|
Name |
Accession |
Description |
Interval |
E-value |
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-346 |
4.18e-76 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 241.87 E-value: 4.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 1 MNKRMIGLLAISTALLVTTACSSGGSGGSGKKIEISFTdvAPSPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKL 80
Cdd:COG1653 1 MRRLALALAAALALALAACGGGGSGAAAAAGKVTLTVW--HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 81 TTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTQYDE--WDNKDNLTAFAKNVTIEQQQrepfkdvYLIPDAFMGGALF 158
Cdd:COG1653 79 LTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDdgLDKDDFLPGALDAGTYDGKL-------YGVPFNTDTLGLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 159 IRTDWMKEANLEMPKTWDELFNVAEKLTDPaKNRYGFSYRGARAGFDQILAYIFSvtkGESYEADGTSVLLRPEALTAFK 238
Cdd:COG1653 152 YNKDLFEKAGLDPPKTWDELLAAAKKLKAK-DGVYGFALGGKDGAAWLDLLLSAG---GDLYDEDGKPAFDSPEAVEALE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 239 RYTDIYKKGWAPKDSINWGYQEMVQGFTSGVTGILAQTTEVVATAKDSMKDGTWTVIPNPHAVDGNTYAGAGASWGYSIS 318
Cdd:COG1653 228 FLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAPLPGGPGGKKPASVLGGSGLAIP 307
|
330 340
....*....|....*....|....*...
gi 690615523 319 KNSKNKEAAWKFIEFISKPENNNKYSKV 346
Cdd:COG1653 308 KGSKNPEAAWKFLKFLTSPEAQAKWDAL 335
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
34-418 |
1.95e-75 |
|
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: 240.77 E-value: 1.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 34 EISFTDVApSPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPIS 113
Cdd:cd13585 1 TLTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 114 TQYDEWDNKDN-LTAFAKNVTIEQQQrepfkdvYLIPDAFMGGALFIRTDWMKEA--NLEMPKTWDELFNVAEKLTDPAK 190
Cdd:cd13585 80 DYIEKDGLDDDfPPGLLDAGTYDGKL-------YGLPFDADTLVLFYNKDLFDKAgpGPKPPWTWDELLEAAKKLTDKKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 191 NRYGFSYRGARAGFDQILAYIFSvtKGESY--EADGTSVLLRPEALTAFKRYTDIYKKGWAPkDSINWGYQEMVQGFTSG 268
Cdd:cd13585 153 GQYGFALRGGSGGQTQWYPFLWS--NGGDLldEDDGKATLNSPEAVEALQFYVDLYKDGVAP-SSATTGGDEAVDLFASG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 269 VTGILAQTTEVVATAKDSMKDGTWTVIPNPHAVDGNTYAGAGaSWGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMT 348
Cdd:cd13585 230 KVAMMIDGPWALGTLKDSKVKFKWGVAPLPAGPGGKRASVLG-GWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 690615523 349 MIPIMQDSLKDPELGQGPMKGFIDMLNDPKLIPPADYGKFPelgEFRESFMDAEVQKYLLG--TQSAEDTLK 418
Cdd:cd13585 309 PAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPW---PEVYPILSEALQEALLGalGKSPEEALK 377
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
34-433 |
1.70e-58 |
|
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: 196.83 E-value: 1.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 34 EISFTDVAPSPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYP-AWLTTFVPAGYLEPI 112
Cdd:cd14749 1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPgGWLAEFVKAGLLLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 113 STQYDEWD-NKDNLTAFAKNVTIEqqqrepfKDVYLIPDAFMGGALFIRTDWMKEA-NLEMPKTWDELFNVAEKLTDPAK 190
Cdd:cd14749 81 TDYLDPNGvDKRFLPGLADAVTFN-------GKVYGIPFAARALALFYNKDLFEEAgGVKPPKTWDELIEAAKKDKFKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 191 NRYGFsyrgARAGFDQILAYIFSVTK----GESYEADGTSVLL--RPEALTAFKRYTDIYKKGWAPKDSINWGYQEMVQG 264
Cdd:cd14749 154 GQTGF----GLLLGAQGGHWYFQYLVrqagGGPLSDDGSGKATfnDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDAGQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 265 FTSGVTGILAQTTEVVATAKDSMKDGTWTVIPNPHAVDGNTY-AGAGASWGYSISKNSKNKEAAWKFIEFISKPENNNKY 343
Cdd:cd14749 230 FAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGKGAQTsTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 344 SKVMTMIPIMQDSLKDPELGQGPMKG-FIDMLNDPKLIPPADYGKfpelGEFRESFMDAeVQKYLLGTQSAEDTLKhlgd 422
Cdd:cd14749 310 LEDVGLLPAKEVVAKDEDPDPVAILGpFADVLNAAGSTPFLDEYW----PAAAQVHKDA-VQKLLTGKIDPEQVVK---- 380
|
410
....*....|.
gi 690615523 423 fltKAQQKFMK 433
Cdd:cd14749 381 ---QAQSAAAK 388
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
42-426 |
1.01e-56 |
|
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: 192.14 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 42 PSPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTQYDEWDN 121
Cdd:cd14747 8 GNSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLEDLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 122 KDNLTAFAKNVTIeqqqrepFKD-VYLIPDAFMGGALFIRTDWMKEAN-LEMPKTWDELFNVAEKLTDPAKNRYGFSYRG 199
Cdd:cd14747 88 DKDLFPGLVDTGT-------VDGkYYGVPWYADTRALFYRTDLLKKAGgDEAPKTWDELEAAAKKIKADGPDVSGFAIPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 200 ARAGFDQILAYIFSvtKGESY--EADGTSVLLRPEALTAFKRYTDIYKKGWAPKDSINWGYQeMVQGFTSGVTGILAQTT 277
Cdd:cd14747 161 KNDVWHNALPFVWG--AGGDLatKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAD-VEQAFANGKVAMIISGP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 278 EVVATAKDSMK--DGTWTV--IPNPHAVDGNTYAGaGASWgySISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIM 353
Cdd:cd14747 238 WEIGAIREAGPdlAGKWGVapLPGGPGGGSPSFAG-GSNL--AVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPAN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 690615523 354 QDSLKDPELGQGP-MKGFIDMLNDPKLIPPAdygkfPELGEFrESFMDAEVQK-YLLGTQSAEDTLKHLGDFLTK 426
Cdd:cd14747 315 TSAWDDPSLANDPlLAVFAEQLKTGKATPAT-----PEWGEI-EAELVLVLEEvWIGVGADVEDALDKAAAEINE 383
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-418 |
1.55e-55 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 189.78 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 1 MNKRMIGLLAISTAL-LVTTAC-----SSGGSGGSGKKIEISFTDvapSPEREKFFNEIIADFEKEnTNIKVKLETVPWD 74
Cdd:COG2182 1 MKRRLLAALALALALaLALAACgsgssSSGSSSAAGAGGTLTVWV---DDDEAEALEEAAAAFEEE-PGIKVKVVEVPWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 75 QAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPIStqyDEWDNKDNLTAFA-KNVTIEQQqrepfkdVYLIPDAFM 153
Cdd:COG2182 77 DLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLD---DDLADKDDFLPAAlDAVTYDGK-------LYGVPYAVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 154 GGALFIRTDWMKEanlEMPKTWDELFNVAEKLTDPakNRYGFSYRGAR--------AGFDqilAYIFsvtkGESYEADGT 225
Cdd:COG2182 147 TLALYYNKDLVKA---EPPKTWDELIAAAKKLTAA--GKYGLAYDAGDayyfypflAAFG---GYLF----GKDGDDPKD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 226 SVLLRPEALTAFKRYTDIYKKGWAPKDsinWGYQEMVQGFTSGVTGILAQTTEVVATAKDSMKDgTWTVIPNPHAVDGNT 305
Cdd:COG2182 215 VGLNSPGAVAALEYLKDLIKDGVLPAD---ADYDAADALFAEGKAAMIINGPWAAADLKKALGI-DYGVAPLPTLAGGKP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 306 YAGAGASWGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQDSLKDPELGQGP-MKGFIDMLNDPKLIPpad 384
Cdd:COG2182 291 AKPFVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPlIAAFAEQAEYAVPMP--- 367
|
410 420 430
....*....|....*....|....*....|....
gi 690615523 385 ygKFPELGEFrESFMDAEVQKYLLGTQSAEDTLK 418
Cdd:COG2182 368 --NIPEMGAV-WTPLGTALQAIASGKADPAEALD 398
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
48-418 |
7.30e-51 |
|
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: 176.71 E-value: 7.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 48 KFFNEIIADFEKENTNIKVKLETVPW-DQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTQYDEWDNKDN-- 124
Cdd:cd14748 14 KALEELVDEFNKSHPDIKVKAVYQGSyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDKDGVDDDdf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 125 LTAFAKNVTIEQQQrepfkdvYLIPDAFMGGALFIRTDWMKEANL---EMPKTWDELFNVAEKLTDPAKN--RYGFS-YR 198
Cdd:cd14748 94 YPAALDAGTYDGKL-------YGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGGKtgRYGFAlPP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 199 GARAGFDQILAYIFSvtkGESYEADGTSVLLR-PEALTAFKRYTD-IYKKGWAPKDSINWGYqemvQGFTSGVTGILAQT 276
Cdd:cd14748 167 GDGGWTFQALLWQNG---GDLLDEDGGKVTFNsPEGVEALEFLVDlVGKDGVSPLNDWGDAQ----DAFISGKVAMTING 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 277 TEVVATAKDSMKDGTWTVIPNPhAVDGNTYAGAGASWGYSISKN-SKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQD 355
Cdd:cd14748 240 TWSLAGIRDKGAGFEYGVAPLP-AGKGKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 690615523 356 SLKDPE--LGQGP-MKGFIDMLNDPKLIPPAdygkFPELGEFRESFMDAeVQKYLLGTQSAEDTLK 418
Cdd:cd14748 319 AAEDPEefLAENPnYKVAVDQLDYAKPWGPP----VPNGAEIRDELNEA-LEAALLGKKTPEEALK 379
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
34-418 |
4.91e-43 |
|
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: 155.53 E-value: 4.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 34 EISFTDVAPSPEREkFFNEIIADFEKENTNIKVKLETVPW--DQAFAKLTTQGQSKTL-PDVVNVYPAWLTTFVPAGYLE 110
Cdd:cd14750 1 TITFAAGSDGQEGE-LLKKAIAAFEKKHPDIKVEIEELPAssDDQRQQLVTALAAGSSaPDVLGLDVIWIPEFAEAGWLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 111 PISTQYDEWDNKDNLTAFAKNVTIEQQqrepfkdVYLIPDAFMGGALFIRTDWMKEANLEMPKTWDELFNVAEKLTDPAK 190
Cdd:cd14750 80 PLTEYLKEEEDDDFLPATVEANTYDGK-------LYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 191 NRYGFSYRGARA-----GFdqiLAYIFSvTKGESYEAD-GTSVLLRPEALTAFKRYTDIYKKGWAPKDSINWGYQEMVQG 264
Cdd:cd14750 153 GIWGYVFQGKQYeglvcNF---LELLWS-NGGDIFDDDsGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 265 FTSGVTGILAQTTEVVATAKDSMKD--GTWTVIPNPHAVDGNTYAGAGAsWGYSISKNSKNKEAAWKFIEFISKPENNNK 342
Cdd:cd14750 229 FQAGKAAFMRNWPYAYALLQGPESAvaGKVGVAPLPAGPGGGSASTLGG-WNLAISANSKHKEAAWEFVKFLTSPEVQKR 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 690615523 343 YSKVMTMIPIMQDSLKDPELGQG-PMKGFI-DMLNDPKLIPPADYgkFPELgefrESFMDAEVQKYLLGTQSAEDTLK 418
Cdd:cd14750 308 RAINGGLPPTRRALYDDPEVLEAyPFLPALlEALENAVPRPVTPK--YPEV----STAIQIALSAALSGQATPEEALK 379
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
43-422 |
7.20e-42 |
|
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: 152.53 E-value: 7.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 43 SPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTQYDEWDNK 122
Cdd:cd14751 9 SDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 123 DNLTAFAKNVTIEQQqrepfkdVYLIPDAFMGGALFIRTDWMKEANLEMPKTWDELFNVAEKLTDpAKNRYGFSYRGARA 202
Cdd:cd14751 89 DYLPGPMETNRYNGH-------YYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKK-KKGRYGLYISGDGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 203 GFdqILAYIFSVTKGESYEADGTSVLLRPEALTAFKRYTDIYKKGWAPKDsINWGYQEMVQGFTSGvtgilaqttEVVAt 282
Cdd:cd14751 161 YW--LLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAITPC-ASGGYPNMQDGFKSG---------RYAM- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 283 akdsMKDGTWTV---IPNPHAVDGNTY------AGAGAS------WGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVM 347
Cdd:cd14751 228 ----IVNGPWAYadiLGGKEFKDPDNLgiapvpAGPGGSgspvggEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 690615523 348 TMIPIMQDSLKDPELGQGPM-KGFIDMLNDPKLIPPadygkFPELGEFRESFMDAeVQKYLLGTQSAEDTLKHLGD 422
Cdd:cd14751 304 GLLPTRTSAYESPEVANNPMvAAFKPALETAVPRPP-----IPEWGELFEPLTLA-FAKVLRGEKSPREALDEAAK 373
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
41-340 |
2.57e-36 |
|
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: 135.24 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 41 APSPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLP-DVVNVYPAWLTTFVPAGYLEPISTqydew 119
Cdd:pfam01547 1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 120 dnkdnltaFAKNVTIEQQQrepfkDVYLIPDAFMGGALFIRTDWMKEANLEMPKTWDELFNVAEKLTDPAKNRYGfSYRG 199
Cdd:pfam01547 76 --------YVANYLVLGVP-----KLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGG-AGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 200 ARAGFDQILAYIFSVTKGESYEADGTSVLLRPEALTAFKRYTDIY-----KKGWAPKDSINWGYQEMVQGFTSGVTG-IL 273
Cdd:pfam01547 142 DASGTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYakvllLKKLKNPGVAGADGREALALFEQGKAAmGI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 690615523 274 AQTTEVVATAKDSMKDGTWTVIPNPHAVDG-----NTYAGAGASWGYSISKNSKNKEAAWKFIEFISKPENN 340
Cdd:pfam01547 222 VGPWAALAANKVKLKVAFAAPAPDPKGDVGyaplpAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
31-438 |
2.92e-28 |
|
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: 116.27 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 31 KKIEIS-----FTDVAPSPEREKFFNEIiadfeKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVY-PAWLTTFV 104
Cdd:cd13580 1 EPVTITivanlGGNPKPDPDDNPYTKYL-----EEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNdPQLSITLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 105 PAGYLEPISTQYDewDNKDNLTAFaknvtIEQQQREPFKD---VYLIP---DAFMGGALFIRTDWMKEANLEMPKTWDEL 178
Cdd:cd13580 76 KQGALWDLTDYLD--KYYPNLKKI-----IEQEGWDSASVdgkIYGIPrkrPLIGRNGLWIRKDWLDKLGLEVPKTLDEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 179 FNVAEKLT--DPAKN----RYGFSYR--GARAGFDQILAYIFSVTKGESYEADGTSV--LLRPEALTAFKRYTDIYKKGW 248
Cdd:cd13580 149 YEVAKAFTekDPDGNgkkdTYGLTDTkdLIGSGFTGLFGAFGAPPNNWWKDEDGKLVpgSIQPEMKEALKFLKKLYKEGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 249 APKDSINWGYQEMVQGFTSGVTGI----LAQTTEVVATAKDSMKDGTWTVIPNPHAVDGNTYAGA-GASWGY-SISKNSK 322
Cdd:cd13580 229 IDPEFAVNDGTKANEKFISGKAGIfvgnWWDPAWPQASLKKNDPDAEWVAVPIPSGPDGKYGVWAeSGVNGFfVIPKKSK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 323 NKEAAWKFIEFISKPENNN--------------KYSKVMTMIPIMQDSLKDPELGQGPMKGFIdMLNDPKLIPPADYGKF 388
Cdd:cd13580 309 KPEAILKLLDFLSDPEVQKlldygiegvhytvkDGGPVNIIPPDKQEVGDATLDYFQGSLALE-KYKLTNNGERKSDAKK 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 690615523 389 PELGEFRESFMDAEVQKYLLG--TQSAEDTLKHLGDFLTKAQQ----KFMKDHPDI 438
Cdd:cd13580 388 EALDERVVNANDEENENIAVGppTETLVSPTEKYGATLDKLEDdaftKIIMGQIPL 443
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
52-366 |
2.06e-26 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 107.88 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 52 EIIADFEKEnTNIKVKLETVPWDQAFAKLTTQGQSKTLPD--VVNVYPAWLTTFVPAGYLEPISTQydewDNKDNLTAFA 129
Cdd:pfam13416 1 ALAKAFEKK-TGVTVEVEPQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLSDV----DNLDDLPDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 130 KNVTIEQQqrepfkdVYLIP-DAFMGGALFIRTDWMKEANLEmPKTWDELFNVAEKLtdpaKNRYGFSyrGARAGFDQIL 208
Cdd:pfam13416 76 DAAGYDGK-------LYGVPyAASTPTVLYYNKDLLKKAGED-PKTWDELLAAAAKL----KGKTGLT--DPATGWLLWA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 209 AYIFsvtkGESYEADGTSVLLRPEALTAFKRYTDiYKKGWapkdsinWGYQEMVQGFTSGVTGILAQTTEVVATAKDsmK 288
Cdd:pfam13416 142 LLAD----GVDLTDDGKGVEALDEALAYLKKLKD-NGKVY-------NTGADAVQLFANGEVAMTVNGTWAAAAAKK--A 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 289 DGTWTVI-PNPHAVDGntyagaGASWGysISKNSKNKE-AAWKFIEFISKPENNNKYSKVMTMIPIMQDSLKDPELGQGP 366
Cdd:pfam13416 208 GKKLGAVvPKDGSFLG------GKGLV--VPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKADP 279
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
45-419 |
2.77e-26 |
|
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: 109.31 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 45 EREKFFNEIIADFEKENtNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTQYDewDNKDN 124
Cdd:cd13586 10 GELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLA--VKIKN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 125 LTAFAKNVTIEQQqrepfkdVYLIPDAFMGGALFIRTDWMKEAnlemPKTWDELFNVAEKLTDPAKNRYGFSYRGARAGF 204
Cdd:cd13586 87 LPVALAAVTYNGK-------LYGVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFNDKAGGKYGFAYDQTNPYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 205 DQIL-----AYIFsvtkGESYEADGTSVLLRPEALTAFKRYTD-IYKKGWAPKDSinwGYQEMVQGFTSGVTGILAQTTE 278
Cdd:cd13586 156 SYPFlaafgGYVF----GENGGDPTDIGLNNEGAVKGLKFIKDlKKKYKVLPPDL---DYDIADALFKEGKAAMIINGPW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 279 VVATAKDSMKDGTWTVIPN-PHAVDGNTYAGagaSWGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQDSL 357
Cdd:cd13586 229 DLADYKDAGINFGVAPLPTlPGGKQAAPFVG---VQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDAL 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 690615523 358 KDPELGQGP-MKGFIDMLNDPKLIPpadygKFPELGEFRESFMDAeVQKYLLGTQSAEDTLKH 419
Cdd:cd13586 306 NDAAVKNDPlVKAFAEQAQYGVPMP-----NIPEMAAVWDAMGNA-LNLVASGKATPEEAAKD 362
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
47-371 |
3.33e-24 |
|
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: 103.33 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 47 EKFFNEIIADFEKEnTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTqydewdNKDNLT 126
Cdd:cd13658 12 MAFIKKIAKQYTKK-TGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKL------SKDKKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 127 AFAKNvtiEQQQREPFKDVYLIPDAFMGGALFIRTDWMKEAnlemPKTWDELFNVAEKLTDPAKNRYGF---------SY 197
Cdd:cd13658 85 GFTDQ---ALKALTYDGKLYGLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLTKEKGKQYGFladatnfyySY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 198 rGARAGFDqilAYIFSVTKGESYEAD-GtsvLLRPEALTAFKRYTDIYKKGWAPK----DSINwgyqemvQGFTSGVTGI 272
Cdd:cd13658 158 -GLLAGNG---GYIFKKNGSDLDINDiG---LNSPGAVKAVKFLKKWYTEGYLPKgmtgDVIQ-------GLFKEGKAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 273 LAQTTEVVATAKDSMKDgtWTVIPNPHAVDGNTYAGAGASWGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPI 352
Cdd:cd13658 224 VIDGPWAIQEYQEAGVN--YGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPP 301
|
330 340
....*....|....*....|
gi 690615523 353 MQDSLKDPELGQGPM-KGFI 371
Cdd:cd13658 302 RKDVRSDPEIKNNPLtSAFA 321
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
43-418 |
6.92e-21 |
|
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: 93.63 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 43 SPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPIstqyDEWDNK 122
Cdd:cd13522 9 DTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPL----DEYVSK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 123 DNLTAFAKNVTIEQQQRepfkdVYLIPDAFMGGALFIRTDwmkeaNLEM--PKTWDELFNVAEKLTdpAKNRYGFSYRGA 200
Cdd:cd13522 85 SGKYAPNTIAAMKLNGK-----LYGVPVSVGAHLMYYNKK-----LVPKnpPKTWQELIALAQGLK--AKNVWGLVYNQN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 201 RAGFDQILAYIFSVTKGESYEADGTSVLLRPEALTAFKRYTD-IYKKGWAPKDSinwGYQEMVQGFTSGVTGILAQTTEV 279
Cdd:cd13522 153 EPYFFAAWIGGFGGQVFKANNGKNNPTLDTPGAVEALQFLVDlKSKYKIMPPET---DYSIADALFKAGKAAMIINGPWD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 280 VATAKDSMKDgTWTVIPNPHaVDGNTYAGAG-ASWGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQDSLK 358
Cdd:cd13522 230 LGDYRQALKI-NLGVAPLPT-FSGTKHAAPFvGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAYE 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 690615523 359 DPELGQGP-MKGFIDMLNDPKLIPpadygKFPELGEFRESFMDAeVQKYLLGTQSAEDTLK 418
Cdd:cd13522 308 SPAVQNKPaQKASAEQAAYGVPMP-----NIPEMRAVWDAFRIA-VNSVLAGKVTPEAAAK 362
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
59-338 |
6.95e-21 |
|
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: 94.83 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 59 KENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNVyPAWLTTFVPAGY---LEPIStqyDEWDNKDNLTAFAKNVtIE 135
Cdd:cd13521 27 EKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGA-DYLKDKFIAYGMegaFLPLS---KYIDQYPNLKAFFKQH-PD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 136 QQQREPFKD--VYLIP----DAFMGGALFIRTDWMKEANLEMPKTWDELFNVAEKLT--DPAKN----RYGFSYRGARAG 203
Cdd:cd13521 102 VLRASTASDgkIYLIPyeppKDVPNQGYFIRKDWLDKLNLKTPKTLDELYNVLKAFKekDPNGNgkadEIPFIDRDPLYG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 204 FDQILA-----YIFSVTKGESYEADGT--SVLLRPEALTAFKRYTDIYKKGWAPKDSINWGYQEMVQGFTSG-VTGILAQ 275
Cdd:cd13521 182 AFRLINswgarSAGGSTDSDWYEDNGKfkHPFASEEYKDGMKYMNKLYTEGLIDKESFTQKDDQAEQKFSNGkLGGFTHN 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 276 TTEVVA--TAKDSMKDGTWTVIPNPHAVDG-----NTYAGAGASWGYSISKNSKNKEAAWKFIEFISKPE 338
Cdd:cd13521 262 WFASDNlfTAQLGKEKPMYILLPIAPAGNVkgrreEDSPGYTGPDGVAISKKAKNPVAALKFFDWLASEE 331
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
43-379 |
7.58e-18 |
|
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: 84.74 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 43 SPEREKFFNEIIADFEKEN--TNIKVKLETVPWDQAfaKLTTQGQSKTLPDVVNVYPAWLTTFVPAGYLEPISTQYDEWD 120
Cdd:cd13657 9 TGAEEDALQQIIDEFEAKYpvPNVKVPFEKKPDLQN--KLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISDYLSEDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 121 NKDNLTAFAKNVTieqqqrepFKD-VYLIPDAFMGGALFIRTDWMKEAnlemPKTWDELFNVAEKLTDPAKNRYGFSYRG 199
Cdd:cd13657 87 FENYLPTAVEAVT--------YKGkVYGLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHTDPAAGSYGLAYQV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 200 ARAGFDQILAYIFSvtkGESYEADGTSVLLR-PEALTAFKRYTDiYKKGWAPKDSinwGYQEMVQGFTSGVTGILAQTTE 278
Cdd:cd13657 155 SDAYFVSAWIFGFG---GYYFDDETDKPGLDtPETIKGIQFLKD-FSWPYMPSDP---SYNTQTSLFNEGKAAMIINGPW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 279 VVATAKDSMKDgtWTVIPNPhAVDGN----TYAGAgASWGYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQ 354
Cdd:cd13657 228 FIGGIKAAGID--LGVAPLP-TVDGTnpprPYSGV-EGIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGYVPAAT 303
|
330 340 350
....*....|....*....|....*....|...
gi 690615523 355 DSLKDPELGQGPM-KGF-------IDMLNDPKL 379
Cdd:cd13657 304 NAYDDAEVAADPViAAFkaqaehgVPMPNSPEM 336
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
1-385 |
2.65e-16 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 79.95 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 1 MNKRMIGLLAISTALLVTTACSSggsggsgkkieisftdvAPSPERE-KFFN-------EIIADFEKEnTNIKVKLETVP 72
Cdd:COG0687 1 MSRRSLLGLAAAALAAALAGGAP-----------------AAAAEGTlNVYNwggyidpDVLEPFEKE-TGIKVVYDTYD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 73 -WDQAFAKLTTQGQSktlPDVVNVYPAWLTTFVPAGYLEPISTqyDEWDNKDNLTAFAKNVTIEQqqrepfKDVYLIPda 151
Cdd:COG0687 63 sNEEMLAKLRAGGSG---YDVVVPSDYFVARLIKAGLLQPLDK--SKLPNLANLDPRFKDPPFDP------GNVYGVP-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 152 FMGGALFI--RTDWMKEAnlemPKTWDELFnvaekltDPA-KNRYGFsYRGARAGFDQILAYIfsvtkGESY----EADG 224
Cdd:COG0687 130 YTWGTTGIayNTDKVKEP----PTSWADLW-------DPEyKGKVAL-LDDPREVLGAALLYL-----GYDPnstdPADL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 225 TSVLlrpEALTAFKRYTDIYkkgWApkdsinwGYQEMVQGFTSGVTGILAQTTEVVATAKDSMKDGTWtVIPnphaVDGN 304
Cdd:COG0687 193 DAAF---ELLIELKPNVRAF---WS-------DGAEYIQLLASGEVDLAVGWSGDALALRAEGPPIAY-VIP----KEGA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 305 TYagagasW--GYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQDSLK--DPElgqgpmkgfidMLNDPKLI 380
Cdd:COG0687 255 LL------WfdNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAAREllPPE-----------LAANPAIY 317
|
....*
gi 690615523 381 PPADY 385
Cdd:COG0687 318 PPEEV 322
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
59-338 |
5.17e-15 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 77.01 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 59 KENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVVNV-YPAWLTTFVPAGYLEPISTQYDEWDN-KDNLTAFAKNVTIEQ 136
Cdd:cd13583 27 EEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPVlYPGEENEFVASGALLPISDYLDYMPNyKKYVEKWGLGKELAT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 137 QQREPFKdVYLIP----DAFMGGALFIRTDWMKEANLEMPKTWDELFNVAEKLTDPAKNRYGFSYRGARAGFDQILAYIF 212
Cdd:cd13583 107 GRQSDGK-YYSLPglheDPGVQYSFLYRKDIFEKAGIKIPTTWDEFYAALKKLKEKYPDSYPYSDRWNSNALLLIAAPAF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 213 SVTKG-----ESYEADGTSVLLRP------EALTAFKRytdIYKKGWAPKDSINWGYQEMVQGFTSGVTGIL---AQTTE 278
Cdd:cd13583 186 GTTAGwgfsnYTYDPDTDKFVYGAttdeykDMLQYFNK---LYAEGLLDPESFTQTDDQAKAKFLNGKSFVIttnPQTVD 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 690615523 279 VVATAKDSMKDGTWTV--IPNPHAVDGNTYAGAGASWGYSIS---KNSKNKEAAWKFIEFISKPE 338
Cdd:cd13583 263 ELQRNLRAADGGNYEVvsITPPAGPAGKAINGSRLENGFMISskaKDSKNFEALLQFLDWLYSDE 327
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
32-338 |
2.78e-13 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270299 [Multi-domain] Cd Length: 490 Bit Score: 71.58 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 32 KIEISFTdVAPSPEREKFFNEIIADFEKENTNIKVKLETVPWDQAFAKLTTQGQSKTLPDVV---NVYPAWLTTFVPAGY 108
Cdd:cd13581 1 KVTLTIF-VRKSPLVEDYNENLFFKRLEEKTGIKIEWETVPEDAWAEKKNLMLASGDLPDAFlgaGASDADLMTYGKQGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 109 LEPISTQYDEwdNKDNLTA-FAKNVTIEQQQREPFKDVYLIPDAF------MGGALFIRTDWMKEANLEMPKTWDELFNV 181
Cdd:cd13581 80 FLPLEDLIDK--YAPNLKAlFDENPDIKAAITAPDGHIYALPSVNecyhcsYGQRMWINKKWLDKLGLEMPTTTDELYEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 182 --AEKLTDPAKN----RYGFSYRGARAGFDQIL----AYIFSVTKGESY---EADGT--SVLLRPEALTAFKRYTDIYKK 246
Cdd:cd13581 158 lkAFKEQDPNGNgkadEIPLSFSGLNGGTDDPAfllnSFGINDGGYGGYgfvVKDGKviYTATDPEYKEALAYLNKLYKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 247 GWAPKDS--INWGY--------QEMVqGFTSGVTGILAQTTEvvaTAKDsmkdgtWTVIPNPHAVDGNTYAGAGAS---- 312
Cdd:cd13581 238 GLIDPEAftQDYDQlaakgkasTAKV-GVFFGWDPGLFFGEE---RYEQ------YVPLPPLKGPNGDQLAWVGNSsgyg 307
|
330 340
....*....|....*....|....*..
gi 690615523 313 -WGYSISKNSKNKEAAWKFIEFISKPE 338
Cdd:cd13581 308 rGGFVITSKNKNPEAAIRWADFLYSPE 334
|
|
| PBP2_AlgQ1_2 |
cd13584 |
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ... |
32-338 |
4.26e-10 |
|
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270302 [Multi-domain] Cd Length: 481 Bit Score: 61.68 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 32 KIEISFTDVAPSPEREKFFNEIiadfeKENTNIKVKLETVPWDQA-FAKLTTQGQSKTLPDVVN----VYPAWLTTFVPA 106
Cdd:cd13584 5 WIHMHFRDKWPNDNDLPVYKEM-----ERKTNVKLNFVANPVAQNsQEQFNLMMASGQLPDIIGgdwlKDKGGFEKYGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 107 GYLEPISTQYDEwdNKDNLTAFAK-NVTIEQQQREPFKDVYLIP--------DAFMGgaLFIRTDWMKEANLEMPKTWDE 177
Cdd:cd13584 80 GAFLPLNDLIDQ--YAPNLKKFLDeHPDVKKAITTDDGNIYGFPylpdgdvaKEARG--YFIRKDWLDKLGLKTPSTIDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 178 LFNV--AEKLTDPAKN----RYGFSYRGARAGFDQILAYIFSVTKgESYEADGTsvLLRPEALTAFKRYTDI----YKKG 247
Cdd:cd13584 156 WYTVlkAFKERDPNGNgkadEVPLILTKPGYDETGRLINAWGAYM-DFYQENGK--VKYGPLEPGFKDFLKTmnqwYKEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 248 WAPKDSI---NWGYQEMVQGFTSG-VTGILAQTTEVVATA-KDSMKDGTWTVIPNPHAVDGNTYAG-----AGASWGYSI 317
Cdd:cd13584 233 LIDPDFFtrkAKAREQNIMNGNIGgFTHDWFASTGTFNLAlLKNVPDFKLVAVPPPVLNKGQTPYEedsrqIAKGDGAAI 312
|
330 340
....*....|....*....|.
gi 690615523 318 SKNSKNKEAAWKFIEFISKPE 338
Cdd:cd13584 313 TASNKNPVLAIKWLDYAYSEE 333
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
53-362 |
6.39e-09 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 56.87 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 53 IIADFEKEnTNIKVKLETVPWDQAFAKLTTQGqSKTLPDVV-NVYPAWLTTFVPAGYLEPISTqyDEWDNkdnltafakn 131
Cdd:COG1840 1 LLEAFEKK-TGIKVNVVRGGSGELLARLKAEG-GNPPADVVwSGDADALEQLANEGLLQPYKS--PELDA---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 132 vtIEQQQREPfkDVYLIPDAFMGGALFIRTDWMKEanLEMPKTWDElfnvaekLTDPA-KNRYGFsYRGARAGFDQILAY 210
Cdd:COG1840 67 --IPAEFRDP--DGYWFGFSVRARVIVYNTDLLKE--LGVPKSWED-------LLDPEyKGKIAM-ADPSSSGTGYLLVA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 211 IFSVTKGESYEADGtsvllrpeaLTAFKRYTDIYKKGwapkDSinwgyqEMVQGFTSGVTGILAQTTEVVATAKDSMKDG 290
Cdd:COG1840 133 ALLQAFGEEKGWEW---------LKGLAANGARVTGS----SS------AVAKAVASGEVAIGIVNSYYALRAKAKGAPV 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 690615523 291 TWtVIPNphavDGNTYAGAGAswgySISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIPIMQDSLKDPEL 362
Cdd:COG1840 194 EV-VFPE----DGTLVNPSGA----AILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGL 256
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
47-351 |
4.31e-08 |
|
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. 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.
Pssm-ID: 270307 [Multi-domain] Cd Length: 268 Bit Score: 54.15 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 47 EKFFNEIIAD-FEKEnTNIKVKLETVPWDQAFAKLTTQGQSKTLpDVVNVYPAWLTTFVPAGYLEPIstQYDEWDNKDNL 125
Cdd:cd13589 12 EDAQRKAVIEpFEKE-TGIKVVYDTGTSADRLAKLQAQAGNPQW-DVVDLDDGDAARAIAEGLLEPL--DYSKIPNAAKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 126 TAFAKnvtieqqqrepFKDVYLIPDAFMGGALFIRTDWMKEAnlemPKTWDelfnvaekLTDPA-KNRYGFsYRGARAGF 204
Cdd:cd13589 88 KAPAA-----------LKTGYGVGYTLYSTGIAYNTDKFKEP----PTSWW--------LADFWdVGKFPG-PRILNTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 205 DQILaYIFSVTKGES-YEADgtsvllrPEAltAFKRYTDIYK--KGWAPKDSinwgyqEMVQGFTSGVTGILAQTTEVVA 281
Cdd:cd13589 144 LALL-EAALLADGVDpYPLD-------VDR--AFAKLKELKPnvVTWWTSGA------QLAQLLQSGEVDMAPAWNGRAQ 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 282 TAKDSMKDGTWtVIPnphavDGNTYAGAGAswgYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTMIP 351
Cdd:cd13589 208 ALIDAGAPVAF-VWP-----KEGAILGPDT---LAIVKGAPNKELAMKFINFALSPEVQAALAEALGYGP 268
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
52-339 |
5.07e-06 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. 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.
Pssm-ID: 270308 [Multi-domain] Cd Length: 315 Bit Score: 48.00 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 52 EIIADFEKEnTNIKVKLETVPW-DQAFAKLTTQGQSKTlpDVVNVYPAWLTTFVPAGYLEPIstqydewdNKDNLTAFAk 130
Cdd:cd13590 14 EVLKAFEKE-TGVKVNYDTYDSnEEMLAKLRAGGGSGY--DLVVPSDYMVERLIKQGLLEPL--------DHSKLPNLK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 131 nvTIEQQQREPFKD---VYLIPdaFMGGALFI--RTDWMKEAnlemPKTWDELFNVAEkltdpAKNRYGFsYRGARAGFD 205
Cdd:cd13590 82 --NLDPQFLNPPYDpgnRYSVP--YQWGTTGIayNKDKVKEP----PTSWDLDLWDPA-----LKGRIAM-LDDAREVLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 206 QILAYIfsvtkGESYEADGTSVLLRP-EALTAFKRYTDIYkkgwapkdsinwGYQEMVQGFTSGVTGIlAQT-TEVVATA 283
Cdd:cd13590 148 AALLAL-----GYSPNTTDPAELAAAaELLIKQKPNVRAF------------DSDSYVQDLASGEIWL-AQAwSGDALQA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 690615523 284 KDSMKDGTWtVIPNPhavdgntyagaGAS-W--GYSISKNSKNKEAAWKFIEFISKPEN 339
Cdd:cd13590 210 NRENPNLKF-VIPKE-----------GGLlWvdNMAIPKGAPNPELAHAFINFLLDPEV 256
|
|
| PBP2_AlgQ_like_3 |
cd13582 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
33-340 |
1.76e-05 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270300 [Multi-domain] Cd Length: 504 Bit Score: 46.93 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 33 IEISFTDVAPSPEREKFFNEIIADFEKEnTNIKVKLETVPWDQAfAKLTTQGQSKTLPDVVNVYPAwLTTFVPAGYLEPI 112
Cdd:cd13582 2 ITFTFFSADSNATPDDFKTPVAKKITEL-TGVTLEIEYLVGGEK-QKIGLMIASGDLPDLIYAKGD-TDKLIEAGALVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 113 StqydewdnkDNLTAFAKNV------TIEQQQREPFKDVY-------LIPDAFMGGALFIRTDWMKEANLEMPKTWDELF 179
Cdd:cd13582 79 D---------DLIEKYGPNIkkwygdYLLKKLRSEDGHIYylpnyrvEDAPWYPNGGFWLQHDVLKELGYPKIKTLDDYE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 180 NVAEKltdpAKNRY---------GFSYRGARAGF----DQILAYIFSVTKGESYEADGTSVL----LRPEALTAFKRYTD 242
Cdd:cd13582 150 NLIKD----YKKKYptingqptiGFTALTDDWRFlisvTNPAFLAGYPNDGEVYVDPKTLKAkfhyTRPYYKEYYKWLNE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 243 IYKKGWAPKDSINWGYQEMVQGFTSG-VTGILAQTTEVvATAKDSMK---DGTWTVIPNPHAVDGNTY------AGAGAS 312
Cdd:cd13582 226 LWNEGLLDKESFTQKYDQYLAKIASGrVLGFYDAGWDI-GNAITALKakgKDERLYAYYPVAVGVDDKdynygdPGYLGG 304
|
330 340
....*....|....*....|....*...
gi 690615523 313 WGYSISKNSKNKEAAWKFIEFISKPENN 340
Cdd:cd13582 305 DGIAITKSCKDPERAFKFLDWLASEEAQ 332
|
|
| PBP2_Fbp_like_1 |
cd13544 |
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
142-361 |
1.44e-03 |
|
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270262 [Multi-domain] Cd Length: 292 Bit Score: 40.28 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 142 FKD-------VYLIPDAFMggalfIRTDWMKEANLEMPKTWDELfnvaeklTDPAknrygfsYRGaragfdQILAyifsv 214
Cdd:cd13544 86 FKDpdgywtgIYLGPLGFG-----VNTDELKEKGLPVPKSWEDL-------LNPE-------YKG------EIVM----- 135
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 215 tkgesyeADGTSvllrpeALTAFKRYTDIY-----KKGWAPKDSINwgyqEMVQGFT-SGVTGI-LAQTTEVVA------ 281
Cdd:cd13544 136 -------PNPAS------SGTAYTFLASLIqlmgeDEAWEYLKKLN----KNVGQYTkSGSAPAkLVASGEAAIgisflh 198
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690615523 282 TAKDSMKDGtwtvipNPHAVdgnTYAGAGASW---GYSISKNSKNKEAAWKFIEFISKPENNNKYSKVMTM-IPIMQDSL 357
Cdd:cd13544 199 DALKLKEQG------YPIKI---IFPKEGTGYeieAVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYaIPTNPDAK 269
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....
gi 690615523 358 KDPE 361
Cdd:cd13544 270 PPEI 273
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