|
Name |
Accession |
Description |
Interval |
E-value |
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
1-275 |
4.12e-104 |
|
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];
Pssm-ID: 441073 [Multi-domain] Cd Length: 270 Bit Score: 304.34 E-value: 4.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 1 MKKLISLFLSVSVVL-LAACGKQQNEPQNGKDsaqlQTVVI-ASTGSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMN 78
Cdd:COG1464 1 MKKLLALLLALALALaLAACGSSSAAAAAADK----KTIKVgATPGPHAEILEVVK--PELAKKGIDLEIVEFTDYVQPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 79 TATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLEPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAG 158
Cdd:COG1464 75 EALADGEIDANYFQHIPYLDNFNKENGYDLVPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 159 LIKLKADFDpAKGTPSDITDNSKKIDIKPIQMATAVRVKDEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDqstKLNVNIL 238
Cdd:COG1464 155 LIKLKDGVG-LLATVKDITENPKNLKFVELDAAQLPRSLDDVDAAVINGNYALEAGLDPTKDALFLEDKD---SPYANII 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 2072809689 239 ATAESRKDDPVLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:COG1464 231 VVREDDKDDPAIKKLVEAYQSDEVKKFIEEKYKGAVV 267
|
|
| PBP2_lipoprotein_GmpC |
cd13596 |
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; ... |
37-268 |
9.91e-90 |
|
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; contains the type 2 periplasmic-binding protein fold; This group includes the membrane-associated lipoprotein-9 from Staphylococcus aureus that binds the dipeptide glycylmethionine (GlyMet). The lipoprotein-9 has both structural and sequential homology to the MetQ family of substrate-binding protein. The GlyMet binding protein belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270314 Cd Length: 230 Bit Score: 266.15 E-value: 9.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 37 TVVIASTGSDADIWRYIATLPETkaAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYL 116
Cdd:cd13596 1 TVKIGVTGEDTDIWDKIVEEAEE--AGIKLELVNFSDYSQPNKALNDGDIDLNAFQHYAYLVQYNSKNNADLTAIGDTVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 117 EPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFDPAKgTPSDITDNSKKIDIKPIQMATAVRV 196
Cdd:cd13596 79 APMGIYSKKITSVDELPDGAKIAIPNDPSNLSRALFILQAAGLIKLKKDAGDFP-TVNDITENPKNLEIVPVDADQVYRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2072809689 197 KDEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDQST-KLNVNILATAESRKDDPVLQKVGQLYHTEAVKKYVEQ 268
Cdd:cd13596 158 LNDVDAAVINNTFALDAGLDPKKDAIFLEDPSSYGsKPYINLIAVREEDKDNPLYKKLVETYHDERVQKAVEE 230
|
|
| Lipoprotein_9 |
pfam03180 |
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ... |
38-275 |
1.23e-75 |
|
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. It contains several antigenic members, that may be involved in bacterial virulence. This entry includes the D-methionine binding lipoprotein MetQ, which is the substrate-binding component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. Other members of this family, such as NlpA, have been identified as putative substrate-binding components of ABC transporters. NlpA, is an inner-membrane-anchored lipoprotein that has been shown to have a minor role in methionine import.
Pssm-ID: 427184 Cd Length: 236 Bit Score: 230.61 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 38 VVIASTGSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLE 117
Cdd:pfam03180 2 KVGATPGPHAEILEVAK--PLLKKKGLDLEIVEFTDYVQPNTALADGEIDANYFQHLPYLDQFNKEKGLDLVAVGNVHIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 118 PMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFdPAKGTPSDITDNSKKIDIKPIQMATAVRVK 197
Cdd:pfam03180 80 PMGLYSKKYKSLSELPDGATIAVPNDPSNEGRALLLLQKAGLIKLKDGK-GLLATVKDITENPKNLKIKELEAAQLPRAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2072809689 198 DEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDQSTklnVNILATAESRKDDPVLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:pfam03180 159 DDVDAAVINTNYALEAGLNPKKDALFEEDKDSPY---VNIIVVREDDKDDEAVKKLVEAYQSEEVKKFIEKKYGGAVI 233
|
|
| PRK09861 |
PRK09861 |
lipoprotein NlpA; |
14-275 |
2.25e-40 |
|
lipoprotein NlpA;
Pssm-ID: 182119 Cd Length: 272 Bit Score: 141.31 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 14 VLLAACGkqqnepQNGKDSAQLQTVVIasTGSDADIWRYIATLPETKAaGLKLEVKNFTDYVAMNTATANKEVDLNAFQS 93
Cdd:PRK09861 19 ILLAGCD------QSSSDAKHIKVGVI--NGAEQDVAEVAKKVAKEKY-GLDVELVGFSGSLLPNDATNHGELDANVFQH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 94 YAYLVAFNASNKDKIAPVATTYLEPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADfdpaKG-- 171
Cdd:PRK09861 90 RPFLEQDNQAHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEG----KGll 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 172 -TPSDITDNSKKIDIKPIQMATAVRVKDE--VDAIVLGNTLAMEGGLNVLKDSIYYEpvDQSTKLnVNILATAESRKDDP 248
Cdd:PRK09861 166 pTALDITDNPRHLQIMELEGAQLPRVLDDpkVDVAIISTTYIQQTGLSPVHDSVFIE--DKNSPY-VNILVAREDNKNAE 242
|
250 260
....*....|....*....|....*..
gi 2072809689 249 VLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:PRK09861 243 NVKEFLQSYQSPEVAKAAETIFNGGAV 269
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
1-275 |
4.12e-104 |
|
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];
Pssm-ID: 441073 [Multi-domain] Cd Length: 270 Bit Score: 304.34 E-value: 4.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 1 MKKLISLFLSVSVVL-LAACGKQQNEPQNGKDsaqlQTVVI-ASTGSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMN 78
Cdd:COG1464 1 MKKLLALLLALALALaLAACGSSSAAAAAADK----KTIKVgATPGPHAEILEVVK--PELAKKGIDLEIVEFTDYVQPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 79 TATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLEPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAG 158
Cdd:COG1464 75 EALADGEIDANYFQHIPYLDNFNKENGYDLVPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 159 LIKLKADFDpAKGTPSDITDNSKKIDIKPIQMATAVRVKDEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDqstKLNVNIL 238
Cdd:COG1464 155 LIKLKDGVG-LLATVKDITENPKNLKFVELDAAQLPRSLDDVDAAVINGNYALEAGLDPTKDALFLEDKD---SPYANII 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 2072809689 239 ATAESRKDDPVLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:COG1464 231 VVREDDKDDPAIKKLVEAYQSDEVKKFIEEKYKGAVV 267
|
|
| PBP2_lipoprotein_GmpC |
cd13596 |
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; ... |
37-268 |
9.91e-90 |
|
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; contains the type 2 periplasmic-binding protein fold; This group includes the membrane-associated lipoprotein-9 from Staphylococcus aureus that binds the dipeptide glycylmethionine (GlyMet). The lipoprotein-9 has both structural and sequential homology to the MetQ family of substrate-binding protein. The GlyMet binding protein belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270314 Cd Length: 230 Bit Score: 266.15 E-value: 9.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 37 TVVIASTGSDADIWRYIATLPETkaAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYL 116
Cdd:cd13596 1 TVKIGVTGEDTDIWDKIVEEAEE--AGIKLELVNFSDYSQPNKALNDGDIDLNAFQHYAYLVQYNSKNNADLTAIGDTVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 117 EPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFDPAKgTPSDITDNSKKIDIKPIQMATAVRV 196
Cdd:cd13596 79 APMGIYSKKITSVDELPDGAKIAIPNDPSNLSRALFILQAAGLIKLKKDAGDFP-TVNDITENPKNLEIVPVDADQVYRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2072809689 197 KDEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDQST-KLNVNILATAESRKDDPVLQKVGQLYHTEAVKKYVEQ 268
Cdd:cd13596 158 LNDVDAAVINNTFALDAGLDPKKDAIFLEDPSSYGsKPYINLIAVREEDKDNPLYKKLVETYHDERVQKAVEE 230
|
|
| Lipoprotein_9 |
pfam03180 |
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ... |
38-275 |
1.23e-75 |
|
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. It contains several antigenic members, that may be involved in bacterial virulence. This entry includes the D-methionine binding lipoprotein MetQ, which is the substrate-binding component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. Other members of this family, such as NlpA, have been identified as putative substrate-binding components of ABC transporters. NlpA, is an inner-membrane-anchored lipoprotein that has been shown to have a minor role in methionine import.
Pssm-ID: 427184 Cd Length: 236 Bit Score: 230.61 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 38 VVIASTGSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLE 117
Cdd:pfam03180 2 KVGATPGPHAEILEVAK--PLLKKKGLDLEIVEFTDYVQPNTALADGEIDANYFQHLPYLDQFNKEKGLDLVAVGNVHIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 118 PMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFdPAKGTPSDITDNSKKIDIKPIQMATAVRVK 197
Cdd:pfam03180 80 PMGLYSKKYKSLSELPDGATIAVPNDPSNEGRALLLLQKAGLIKLKDGK-GLLATVKDITENPKNLKIKELEAAQLPRAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2072809689 198 DEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDQSTklnVNILATAESRKDDPVLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:pfam03180 159 DDVDAAVINTNYALEAGLNPKKDALFEEDKDSPY---VNIIVVREDDKDDEAVKKLVEAYQSEEVKKFIEKKYGGAVI 233
|
|
| PBP2_lipoprotein_Tp32 |
cd13597 |
The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum ... |
38-275 |
8.83e-71 |
|
The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum binds L-methionine; the type 2 periplasmic-binding protein fold; This group includes the lipoprotein Tp32, a periplasmic component of a methionine uptake transporter system, and its closely related homologs. The Tp32 has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus it belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270315 Cd Length: 236 Bit Score: 218.30 E-value: 8.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 38 VVIASTGSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLE 117
Cdd:cd13597 3 KVGATPVPHAEILEFIK--PELKKQGIDLEIVEFTDYVQPNTALADGELDANYFQHVPYLESFNKEKGYDLVAVAGVHLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 118 PMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFDPAkGTPSDITDNSKKIDIKPIQMATAVRVK 197
Cdd:cd13597 81 PMGLYSKKYKSLEDLPDGATIAIPNDPTNQGRALLLLEEAGLITLKDGAGLT-ATVKDIVKNPKNLKFKELEAAQLPRSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2072809689 198 DEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDQSTklNVNILATAESRKDDPVLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:cd13597 160 DDVDAAVINGNYALEAGLNPKKDALALEDKDNSP--YANILVVRKGNEDDPRIKKLAKALQSDEVKDFIEEKYDGAVV 235
|
|
| PBP2_lipoprotein_MetQ_like |
cd13526 |
The periplasmic-binding component of ABC-type methionine uptake transporter system and its ... |
37-268 |
2.20e-70 |
|
The periplasmic-binding component of ABC-type methionine uptake transporter system and its related lipoproteins; the type 2 periplasmic-binding protein fold; This family represents the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ) and its related homologs. Members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270244 Cd Length: 228 Bit Score: 216.80 E-value: 2.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 37 TVVIAST-GSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTY 115
Cdd:cd13526 1 KLKIGVTaGPSADVVEAAK--KEAKKKGYELELVVFTDYVAPNEALNDGSIDANFFQHVPFLDQFNKERNGDLVKVGKTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 116 LEPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFDPaKGTPSDITDNSKKIDIKPIQMATAVR 195
Cdd:cd13526 79 IAPIGLYSKKYKSLDELPDGARIAIPNDPSNGARALLLLEDAGLIKLKDGVGL-FATVLDITENPKNLEIVEVDAAQLPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2072809689 196 VKDEVDAIVLGNTLAMEGGLNVLKDSIYYEPVDQstKLNVNILATAESRKDDPVLQKVGQLYHTEAVKKYVEQ 268
Cdd:cd13526 158 SLDDVDAAVINGNYAISAGLDPRKDAIFLEDSDA--SPYVNVLAVREDNKDDPWVKALVEAYQSEEVRKFLKE 228
|
|
| PBP2_lipoprotein_IlpA_like |
cd13598 |
Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar ... |
43-267 |
3.25e-54 |
|
Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar lipoproteins; the type 2 periplasmic binding protein fold; This group includes the IlpA protein which has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270316 Cd Length: 227 Bit Score: 175.62 E-value: 3.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 43 TGSDADIWRYIATLpeTKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLEPMGIY 122
Cdd:cd13598 8 RGPDAQIWEVVQKV--AKEKGLDVELVTFNDYAQPNEALAAGDLDANAFQHKPYLDAQIKARGYKLVIVGNTFVYPIGLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 123 SSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFDpAKGTPSDITDNSKKIDIKPIQMATAVRVKDEVDA 202
Cdd:cd13598 86 SKKIKSLAELPNGATVAIPNDPSNEGRALLLLQKEGLIKLKDGVG-LLATVRDIAENPKKLKIVELDAGQLPRALDDVDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2072809689 203 IVLGNTLAMEGGLNVLKDSIYYEPVDQStklNVNILATAESRKDDPVLQKVGQLYHTEAVKKYVE 267
Cdd:cd13598 165 AAINTDYASKAGLTPARDAIAQEDKRSP---YANVIAVREDDKDAPWVKTLVQAYQSEEVKAFAL 226
|
|
| PBP2_lipoprotein_Gna1946 |
cd13599 |
The membrane-associated lipoprotein Gna1946 from Neisseria meningitidis; the type 2 ... |
57-266 |
6.44e-48 |
|
The membrane-associated lipoprotein Gna1946 from Neisseria meningitidis; the type 2 periplasmic binding protein fold; Gna1946 shares significant structural and sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270317 Cd Length: 228 Bit Score: 159.48 E-value: 6.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 57 PETKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLEPMGIYSSKYKKVDEFPQGA 136
Cdd:cd13599 21 PYLEKKGYEVKLKEFTDYVQPNNALANGEIDANVFQHKPYLDAFNKENGLDLVGIVQVPTPPMGLYSNKHKSLEEVKDGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 137 SIAIPNDAANEARALLLLQSAGLIKLKADFDPAKGTPSDITDNSKKIDIKPIQMATAVRVKDEVDAIVLGNTLAMEGGLN 216
Cdd:cd13599 101 TVAIPNDPSNLARALVMLQDLGWITLKDNIDPLKASVNDIAENPKNIKIVELEAAQLPRSLDDVDFAAIQGNFAISSGIK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2072809689 217 vLKDSIYYEpvdQSTKLNVNILATAESRKDDPVLQKVGQLYHTEAVKKYV 266
Cdd:cd13599 181 -LTSALALE---EMTDPYVNVVAVKTADKDKQFAKDVTAAYNSDAFKAYI 226
|
|
| PBP2_lipoprotein_like_1 |
cd13600 |
Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; ... |
39-267 |
4.68e-43 |
|
Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; the type 2 periplasmic binding protein fold; This subgroup shares significant sequence homology with the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ). The members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically 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.
Pssm-ID: 270318 Cd Length: 228 Bit Score: 146.71 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 39 VIASTGSDADIWRYIAtlPETKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLEP 118
Cdd:cd13600 4 VATNSGPMTEILEYIA--AELAPDGITIEPVQVSDYVQANRAVAAGEIDANFFQHQPFMEQFNEANGFELVAVQPIYHWA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 119 MGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADFDPAKGTPSDITDNSKKIDIKPIQMATAVRVKD 198
Cdd:cd13600 82 FGFYSKKYKSVEDLPDGAKVAIPNDPANQARALLLLQRAGLITLKPGVDPTTATLADIVTNPKNLKFTEVDLLALPRALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072809689 199 EVDAiVLGNTLAMEGGLNVLKDSIYYEPVDqsTKLNVNILATAESRKDDPVLQKVGQLYHTEAVKKYVE 267
Cdd:cd13600 162 DVDL-AFGYPSYFDAAGLTPKDGILLEEPD--AKRFAIQLVAREDNKDSPKIKKLKEAFTDPRVRKFLE 227
|
|
| PRK09861 |
PRK09861 |
lipoprotein NlpA; |
14-275 |
2.25e-40 |
|
lipoprotein NlpA;
Pssm-ID: 182119 Cd Length: 272 Bit Score: 141.31 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 14 VLLAACGkqqnepQNGKDSAQLQTVVIasTGSDADIWRYIATLPETKAaGLKLEVKNFTDYVAMNTATANKEVDLNAFQS 93
Cdd:PRK09861 19 ILLAGCD------QSSSDAKHIKVGVI--NGAEQDVAEVAKKVAKEKY-GLDVELVGFSGSLLPNDATNHGELDANVFQH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 94 YAYLVAFNASNKDKIAPVATTYLEPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLIKLKADfdpaKG-- 171
Cdd:PRK09861 90 RPFLEQDNQAHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEG----KGll 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 172 -TPSDITDNSKKIDIKPIQMATAVRVKDE--VDAIVLGNTLAMEGGLNVLKDSIYYEpvDQSTKLnVNILATAESRKDDP 248
Cdd:PRK09861 166 pTALDITDNPRHLQIMELEGAQLPRVLDDpkVDVAIISTTYIQQTGLSPVHDSVFIE--DKNSPY-VNILVAREDNKNAE 242
|
250 260
....*....|....*....|....*..
gi 2072809689 249 VLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:PRK09861 243 NVKEFLQSYQSPEVAKAAETIFNGGAV 269
|
|
| metQ |
PRK11063 |
D-methionine ABC transporter substrate-binding protein MetQ; |
1-275 |
9.94e-34 |
|
D-methionine ABC transporter substrate-binding protein MetQ;
Pssm-ID: 182939 [Multi-domain] Cd Length: 271 Bit Score: 123.72 E-value: 9.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 1 MKKLISLFLSVSVVLLAACGKQQnepqngKDSAQLQTVVIAstGSDADIWRYIATLPETKAaGLKLEVKNFTDYVAMNTA 80
Cdd:PRK11063 5 FKTFAAVGALIGTLALVGCGQDE------KDPNHIKVGVIV--GAEQQVAEVAQKVAKEKY-GLDVELVTFNDYVLPNEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 81 TANKEVDLNAFQSYAYLVAFNASNKDKIAPVATTYLEPMGIYSSKYKKVDEFPQGASIAIPNDAANEARALLLLQSAGLI 160
Cdd:PRK11063 76 LSKGDIDANAFQHKPYLDQQIKDRGYKLVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 161 KLKADFDPAKgTPSDITDNSKKIDIKPIQMATAVRVKDE--VDAIVLGNTLAMEGGLNVLKDSIYYEPVDQSTklnVNIL 238
Cdd:PRK11063 156 KLKDGVGLLP-TVLDIVENPKNLKIVELEAPQLPRSLDDaqIALAVINTTYASQIGLTPAKDGIFVEDKDSPY---VNLI 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 2072809689 239 ATAESRKDDPVLQKVGQLYHTEAVKKYVEQHFGGTKV 275
Cdd:PRK11063 232 VAREDNKDAENVKKFVQAYQSDEVYEAANKVFNGGAV 268
|
|
| TauA |
COG0715 |
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ... |
60-221 |
8.92e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440479 [Multi-domain] Cd Length: 297 Bit Score: 52.31 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 60 KAAGLKLEVKNFTDYVAMNTATANKEVDLnAFQSYAYLVAFNASNKDKIAPVATTYLEPMGIYS---SKYKKVDEFpQGA 136
Cdd:COG0715 47 KKEGLDVELVEFAGGAAALEALAAGQADF-GVAGAPPALAARAKGAPVKAVAALSQSGGNALVVrkdSGIKSLADL-KGK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 137 SIAIPNDAANEARALLLLQSAGLiklkadfdpakgTPSDITdnskKIDIKPIQMATAVRvKDEVDAIVLGNT----LAME 212
Cdd:COG0715 125 KVAVPGGSTSHYLLRALLAKAGL------------DPKDVE----IVNLPPPDAVAALL-AGQVDAAVVWEPfesqAEKK 187
|
....*....
gi 2072809689 213 GGLNVLKDS 221
Cdd:COG0715 188 GGGRVLADS 196
|
|
| Periplasmic_Binding_Protein_Type_2 |
cd00648 |
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ... |
37-235 |
4.10e-04 |
|
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.
Pssm-ID: 270214 [Multi-domain] Cd Length: 196 Bit Score: 40.63 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 37 TVVIASTGSDADIWRYIATLPE-TKAAGLKLEVKNFTDYVAMNTATANKEVDLNAFQS-YAYLVAFNASNKDKIAPVATT 114
Cdd:cd00648 1 TLTVASIGPPPYAGFAEDAAKQlAKETGIKVELVPGSSIGTLIEALAAGDADVAVGPIaPALEAAADKLAPGGLYIVPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072809689 115 YLEPMGIYSSKYKKV-----DEFPQGASIAIPNDAA-NEARALLLLQSAGLIKLKADFDPAKGTpsditdnskkidikpI 188
Cdd:cd00648 81 YVGGYVLVVRKGSSIkgllaVADLDGKRVGVGDPGStAVRQARLALGAYGLKKKDPEVVPVPGT---------------S 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2072809689 189 QMATAVrVKDEVDAIVLGNTLAMEGGLNVLKdsiyYEPVDQSTKLNV 235
Cdd:cd00648 146 GALAAV-ANGAVDAAIVWVPAAERAQLGNVQ----LEVLPDDLGPLV 187
|
|
| |
