|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
72-445 |
1.14e-81 |
|
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: 256.95 E-value: 1.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 72 KQFFEENNAAFESEY-GVDVEFTSVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDGEFGEK-FA 149
Cdd:cd13585 13 TAALKKLIDAFEKENpGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKDGLDDdFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 150 EGVANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGLDPENPAldTWEDMLAAAKALTESDEVSVpalGLAGADAIETGS 229
Cdd:cd13585 93 PGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPW--TWDELLEAAKKLTDKKGGQY---GFALRGGSGGQT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 230 QYYHYHWSHGADLVD-DEGMPVVNSDGAVEALSFYADLHLEHGVTQSSplSSTRQDIRQLFENGDLGMVIGHVYTGLNIT 308
Cdd:cd13585 168 QWYPFLWSNGGDLLDeDDGKATLNSPEAVEALQFYVDLYKDGVAPSSA--TTGGDEAVDLFASGKVAMMIDGPWALGTLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 309 ESqengEVDFDYGIVQVPKGPAG-RYSLFTIDTLGIFSQSEHKDIARDLIRFYFDEE--RRFQYSKQKGFLPVVEAVGER 385
Cdd:cd13585 246 DS----KVKFKWGVAPLPAGPGGkRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKEnqLKLGGAAGPAALAAAAASAAA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895616407 386 EYFSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQ--KSPQKALNDAQSDL 445
Cdd:cd13585 322 PDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEAAKEI 383
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
17-450 |
8.03e-74 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 236.09 E-value: 8.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 17 RRLLQALGAGGMIAVAGCTGGGDGSESGsdgegsgeggddTQSVQLLTMGVGDNIKQFFEENNAAFESEY-GVDVEFTSV 95
Cdd:COG1653 2 RRLALALAAALALALAACGGGGSGAAAA------------AGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 96 TWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMD--GEFGEKFAEGVANGTMYNGSHYGVPWAASNKC 173
Cdd:COG1653 70 PYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDddGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 174 LYYNKDAFEAAGLDPenPAldTWEDMLAAAKALTESDEVSvpALGLAGADaietGSQYYHYHWSHGADLVDDEGMPVVNS 253
Cdd:COG1653 150 LYYNKDLFEKAGLDP--PK--TWDELLAAAKKLKAKDGVY--GFALGGKD----GAAWLDLLLSAGGDLYDEDGKPAFDS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 254 DGAVEALSFYADLhLEHGVTQSSPLSSTRQDIRQLFENGDLGMVIghvyTGLNITESQENGEVDFDYGIVQVPKGPAG-- 331
Cdd:COG1653 220 PEAVEALEFLKDL-VKDGYVPPGALGTDWDDARAAFASGKAAMMI----NGSWALGALKDAAPDFDVGVAPLPGGPGGkk 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 332 RYSLFTIDTLGIFSQSEHKDIARDLIRFYFDEErrfqyskqkgflpvveavgereyfsesknwgpfveagqyararpkls 411
Cdd:COG1653 295 PASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPE----------------------------------------------- 327
|
410 420 430
....*....|....*....|....*....|....*....
gi 1895616407 412 nfsqfNDRMVQAIQEALADQKSPQKALNDAQSDLEDAMN 450
Cdd:COG1653 328 -----AQAKWDALQAVLLGQKTPEEALDAAQAAANAALA 361
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
16-450 |
2.64e-69 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 225.60 E-value: 2.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 16 RRRLLQALGAGGMIA--VAGCTGGGDGSESGSDGEGSGEggddtqsvqlLTMGVGDNIKQFFEENNAAFESEYGVDVEFT 93
Cdd:COG2182 2 KRRLLAALALALALAlaLAACGSGSSSSGSSSAAGAGGT----------LTVWVDDDEAEALEEAAAAFEEEPGIKVKVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 94 SVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDlmDGEFGEKFAEGVANGTMYNGSHYGVPWAASNKC 173
Cdd:COG2182 72 EVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDD--DLADKDDFLPAALDAVTYDGKLYGVPYAVETLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 174 LYYNKDAFEAagldpENPAldTWEDMLAAAKALTESDEVSVpalglagadAIETGSQYYHY--HWSHGADLV----DDEG 247
Cdd:COG2182 150 LYYNKDLVKA-----EPPK--TWDELIAAAKKLTAAGKYGL---------AYDAGDAYYFYpfLAAFGGYLFgkdgDDPK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 248 MPVVNSDGAVEALSFYADLhLEHGVtqsSPLSSTRQDIRQLFENGDLGMVIGHVYTGLNITESqengeVDFDYGIVQVPK 327
Cdd:COG2182 214 DVGLNSPGAVAALEYLKDL-IKDGV---LPADADYDAADALFAEGKAAMIINGPWAAADLKKA-----LGIDYGVAPLPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 328 GPAGR--YSLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVVEAVGEREYFSESKNWGPFVEAGQYAR 405
Cdd:COG2182 285 LAGGKpaKPFVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAV 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1895616407 406 ARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQSDLEDAMN 450
Cdd:COG2182 365 PMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAAIA 409
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
66-445 |
1.76e-68 |
|
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: 222.94 E-value: 1.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 66 GVGDNIKQFFEENNAAF-ESEYGVDVEFTSVTWDN-ARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDGE 143
Cdd:cd14748 7 GMSGPDGKALEELVDEFnKSHPDIKVKAVYQGSYDdTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 144 FGEK--FAEGVANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGLDPENPAlDTWEDMLAAAKALT-ESDEVSVPALGLA 220
Cdd:cd14748 87 GVDDddFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPP-KTWDELEEAAKKLKdKGGKTGRYGFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 221 GADaieTGSQYYHYHWSHGADLVDDE-GMPVVNSDGAVEALSFYADLHLEHGVTQssplSSTRQDIRQLFENGDLGMVIg 299
Cdd:cd14748 166 PGD---GGWTFQALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGKDGVSP----LNDWGDAQDAFISGKVAMTI- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 300 hvyTGLNITESQENGEVDFDYGIVQVPKGPAGRYSLFT-IDTLGIFSQ-SEHKDIARDLIRFYFDEERRFQYSKQKGFLP 377
Cdd:cd14748 238 ---NGTWSLAGIRDKGAGFEYGVAPLPAGKGKKGATPAgGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895616407 378 VVEAVGE--REYFSESKNWGPFVEAGQYARAR-PKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQSDL 445
Cdd:cd14748 315 VRKSAAEdpEEFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
65-450 |
4.45e-59 |
|
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: 198.31 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 65 MGVGDNIKqFFEENNAAFESEY-GVDVEFTSVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDGE 143
Cdd:cd14747 7 MGNSAEAE-LLKELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLEDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 144 FGEK-FAEGVANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGLDpENPAldTWEDMLAAAKALTESDEvSVPALGLAG- 221
Cdd:cd14747 86 GGDKdLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGD-EAPK--TWDELEAAAKKIKADGP-DVSGFAIPGk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 222 ADAIETGSQYYhyhWSHGADLV-DDEGMPVVNSDGAVEALSFYADLHLEHGVTQSSPLSSTrqDIRQLFENGDLGMVIGH 300
Cdd:cd14747 162 NDVWHNALPFV---WGAGGDLAtKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSA--DVEQAFANGKVAMIISG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 301 VYTGLNITEsqENGEVDFDYGIVQVPKGPAG-RYSLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVV 379
Cdd:cd14747 237 PWEIGAIRE--AGPDLAGKWGVAPLPGGPGGgSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPAN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895616407 380 EAVGEREYFSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEA-LADQKSPQKALNDAQSDLEDAMN 450
Cdd:cd14747 315 TSAWDDPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVwIGVGADVEDALDKAAAEINEILN 386
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
72-441 |
4.01e-50 |
|
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: 174.49 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 72 KQFFEENNAAFESEY-GVDVEFTSVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDGEFGEKFAE 150
Cdd:cd14751 13 KVLYEKLIPAFEKEYpKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDIVDYLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 151 GVANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGLDPenPAldTWEDMLAAAKALTESDEVSvpALGLAGADAietgsq 230
Cdd:cd14751 93 GPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEV--PK--TMDELVAAAKAIKKKKGRY--GLYISGDGP------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 231 YYH--YHWSHGADLVDDEGMPV-VNSDGAVEALSFYADLHLEHGVTqsSPLSSTRQDIRQLFENGDLGMVIGHVYTGLNI 307
Cdd:cd14751 161 YWLlpFLWSFGGDLTDEKKATGyLNSPESVRALETIVDLYDEGAIT--PCASGGYPNMQDGFKSGRYAMIVNGPWAYADI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 308 TESQENgEVDFDYGIVQVPKGPAGRYSLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVVEAVGEREY 387
Cdd:cd14751 239 LGGKEF-KDPDNLGIAPVPAGPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESPE 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1895616407 388 FSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDA 441
Cdd:cd14751 318 VANNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
68-446 |
5.80e-49 |
|
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: 171.79 E-value: 5.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 68 GDNIKQFFEENNAAFESEY-GVDVEFTSVTWDNARQTVNNRVDGGQAPDV-SRWPARWIPQLVGKDALEPVDDLMD-GEF 144
Cdd:cd14749 10 GDTKKKYMDELIADFEKENpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVfNLWPGGWLAEFVKAGLLLPLTDYLDpNGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 145 GEKFAEGVANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGLDpENPAldTWEDMLAAAKALTESDEVSVPaLGLAGADA 224
Cdd:cd14749 90 DKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGV-KPPK--TWDELIEAAKKDKFKAKGQTG-FGLLLGAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 225 iETGSQYYHYHWSHGADLV-DDEGMPV-VNSDGAVEALSFYADLhLEHGVTQSSPLSSTRQDIRQLFENGDLGMVIGhvy 302
Cdd:cd14749 166 -GGHWYFQYLVRQAGGGPLsDDGSGKAtFNDPAFVQALQKLQDL-VKAGAFQEGFEGIDYDDAGQAFAQGKAAMNIG--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 303 tGLNITESQENGEVDFDYGIVQVPKGPAG---RYSLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVV 379
Cdd:cd14749 241 -GSWDLGAIKAGEPGGKIGVFPFPTVGKGaqtSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1895616407 380 EAVGEREYFSESKNWGPFVEAGQYARARPKLSNF-SQFNDRMVQAIQEALADQKSPQKALNDAQSDLE 446
Cdd:cd14749 320 EVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEYwPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAA 387
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
80-445 |
9.82e-44 |
|
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: 157.46 E-value: 9.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 80 AAFESEYG---VDVEFTSVTWDNARQTVNNRVDGG-QAPDV----SRWPARWIPQLVgkdaLEPVDDLMDGEFGEKFAEG 151
Cdd:cd14750 21 AAFEKKHPdikVEIEELPASSDDQRQQLVTALAAGsSAPDVlgldVIWIPEFAEAGW----LLPLTEYLKEEEDDDFLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 152 VANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGLDPenPAldTWEDMLAAAKALTESDEVSVPALGlagadaieTGSQY 231
Cdd:cd14750 97 TVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEP--PK--TWDELLEAAKKRKAGEPGIWGYVF--------QGKQY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 232 YH-------YHWSHGADLVDDE-GMPVVNSDGAVEALSFYADLhLEHGVTQSSPLSSTRQDIRQLFENGDLGMVIG--HV 301
Cdd:cd14750 165 EGlvcnfleLLWSNGGDIFDDDsGKVTVDSPEALEALQFLRDL-IGEGISPKGVLTYGEEEARAAFQAGKAAFMRNwpYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 302 YTGLNITESQENGEVdfdyGIVQVPKGPAGRY-SLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVVE 380
Cdd:cd14750 244 YALLQGPESAVAGKV----GVAPLPAGPGGGSaSTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLPPTRR 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895616407 381 AVG-EREYFSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQSDL 445
Cdd:cd14750 320 ALYdDPEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEKL 385
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
72-442 |
3.72e-42 |
|
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: 152.83 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 72 KQFFEENNAAFESEYGVDVEFTSVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDGEFgeKFAEG 151
Cdd:cd13586 12 LEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKI--KNLPV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 152 VANGTMYNGSHYGVPWAASNKCLYYNKDafeaagLDPENPAldTWEDMLAAAKALTESDEVSVpalGLAgadaIETGSQY 231
Cdd:cd13586 90 ALAAVTYNGKLYGVPVSVETIALFYNKD------LVPEPPK--TWEELIALAKKFNDKAGGKY---GFA----YDQTNPY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 232 YHYHW--SHGADLVDDEGMPV----VNSDGAVEALSFYADLHLEHGVTqssPLSSTRQDIRQLFENGDLGMVIghvyTGL 305
Cdd:cd13586 155 FSYPFlaAFGGYVFGENGGDPtdigLNNEGAVKGLKFIKDLKKKYKVL---PPDLDYDIADALFKEGKAAMII----NGP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 306 -NITESQENGevdFDYGIVQVPKGPAGRYSLFTIDTLGIF--SQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPV---- 378
Cdd:cd13586 228 wDLADYKDAG---INFGVAPLPTLPGGKQAAPFVGVQGAFvsAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPAlkda 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895616407 379 --VEAVGEREYFSesknwgPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQ 442
Cdd:cd13586 305 lnDAAVKNDPLVK------AFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAV 364
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
73-364 |
2.33e-33 |
|
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: 127.15 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 73 QFFEENNAAFESEY-GVDVEFTSVTWDNARQTVNNRVDGGQAP-DVSRWPARWIPQLVGKDALEPVDDLMDGEFGEKfae 150
Cdd:pfam01547 8 AALQALVKEFEKEHpGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLG--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 151 gvangtmyNGSHYGVPWAASNKCLYYNKDAFEAAGLDPEnpalDTWEDMLAAAKALTESDEVSVPALGLAGADaiETGSQ 230
Cdd:pfam01547 85 --------VPKLYGVPLAAETLGLIYNKDLFKKAGLDPP----KTWDELLEAAKKLKEKGKSPGGAGGGDASG--TLGYF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 231 YYHYHWSHGADLVDDEGMpVVNSDGAVEALSFYADL----HLEHGVTQSSPLSSTRQDIRQLFENGDLGMVIGHVYTGLN 306
Cdd:pfam01547 151 TLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLyakvLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895616407 307 ITESQENGEVDFD----YGIVQVPKGPAGRYSLFTIDTLGIFSQSEHKDIARDLIRFYFDEE 364
Cdd:pfam01547 230 ANKVKLKVAFAAPapdpKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
64-442 |
2.03e-30 |
|
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: 120.98 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 64 TMGVGDNikQFFEENNAAFESEY-GVDVEFTSVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDg 142
Cdd:cd13522 7 QYDTGEN--QAVNELIAKFEKAYpGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 143 eFGEKFAEGVANGTMYNGSHYGVPWAASNKCLYYNKDAFeaagldPENPAlDTWEDMLAAAKALTESDeVSVPALGLAGA 222
Cdd:cd13522 84 -KSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPP-KTWQELIALAQGLKAKN-VWGLVYNQNEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 223 daietgsqYYHYHW--SHGADLVDDEGM---PVVNSDGAVEALSFYADLHLEHGVTqssPLSSTRQDIRQLFENGDLGMV 297
Cdd:cd13522 155 --------YFFAAWigGFGGQVFKANNGknnPTLDTPGAVEALQFLVDLKSKYKIM---PPETDYSIADALFKAGKAAMI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 298 IGHVYTgLNITESQENGevdfDYGIVQVPKGPAGRYSLFTIDTLGIF--SQSEHKDIARDLIRFYFDEERRFQYSKQKGF 375
Cdd:cd13522 224 INGPWD-LGDYRQALKI----NLGVAPLPTFSGTKHAAPFVGGKGFGinKESQNKAAAVEFVKYLTSYQAQLVLFDDAGD 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895616407 376 LPVVEAVGEREYFSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQ 442
Cdd:cd13522 299 IPANLQAYESPAVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQ 365
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
80-390 |
2.43e-30 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 118.66 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 80 AAFESEYGVDVEFTSVTWDNARQTVNNRVDGGQAPDVSRW--PARWIPQLVGKDALEPVDDLMDGefgeKFAEGVANGTM 157
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVwiAADQLATLAEAGLLADLSDVDNL----DDLPDALDAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 158 YNGSHYGVPWAASNK-CLYYNKDAFEAAGLDPenpalDTWEDMLAAAKALTesdevsvpalglaGADAIET-GSQYYH-Y 234
Cdd:pfam13416 80 YDGKLYGVPYAASTPtVLYYNKDLLKKAGEDP-----KTWDELLAAAAKLK-------------GKTGLTDpATGWLLwA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 235 HWSHGADLVDDEGMPvvnsDGAVEALSFYADLhlehgvTQSSPLSSTRQDIRQLFENGDLGMVIGhvYTGlNITESQENG 314
Cdd:pfam13416 142 LLADGVDLTDDGKGV----EALDEALAYLKKL------KDNGKVYNTGADAVQLFANGEVAMTVN--GTW-AAAAAKKAG 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895616407 315 evdFDYGIVqVPKGpagrYSLFTIDTLGIFSQSEHKDI-ARDLIRFYFDEERRFQYSKQKGFLPVVEAVGEREYFSE 390
Cdd:pfam13416 209 ---KKLGAV-VPKD----GSFLGGKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKA 277
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
75-445 |
1.84e-26 |
|
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: 109.77 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 75 FEENNAAFESEYGVD-VEFTSVTWDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDDLMDGEFGEKFAEGVA 153
Cdd:cd13657 16 LQQIIDEFEAKYPVPnVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISDYLSEDDFENYLPTAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 154 NGTMYNGSHYGVPWAASNKCLYYNKDafeaagLDPENPAldTWEDMLAAAKALTESDEVSvpaLGLAGadaiETGSQYYH 233
Cdd:cd13657 96 EAVTYKGKVYGLPEAYETVALIYNKA------LVDQPPE--TTDELLAIMKDHTDPAAGS---YGLAY----QVSDAYFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 234 YHWSH--GADLVDDEGM-PVVNSDGAVEALSFYADLHLehGVTQSSPLSSTrqdIRQLFENGDLGMVIghvyTG-LNITE 309
Cdd:cd13657 161 SAWIFgfGGYYFDDETDkPGLDTPETIKGIQFLKDFSW--PYMPSDPSYNT---QTSLFNEGKAAMII----NGpWFIGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 310 SQENGevdFDYGIVQVPK----GPAGRYSlfTIDTLGI--FSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVVEAVG 383
Cdd:cd13657 232 IKAAG---IDLGVAPLPTvdgtNPPRPYS--GVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAY 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895616407 384 EREYFSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQSDL 445
Cdd:cd13657 307 DDAEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
63-447 |
2.07e-26 |
|
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: 109.88 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 63 LTMGV-GDNIKQFFEENNAAFESEYGVDVEFtsVTWDNARQTVNNRVDG--GQAPDVSRWPARWIPQLVGKDALEPVDDL 139
Cdd:cd13658 2 LTVWVdEDKKMAFIKKIAKQYTKKTGVKVKL--VEVDQLDQLEKLSLDGpaGKGPDVMVAPHDRIGSAVLQGLLSPIKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 140 MDGEFGekFAEGVANGTMYNGSHYGVPWAASNKCLYYNKDafeaagLDPENPalDTWEDMLAAAKALTESDEVSVPALgl 219
Cdd:cd13658 80 KDKKKG--FTDQALKALTYDGKLYGLPAAVETLALYYNKD------LVKNAP--KTFDELEALAKDLTKEKGKQYGFL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 220 agADAietGSQYYHYHW----------SHGADL-VDDEGMpvvNSDGAVEAL----SFYADLHLehgvtqssPLSSTRQD 284
Cdd:cd13658 148 --ADA---TNFYYSYGLlagnggyifkKNGSDLdINDIGL---NSPGAVKAVkflkKWYTEGYL--------PKGMTGDV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 285 IRQLFENGDLGMVIGHVYtglNITESQENGevdFDYGIVQVPKGPAGRYSLFTIDTLG--IFSQSEHKDIARDLIRFYFD 362
Cdd:cd13658 212 IQGLFKEGKAAAVIDGPW---AIQEYQEAG---VNYGVAPLPTLPNGKPMAPFLGVKGwyLSAYSKHKEWAQKFMEFLTS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 363 EERRFQYSKQKGFLPVVEAVGEREYFSESKNWGPFveAGQYARAR--PKLSNFSQFNDRMVQAIQEALADQKSPQKALND 440
Cdd:cd13658 286 KENLKKRYDETNEIPPRKDVRSDPEIKNNPLTSAF--AKQASRAVpmPNIPEMGAVWEPANNALFFILSGKKTPKQALND 363
|
....*..
gi 1895616407 441 AQSDLED 447
Cdd:cd13658 364 AVNDIKE 370
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
59-364 |
5.08e-19 |
|
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: 88.92 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 59 SVQLLTMGVGDNIKQFFEENNAA----FESEYGVDVEFTSVTWDNARQTVNNRVDGGQAPDVSR-WPARWIPQLVGKDAL 133
Cdd:cd13580 1 EPVTITIVANLGGNPKPDPDDNPytkyLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 134 EPVDDLMDgEFGEKFA-----EGVANGtMYNGSHYGVPWAASNK---CLYYNKDAFEAAGLDPenPAldTWEDMLAAAKA 205
Cdd:cd13580 81 WDLTDYLD-KYYPNLKkiieqEGWDSA-SVDGKIYGIPRKRPLIgrnGLWIRKDWLDKLGLEV--PK--TLDELYEVAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 206 LTESDevsvPAL-------GLAGADAIETGSQY--------YHYHWshgadLVDDEG--MPVVNSDGAVEALSFYADLHL 268
Cdd:cd13580 155 FTEKD----PDGngkkdtyGLTDTKDLIGSGFTglfgafgaPPNNW-----WKDEDGklVPGSIQPEMKEALKFLKKLYK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 269 EHGVTQSSPLSSTrQDIRQLFENGDLGMVIGHVYTGLNITESQENGEVDFDYGIVQVPKGPAGRYSLFTIDTLGIFS--- 345
Cdd:cd13580 226 EGLIDPEFAVNDG-TKANEKFISGKAGIFVGNWWDPAWPQASLKKNDPDAEWVAVPIPSGPDGKYGVWAESGVNGFFvip 304
|
330 340
....*....|....*....|
gi 1895616407 346 -QSEHKDIARDLIRFYFDEE 364
Cdd:cd13580 305 kKSKKPEAILKLLDFLSDPE 324
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
68-445 |
1.99e-11 |
|
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270374 [Multi-domain] Cd Length: 364 Bit Score: 65.31 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 68 GDNIKQFFEENNAAFESEYGVDVEFTSVtwDNARQTVNNRVDGGQAPDVSRWPARWIPQLVGKDALEPVDdlMDGEFGEK 147
Cdd:cd13656 9 GDKGYNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT--PDKAFQDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 148 FAEGVANGTMYNGSHYGVPWAASNKCLYYNKDafeaagLDPENPAldTWEDMLAAAKALTESDEVSV-----------PA 216
Cdd:cd13656 85 LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD------LLPNPPK--TWEEIPALDKELKAKGKSALmfnlqepyftwPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 217 LGLAGAdaietgsqyYHYHWSHGADLVDDEGmpvVNSDGAVEALSFYADLhLEHGVTqssPLSSTRQDIRQLFENGDLGM 296
Cdd:cd13656 157 IAADGG---------YAFKYENGKYDIKDVG---VDNAGAKAGLTFLVDL-IKNKHM---NADTDYSIAEAAFNKGETAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 297 VIGHVYTGLNITESQengevdFDYGIVQVP--KGPAGRySLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKG 374
Cdd:cd13656 221 TINGPWAWSNIDTSK------VNYGVTVLPtfKGQPSK-PFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1895616407 375 FLPVVEAVGEREYFSESKNWGPFVEAGQYARARPKLSNFSQFNDRMVQAIQEALADQKSPQKALNDAQSDL 445
Cdd:cd13656 294 PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
63-326 |
1.97e-09 |
|
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270373 [Multi-domain] Cd Length: 363 Bit Score: 58.90 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 63 LTMGVGDNIKQFFEENNAAFESEYG-VDVEFT--SVTWDNARQTVNNrvDGGQAPDVSRWPARWIPQLVGKDALEPVDDL 139
Cdd:cd13655 2 LTVWGPQEDQEWLKEMVDAFKEKHPeWKITITigVVGEADAKDEVLK--DPSAAADVFAFANDQLGELVDAGAIYPLTGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 140 MDGEFGEKFAEGVANGTMYNGSHYGVPWAASNKCLYYNKDAFEAAGldpenpaLDTWEDMLAAAKALTesdevsvpalgl 219
Cdd:cd13655 80 AVDKIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDD-------VKSLDTMLAKAPDAK------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 220 aGADAIETGSQYYHYHW--SHGADLVDDEGMPV----VNSDGAVEALSFYADLHLEHGVTQSSplsstRQDIRQLFENGD 293
Cdd:cd13655 141 -GKVSFDLSNSWYLYAFffGAGCKLFGNNGGDTagcdFNNEKGVAVTNYLVDLVANPKFVNDA-----DGDAISGLKDGT 214
|
250 260 270
....*....|....*....|....*....|...
gi 1895616407 294 LGMVIGHVYTGLNITESQENgevdfDYGIVQVP 326
Cdd:cd13655 215 LGAGVSGPWDAANLKKALGD-----NYAVAKLP 242
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
127-441 |
2.35e-09 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 59.04 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 127 LVGKDALEPVDDLMDgEFGEKFAEGVANGTM---YNGSHYG----VPWAASNKCLYYNKDAFEAAGLDPENPAlDTWEDM 199
Cdd:PRK10974 96 MMASKAIKPVYDVFK-DAGIPFDESQFVPTVagyYSDAKTGhllsQPFNSSTPVLYYNKDAFKKAGLDPEQPP-KTWQDL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 200 LAAAKALTESDEVSVPALGLAGADAIETGSQYYhyhwshgadlvddeGMPVVNS----DGAVEALSFYADLHLEH-GVTQ 274
Cdd:PRK10974 174 AAYAAKLRAAGMKCGYASGWQGWIQLENFSAWH--------------GLPFASKnngfDGTDAVLEFNKPEQVKHiALLE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 275 SSPLSST-----RQDIRQL-FENGDLGMVIGHVYTGLNITESQEngevdFDYGIVQVPKGPA----------GRYSLFTI 338
Cdd:PRK10974 240 EMNKKGDftyvgRKDESTEkFYNGDCAITTASSGSLANIRKYAK-----FNYGVGMMPYDADvkgapqnaiiGGASLWVM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 339 DTLgifSQSEHKDIARdLIRFYFDEERRFQYSKQKGFLPVVEAVGE--REYFSESKNWGPFVEAGQYARARP-------K 409
Cdd:PRK10974 315 QGK---DKETYKGVAK-FLDFLAKPENAAEWHQKTGYLPITTAAYDltREQGFYEKNPGADTATRQMLNKPPlpftkglR 390
|
330 340 350
....*....|....*....|....*....|..
gi 1895616407 410 LSNFSQFNDRMVQAIQEALADQKSPQKALNDA 441
Cdd:PRK10974 391 LGNMPQIRTIVDEELESVWTGKKTPQQALDSA 422
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
80-333 |
1.79e-08 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 56.60 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 80 AAFESEYGVDVEFTSV---TWDNARQTVnnrVDGGQAPDvsrwparWIP--------QLVGKDALEPVDDLMD-----GE 143
Cdd:cd13583 24 KEIEEKTNVKFKRTPIpssDYETKRSLL---IASGDAPD-------IIPvlypgeenEFVASGALLPISDYLDympnyKK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 144 FGEKFAEGV--ANGTMYNGSHYGVPWAASNK----CLYYNKDAFEAAGLDPENpaldTWEDMLAAAKALTESDEVSVP-- 215
Cdd:cd13583 94 YVEKWGLGKelATGRQSDGKYYSLPGLHEDPgvqySFLYRKDIFEKAGIKIPT----TWDEFYAALKKLKEKYPDSYPys 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 216 ------ALGLAGADAIET----GSQYYHYHWShgadlvDDEGMPVVNSDGAVEALSFYADLHLEhGVTQSSPLSSTRQDI 285
Cdd:cd13583 170 drwnsnALLLIAAPAFGTtagwGFSNYTYDPD------TDKFVYGATTDEYKDMLQYFNKLYAE-GLLDPESFTQTDDQA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1895616407 286 RQLFENGDlGMVIGhvYTGLNITESQENGEVDF--DYGIVQ--VPKGPAGRY 333
Cdd:cd13583 243 KAKFLNGK-SFVIT--TNPQTVDELQRNLRAADggNYEVVSitPPAGPAGKA 291
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
14-390 |
1.28e-07 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 53.38 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 14 LDRRRLLQALGAGGMIAVAGCTGGGDgsesgsdgegsgeggddtQSVQLLTMGVGDNI-KQFFEennaAFESEYGVDVEF 92
Cdd:COG0687 1 MSRRSLLGLAAAALAAALAGGAPAAA------------------AEGTLNVYNWGGYIdPDVLE----PFEKETGIKVVY 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 93 TsvTWDNARQTVNNRVDGGQAPDVSrWP-ARWIPQLVGKDALEPVD-------DLMDGEFgekfaegvANGTMYNGSHYG 164
Cdd:COG0687 59 D--TYDSNEEMLAKLRAGGSGYDVV-VPsDYFVARLIKAGLLQPLDksklpnlANLDPRF--------KDPPFDPGNVYG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 165 VPWAASNKCLYYNKDAFEAagldpenpALDTWEDMLAAAKA-----LTESDEVSVPALGLAGADAIETgsqyyhyhwshg 239
Cdd:COG0687 128 VPYTWGTTGIAYNTDKVKE--------PPTSWADLWDPEYKgkvalLDDPREVLGAALLYLGYDPNST------------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 240 adlvDDEGMpvvnsDGAVEAL--------SFYadlhlehgvtqssplsSTRQDIRQLFENGDLgmVIGHVYTGLNITESQ 311
Cdd:COG0687 188 ----DPADL-----DAAFELLielkpnvrAFW----------------SDGAEYIQLLASGEV--DLAVGWSGDALALRA 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895616407 312 ENGEVDFdygivQVPK-GpagrySLFTIDTLGIFSQSEHKDIARDLIRFYFDEERRFQYSKQKGFLPVVEAVgeREYFSE 390
Cdd:COG0687 241 EGPPIAY-----VIPKeG-----ALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAA--RELLPP 308
|
|
| |
