGQGD----WDAVKKVFTDDWAK 443
Cdd:COG2182 356 FAEQAEYAVP-MPNIPEMGAVWT-PLGTALQAIASGKADpaeaLDAAQKQIEAAIAQ 410
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
58-388 |
6.39e-26 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 106.34 E-value: 6.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 58 ALAQAFQDETGIETQIQLSAT-DYDQTLRSEMAKDEAPT--MFQADGPSFM-YSWLDYAADMSDSKIYGELTDSYKDRTL 133
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEPQASnDLQAKLLAAAAAGNAPDldVVWIAADQLAtLAEAGLLADLSDVDNLDDLPDALDAAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 134 knaDGKPVGIPYAVES-YGIIYNKSLLKKyfdaSWSSVKSIDGLNNFKAlktvadeiqehkddmGVKGAFTSAgMDSSAF 212
Cdd:pfam13416 81 ---DGKLYGVPYAASTpTVLYYNKDLLKK----AGEDPKTWDELLAAAA---------------KLKGKTGLT-DPATGW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 213 RYNFhlpslpLFYEYRDDGVDMNSVPESVKgtYVDYMQNIYDlyitDATVPASSlsgktmDDATSEFALGEAVFFQDGVW 292
Cdd:pfam13416 138 LLWA------LLADGVDLTDDGKGVEALDE--ALAYLKKLKD----NGKVYNTG------ADAVQLFANGEVAMTVNGTW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 293 IYSALQDQGFPdedLGVLPIYMG--VDGEekqglnqvisnYWCVNSKSSqKDQEATQQFLEWLvTSDAARESISQDMGLV 370
Cdd:pfam13416 200 AAAAAKKAGKK---LGAVVPKDGsfLGGK-----------GLVVPAGAK-DPRLAALDFIKFL-TSPENQAALAEDTGYI 263
|
330
....*....|....*...
gi 1143275849 371 TPFKTFDEEAYTVKNPLV 388
Cdd:pfam13416 264 PANKSAALSDEVKADPAL 281
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
50-361 |
1.40e-17 |
|
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: 83.99 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 50 AEEQEKWEALAQAFQDE-TGIETQ-IQLSATDYDQTLRSEMAKDEAPTMFQADGPSF-MYSWLDYAADMSDSKIYGELTD 126
Cdd:cd13585 10 PAETAALKKLIDAFEKEnPGVKVEvVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVpEFASNGALLDLDDYIEKDGLDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 127 SYKDRTLK--NADGKPVGIPYAVESYGIIYNKSLLKKYFDASwssvksidglnnfKALKTVADEI---QEHKDDMGVKGA 201
Cdd:cd13585 90 DFPPGLLDagTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGP-------------KPPWTWDELLeaaKKLTDKKGGQYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 202 FTSAGMDSSAFRYnfhlpsLPLFYEY------RDDG-VDMNSvPESVKGtyvdyMQNIYDLYiTDATVPASSLSGKtmDD 274
Cdd:cd13585 157 FALRGGSGGQTQW------YPFLWSNggdlldEDDGkATLNS-PEAVEA-----LQFYVDLY-KDGVAPSSATTGG--DE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 275 ATSEFALGEAVFFQDGVWIYSALQDQGfPDEDLGVLPIYMGVDGEEKQGLNqviSNYWCVNSKSsqKDQEATQQFLEWLV 354
Cdd:cd13585 222 AVDLFASGKVAMMIDGPWALGTLKDSK-VKFKWGVAPLPAGPGGKRASVLG---GWGLAISKNS--KHPEAAWKFIKFLT 295
|
....*..
gi 1143275849 355 TSDAARE 361
Cdd:cd13585 296 SKENQLK 302
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
43-362 |
3.29e-13 |
|
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: 70.87 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 43 VYYLNKKAEEQEKWEALAQAFQDET-GIETQIQLSATDYDQT-LRSEMAKDEAPTMFQADGPSFMYSWLD--YAADMSDS 118
Cdd:cd14749 4 YWQYFTGDTKKKYMDELIADFEKENpNIKVKVVVFPYDNYKTkLKTAVAAGEGPDVFNLWPGGWLAEFVKagLLLPLTDY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 119 KIYGELTDSYKDRTLKNA--DGKPVGIPYAVESYGIIYNKSLLKKYfdaswssvksidglNNFKALKT---VADEIQEHK 193
Cdd:cd14749 84 LDPNGVDKRFLPGLADAVtfNGKVYGIPFAARALALFYNKDLFEEA--------------GGVKPPKTwdeLIEAAKKDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 194 DDMGVKGAFTSAGMDSSAFrynfhlpslpLFYEY--RDDGVDMNSVPESVKGTY-----VDYMQNIYDLYITDATVPAss 266
Cdd:cd14749 150 FKAKGQTGFGLLLGAQGGH----------WYFQYlvRQAGGGPLSDDGSGKATFndpafVQALQKLQDLVKAGAFQEG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 267 LSGKTMDDATSEFALGEAVFFQDGVWIYSALqDQGFPDEDLGVLPIYMGVDGEEKQglnQVISNYWCVNSKSSQKDQEAT 346
Cdd:cd14749 218 FEGIDYDDAGQAFAQGKAAMNIGGSWDLGAI-KAGEPGGKIGVFPFPTVGKGAQTS---TIGGSDWAIAISANGKKKEAA 293
|
330
....*....|....*.
gi 1143275849 347 QQFLEWLVTSDAARES 362
Cdd:cd14749 294 VKFLKYLTSPEVMKQY 309
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
125-390 |
3.45e-13 |
|
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: 70.59 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 125 TDSYKDRTLK--NADGKPVGIPYAVESYGIIYNKSLLKkyfdaswssvksidglnnfKALKTVADEIQEHKDDMGVKGAF 202
Cdd:cd13658 83 KKGFTDQALKalTYDGKLYGLPAAVETLALYYNKDLVK-------------------NAPKTFDELEALAKDLTKEKGKQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 203 TSAGMDSSAFRYNFhlpslPLFYEY-------RDDGVDMNSV----PESVKGtyVDYMQNIYdlyiTDATVPAsSLSGKT 271
Cdd:cd13658 144 YGFLADATNFYYSY-----GLLAGNggyifkkNGSDLDINDIglnsPGAVKA--VKFLKKWY----TEGYLPK-GMTGDV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 272 MDdatSEFALGEAVFFQDGVWIYSALQDQGFpdeDLGVLPIYMGVDGEEKQ----GLNQVISNYwcvnskssQKDQEATQ 347
Cdd:cd13658 212 IQ---GLFKEGKAAAVIDGPWAIQEYQEAGV---NYGVAPLPTLPNGKPMApflgVKGWYLSAY--------SKHKEWAQ 277
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1143275849 348 QFLEWLvTSDAARESISQDMGLVTPFKTFDEEAYTVKNPLVEA 390
Cdd:cd13658 278 KFMEFL-TSKENLKKRYDETNEIPPRKDVRSDPEIKNNPLTSA 319
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
51-359 |
4.37e-12 |
|
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: 66.67 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 51 EEQEKWEALAQAFQ-DETGIETQIQ-LSATDYDQTLRSEMAKDEAPtmfqADgpsFMYSWLDYAADMSDSKIYGELtDSY 128
Cdd:pfam01547 5 TEAAALQALVKEFEkEHPGIKVEVEsVGSGSLAQKLTTAIAAGDGP----AD---VFASDNDWIAELAKAGLLLPL-DDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 129 KDRTLKNADGKPVGIPYAVESYGIIYNKSLLKKYfdaswssvkSIDGLNNFKALKTVADEIQEHKDDMGVKGAFTSAGmD 208
Cdd:pfam01547 77 VANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKA---------GLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASG-T 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 209 SSAFRYNFHLPSLPLFYEYRDDGVDmnsvpESVKGTYVDYMQNIYDLYITDATVPASSLSGKTMDDATSEFALGEAVFFQ 288
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGGGLD-----NPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143275849 289 DGVWIYSALQDQG---FPDEDLGVLPIYMGVDGEEKQGLNQVISNYWCVNSKSsqKDQEATQQFLEWLVTSDAA 359
Cdd:pfam01547 222 VGPWAALAANKVKlkvAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGS--KNKEAAKKFLDFLTSPEAQ 293
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
51-390 |
9.72e-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: 66.16 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 51 EEQEKWEALAQAFQDETGIETQIQLSATDydqTLRSEMAKDeAPTmfqADGPSFMYSWLDYAADMSDSKIYGELtDSYKD 130
Cdd:cd13586 10 GELEYLKELAEEFEKKYGIKVEVVYVDSG---DTREKFITA-GPA---GKGPDVFFGPHDWLGELAAAGLLAPI-PEYLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 131 RTLKNA---------DGKPVGIPYAVESYGIIYNKSLLKkyfdaswssvksidglnnfKALKTVADEIQEHKDDMGVKGa 201
Cdd:cd13586 82 VKIKNLpvalaavtyNGKLYGVPVSVETIALFYNKDLVP-------------------EPPKTWEELIALAKKFNDKAG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 202 ftsagmDSSAFRYNFHLP--SLPLF-----YEYRDDGVDMNSV----PESVKGtyvdyMQNIYDLyITDATVPASSLSGK 270
Cdd:cd13586 142 ------GKYGFAYDQTNPyfSYPFLaafggYVFGENGGDPTDIglnnEGAVKG-----LKFIKDL-KKKYKVLPPDLDYD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 271 TMDdatSEFALGEAVFFQDGVWIYSALQDQGFpdeDLGVLPIYMgVDGeEKQGLNQVISNYWCVNSKSsqKDQEATQQFL 350
Cdd:cd13586 210 IAD---ALFKEGKAAMIINGPWDLADYKDAGI---NFGVAPLPT-LPG-GKQAAPFVGVQGAFVSAYS--KNKEAAVEFA 279
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1143275849 351 EWLvTSDAARESISQDMGLVTPFKTFDEEAYTVKNPLVEA 390
Cdd:cd13586 280 EYL-TSDEAQLLLFEKTGRIPALKDALNDAAVKNDPLVKA 318
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
57-393 |
3.98e-09 |
|
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: 58.07 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 57 EALAQAF---QDETGIETQIQLSATDYDQTLRSEMAKDEAPTMFQADG---PSF--------MYSWLDyAADMSDSKIYG 122
Cdd:cd14748 17 EELVDEFnksHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDAswvAQLadsgalepLDDYID-KDGVDDDDFYP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 123 ELTDSYKDrtlknaDGKPVGIPYAVESYGIIYNKSLLKKYfdaswssvkSIDGLN---NFKALKTVADEIQEHKDDMGVK 199
Cdd:cd14748 96 AALDAGTY------DGKLYGLPFDTSTPVLYYNKDLFEEA---------GLDPEKppkTWDELEEAAKKLKDKGGKTGRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 200 GaFTSAGMDSSAFRYNFHLPSLPLFYEYRDDGVDMNSvPESVKgtyvdYMQNIYDLYITDATVPasslsGKTMDDATSEF 279
Cdd:cd14748 161 G-FALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNS-PEGVE-----ALEFLVDLVGKDGVSP-----LNDWGDAQDAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 280 ALGEAVFFQDGVWIYSALQDQGfPDEDLGVLPIymgVDGEEKQGLNQVISNYWCVNSKSSqKDQEATQQFLEWLvTSDAA 359
Cdd:cd14748 229 ISGKVAMTINGTWSLAGIRDKG-AGFEYGVAPL---PAGKGKKGATPAGGASLVIPKGSS-KKKEAAWEFIKFL-TSPEN 302
|
330 340 350
....*....|....*....|....*....|....*.
gi 1143275849 360 RESISQDMGLVTPFKTF--DEEAYTVKNPLVEANRE 393
Cdd:cd14748 303 QAKWAKATGYLPVRKSAaeDPEEFLAENPNYKVAVD 338
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
50-390 |
5.37e-09 |
|
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270454 [Multi-domain] Cd Length: 376 Bit Score: 57.77 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 50 AEEQEKWEALAQAFQDETGietQIQLSAT--DYDQTL---RSEMAKDEAPTMFQAD---GPSFmySWLDYAADMSDSKIY 121
Cdd:cd14751 10 DEEKVLYEKLIPAFEKEYP---KIKVKAVrvPFDGLHnqiKTAAAGGQAPDVMRADiawVPEF--AKLGYLQPLDGTPAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 122 GELTDsYKDRTLKNA--DGKPVGIPYAVESYGIIYNKSLLKkyfDASWSSVKSIDglnnfkALKTVADEIQEHKddmGVK 199
Cdd:cd14751 85 DDIVD-YLPGPMETNryNGHYYGVPQVTNTLALFYNKRLLE---EAGTEVPKTMD------ELVAAAKAIKKKK---GRY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 200 GAFTSAgmDSSafrYNFhlpsLPLFYEYRDDGVD-------MNSvPESVKGtyvdyMQNIYDLYITDATVPASSLSGKTM 272
Cdd:cd14751 152 GLYISG--DGP---YWL----LPFLWSFGGDLTDekkatgyLNS-PESVRA-----LETIVDLYDEGAITPCASGGYPNM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 273 DDAtseFALGEAVFFQDGVWIYSALQ-DQGF-PDEDLGVLPIYMGvdgeeKQGLNQVISNYWCVNSKSSQKDQEATqQFL 350
Cdd:cd14751 217 QDG---FKSGRYAMIVNGPWAYADILgGKEFkDPDNLGIAPVPAG-----PGGSGSPVGGEDLVIFKGSKNKDAAW-KFV 287
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1143275849 351 EWLvTSDAARESISQDMGLVTPFKTFDEEAYTVKNPLVEA 390
Cdd:cd14751 288 KFM-SSAEAQALTAAKLGLLPTRTSAYESPEVANNPMVAA 326
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
50-360 |
6.20e-07 |
|
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: 51.22 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 50 AEEQEKWEALAQAFQDETGIET-QIQLSAT-DYDQTLRSEMAKDEAPTMFqadgpSFMYSWLDYAADMSDSK-IYGELTD 126
Cdd:cd13657 10 GAEEDALQQIIDEFEAKYPVPNvKVPFEKKpDLQNKLLTAIPAGEGPDLF-----IWAHDWIGQFAEAGLLVpISDYLSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 127 SYKDRTLKNA------DGKPVGIPYAVESYGIIYNKSLLKKyfdaswssvksidglnnfkALKTVADEIQEHKDdmgvkg 200
Cdd:cd13657 85 DDFENYLPTAveavtyKGKVYGLPEAYETVALIYNKALVDQ-------------------PPETTDELLAIMKD------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 201 aFTSAGMDSSAFRYNFHLP--SLPLFY----EYRDDGVDMNSV--PESVKGtyVDYMQNIYDLYItdatvpASSLSGKTM 272
Cdd:cd13657 140 -HTDPAAGSYGLAYQVSDAyfVSAWIFgfggYYFDDETDKPGLdtPETIKG--IQFLKDFSWPYM------PSDPSYNTQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 273 ddaTSEFALGEAVFFQDGVWIYSALQDQGFpdeDLGVLPI-----------YMGVDGeekqglnqvisnyWCVNSKSSQK 341
Cdd:cd13657 211 ---TSLFNEGKAAMIINGPWFIGGIKAAGI---DLGVAPLptvdgtnpprpYSGVEG-------------IYVTKYAERK 271
|
330
....*....|....*....
gi 1143275849 342 DQEATQQFLEWLVTSDAAR 360
Cdd:cd13657 272 NKEAALDFAKFFTTAEASK 290
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
13-398 |
4.01e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 48.85 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 13 AIGLVSVAALSFGALAAC--GNTTA-VDSSKGrvyYlNKKAEEQEKWEAlaqafqdETGIETQIQL--SATD-YDQTlrs 86
Cdd:PRK09474 11 ALSALATLMFSASALAKIeeGKLVIwINGDKG---Y-NGLAEVGKKFEK-------DTGIKVTVEHpdKLEEkFPQV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 87 emakdeAPTmfqADGPSFMYSWLDYAADMSDSKIYGELTDS--YKDRTLKNA------DGKPVGIPYAVESYGIIYNKSL 158
Cdd:PRK09474 77 ------AAT---GDGPDIIFWAHDRFGGYAQSGLLAEVTPSkaFKDKLVPFTwdavryNGKLIGYPIAVEALSLIYNKDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 159 LKKYfDASWSSVKSIDglnnfKALKTvadeiqehkddmgvKGaftsagmdSSAFRYNFHLP--SLPLF-------YEYRD 229
Cdd:PRK09474 148 VPTP-PKTWEEIPALD-----KELKA--------------KG--------KSAIMWNLQEPyfTWPLIaadggyaFKFEN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 230 DGVDMNSVPESVKGTyVDYMQNIYDLyITDATVPAsslsgkTMDDATSE--FALGEAVFFQDGVWIYSALQDQGFpdeDL 307
Cdd:PRK09474 200 GGYDVKDVGVNNAGA-KAGLQFLVDL-VKNKHMNA------DTDYSIAEaaFNKGETAMTINGPWAWSNIDKSGI---NY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 308 GVLPIyMGVDGEEKQGLNQVISNywCVNSKSSQKDqeATQQFLEWLVTSDAARESISQDMGL-VTPFKTFDEEayTVKNP 386
Cdd:PRK09474 269 GVTVL-PTFNGKPSKPFVGVLSA--GINAASPNKE--LAKEFLENYLLTDEGLETVNKDKPLgAVALKSFQEE--LAKDP 341
|
410
....*....|..
gi 1143275849 387 LVEANREYQENG 398
Cdd:PRK09474 342 RIAATMDNAQNG 353
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
43-404 |
8.65e-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: 47.67 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 43 VYYLNKKAEEQEKWEALAQAFQDETGIET----QIQLSATDYDQTLRSEM-AKDEAPTMFQADGPsfmysWL-DYAADMS 116
Cdd:cd14750 3 TFAAGSDGQEGELLKKAIAAFEKKHPDIKveieELPASSDDQRQQLVTALaAGSSAPDVLGLDVI-----WIpEFAEAGW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 117 DSKIYGELTDSYKDRTLKNA------DGKPVGIPYAVESYGIIYNKSLLKKYFD---ASWssvksidglnnfKALKTVAD 187
Cdd:cd14750 78 LLPLTEYLKEEEDDDFLPATveantyDGKLYALPWFTDAGLLYYRKDLLEKYGPeppKTW------------DELLEAAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 188 EIQEHKDDMgvkGAFTSAGMDSSAFRYNFhlpsLPLFYEYRDDGVD-------MNSvPESVKGtyVDYMQNIYDLYITda 260
Cdd:cd14750 146 KRKAGEPGI---WGYVFQGKQYEGLVCNF----LELLWSNGGDIFDddsgkvtVDS-PEALEA--LQFLRDLIGEGIS-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 261 tvPASSLSGKTmDDATSEFALGEAVFFQDGVWIYSALQDQGFPDED-LGVLPIYMGVDGEEKQ---GLNqvisnyWCVNS 336
Cdd:cd14750 214 --PKGVLTYGE-EEARAAFQAGKAAFMRNWPYAYALLQGPESAVAGkVGVAPLPAGPGGGSAStlgGWN------LAISA 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143275849 337 KSsqKDQEATQQFLEWLVTSDAARESISQDMGLVTPFKTFDEEAYTVKNPLVEANREYQENG-------YYDVIS 404
Cdd:cd14750 285 NS--KHKEAAWEFVKFLTSPEVQKRRAINGGLPPTRRALYDDPEVLEAYPFLPALLEALENAvprpvtpKYPEVS 357
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
20-168 |
5.29e-05 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 45.29 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 20 AALSFGALAACGNTTAVDSSKGRVYYLNkkaeeqekW-----EALAQAFQDETGIETQIQLSATDydqtlrsemakDEAP 94
Cdd:COG0687 8 GLAAAALAAALAGGAPAAAAEGTLNVYN--------WggyidPDVLEPFEKETGIKVVYDTYDSN-----------EEML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 95 TMFQADGPSF--MYSWLDYAADMSDSKIYGELTDS----YKD-----RTLKNADGKPVGIPYAVESYGIIYNKSLLKKYF 163
Cdd:COG0687 69 AKLRAGGSGYdvVVPSDYFVARLIKAGLLQPLDKSklpnLANldprfKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPP 148
|
....*
gi 1143275849 164 DaSWS 168
Cdd:COG0687 149 T-SWA 152
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
61-358 |
1.75e-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: 40.77 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 61 QAFQDETGIETQIQ-LSATDYDQTLRSEMAKDEAPTMFQADGPSFMYSWLDYAADMSDSKIYGELTDSYK----DRTLKN 135
Cdd:cd13580 26 KYLEEKTNIDVKVKwVPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLVKQGALWDLTDYLDKYYPNLKkiieQEGWDS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 136 A--DGKPVGIPYAVESY---GIIYNKSLLKKYfdaswssvksidGLnnfKALKTVaDEIQE--------------HKDDM 196
Cdd:cd13580 106 AsvDGKIYGIPRKRPLIgrnGLWIRKDWLDKL------------GL---EVPKTL-DELYEvakaftekdpdgngKKDTY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 197 GVKGAFTSAGMDSSAFRYNFHLPSLPLFYEyrDDGVDmnsVPESVKGTYVDYMQNIYDLY---------ITDATvpassl 267
Cdd:cd13580 170 GLTDTKDLIGSGFTGLFGAFGAPPNNWWKD--EDGKL---VPGSIQPEMKEALKFLKKLYkeglidpefAVNDG------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 268 sgktmDDATSEFALGEAVFFQ----DGVWIYSALQDqGFPDEDLGVLPIYMGVDGEEKQGLNQVISNYWCVNSKSsqKDQ 343
Cdd:cd13580 239 -----TKANEKFISGKAGIFVgnwwDPAWPQASLKK-NDPDAEWVAVPIPSGPDGKYGVWAESGVNGFFVIPKKS--KKP 310
|
330
....*....|....*
gi 1143275849 344 EATQQFLEWLVTSDA 358
Cdd:cd13580 311 EAILKLLDFLSDPEV 325
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
59-161 |
4.18e-03 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 39.15 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143275849 59 LAQAFQDETGIETQ-IQLSATDYDQTLRSEmAKDEAPTMFQADGPSFMYSW--LDYAADMsDSKIYGELTDSYKDrtlkn 135
Cdd:COG1840 1 LLEAFEKKTGIKVNvVRGGSGELLARLKAE-GGNPPADVVWSGDADALEQLanEGLLQPY-KSPELDAIPAEFRD----- 73
|
90 100
....*....|....*....|....*.
gi 1143275849 136 ADGKPVGIpyAVESYGIIYNKSLLKK 161
Cdd:COG1840 74 PDGYWFGF--SVRARVIVYNTDLLKE 97
|
|
|