|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09861 |
PRK09861 |
lipoprotein NlpA; |
1-272 |
0e+00 |
|
lipoprotein NlpA;
Pssm-ID: 182119 Cd Length: 272 Bit Score: 588.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 1 MKLTTHHLRAGAALLLAGVLLAGCDQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNG 80
Cdd:PRK09861 1 MKLTTHHLRAGAALLLAGILLAGCDQSSSDAKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 81 ELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKE 160
Cdd:PRK09861 81 ELDANVFQHRPFLEQDNQAHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 161 GKGLLPTALDITDNPRHLQIMELEGAQLPRVLDDPKVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKN 240
Cdd:PRK09861 161 GKGLLPTALDITDNPRHLQIMELEGAQLPRVLDDPKVDVAIISTTYIQQTGLSPVHDSVFIEDKNSPYVNILVAREDNKN 240
|
250 260 270
....*....|....*....|....*....|..
gi 15833849 241 AENVKEFLQSYQSPEVAKAAETIFNGGAVPGW 272
Cdd:PRK09861 241 AENVKEFLQSYQSPEVAKAAETIFNGGAVPGW 272
|
|
| TIGR00363 |
TIGR00363 |
lipoprotein, YaeC family; This family of putative lipoproteins contains a consensus site for ... |
24-272 |
2.26e-165 |
|
lipoprotein, YaeC family; This family of putative lipoproteins contains a consensus site for lipoprotein signal sequence cleavage. Included in this family is the E. coli hypothetical protein yaeC. About half of the proteins between the noise and trusted cutoffs contain the consensus lipoprotein signature and may belong to this family. [Cell envelope, Other]
Pssm-ID: 129460 Cd Length: 258 Bit Score: 458.21 E-value: 2.26e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 24 CDQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYK 103
Cdd:TIGR00363 10 CKQDKKDPLHIKVGVISGAEQQVAEVAAKVAKEKYGLDVELVEFNDYALPNEAVSKGDLDANAFQHKPYLDQDAKAKGYK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 104 LVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMEL 183
Cdd:TIGR00363 90 LVAVGNTFVYPLAGYSKKIKNVNELQDGAKVAVPNDPTNLGRALLLLQKQGLIKLKDGNGLLPTVLDIVENPKKLNITEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 184 EGAQLPRVLDDPKVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETI 263
Cdd:TIGR00363 170 ETSQLPRALDDPKVDLAVINTTYAGQVGLNPQDDGVFVEDKDSPYVNIIVSREDNKDAENVKDFIQSYQSEEVYQAAQKH 249
|
....*....
gi 15833849 264 FNGGAVPGW 272
Cdd:TIGR00363 250 FNGGAVKGW 258
|
|
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
25-272 |
6.56e-129 |
|
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: 366.36 E-value: 6.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 25 DQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKL 104
Cdd:COG1464 26 AAAAADKKTIKVGATPGPHAEILEVVKPELAKK-GIDLEIVEFTDYVQPNEALADGEIDANYFQHIPYLDNFNKENGYDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 105 VAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELE 184
Cdd:COG1464 105 VPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKAGLIKLKDGVGLLATVKDITENPKNLKFVELD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 185 GAQLPRVLDDpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIF 264
Cdd:COG1464 185 AAQLPRSLDD--VDAAVINGNYALEAGLDPTKDALFLEDKDSPYANIIVVREDDKDDPAIKKLVEAYQSDEVKKFIEEKY 262
|
....*...
gi 15833849 265 NGGAVPGW 272
Cdd:COG1464 263 KGAVVPAW 270
|
|
| PBP2_lipoprotein_IlpA_like |
cd13598 |
Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar ... |
33-262 |
5.39e-117 |
|
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: 334.70 E-value: 5.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 33 HIKVGVINGAEQDVAEVAKKVAKEKYgLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFV 112
Cdd:cd13598 1 PIKVGVIRGPDAQIWEVVQKVAKEKG-LDVELVTFNDYAQPNEALAAGDLDANAFQHKPYLDAQIKARGYKLVIVGNTFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 113 FPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVL 192
Cdd:cd13598 80 YPIGLYSKKIKSLAELPNGATVAIPNDPSNEGRALLLLQKEGLIKLKDGVGLLATVRDIAENPKKLKIVELDAGQLPRAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 193 DDpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAET 262
Cdd:cd13598 160 DD--VDLAAINTDYASKAGLTPARDAIAQEDKRSPYANVIAVREDDKDAPWVKTLVQAYQSEEVKAFALK 227
|
|
| Lipoprotein_9 |
pfam03180 |
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ... |
34-272 |
1.61e-116 |
|
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: 333.85 E-value: 1.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 34 IKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVF 113
Cdd:pfam03180 1 LKVGATPGPHAEILEVAKPLLKKK-GLDLEIVEFTDYVQPNTALADGEIDANYFQHLPYLDQFNKEKGLDLVAVGNVHIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 114 PMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVLD 193
Cdd:pfam03180 80 PMGLYSKKYKSLSELPDGATIAVPNDPSNEGRALLLLQKAGLIKLKDGKGLLATVKDITENPKNLKIKELEAAQLPRALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833849 194 DpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIFNGGAVPGW 272
Cdd:pfam03180 160 D--VDAAVINTNYALEAGLNPKKDALFEEDKDSPYVNIIVVREDDKDDEAVKKLVEAYQSEEVKKFIEKKYGGAVIPAW 236
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09861 |
PRK09861 |
lipoprotein NlpA; |
1-272 |
0e+00 |
|
lipoprotein NlpA;
Pssm-ID: 182119 Cd Length: 272 Bit Score: 588.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 1 MKLTTHHLRAGAALLLAGVLLAGCDQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNG 80
Cdd:PRK09861 1 MKLTTHHLRAGAALLLAGILLAGCDQSSSDAKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 81 ELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKE 160
Cdd:PRK09861 81 ELDANVFQHRPFLEQDNQAHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 161 GKGLLPTALDITDNPRHLQIMELEGAQLPRVLDDPKVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKN 240
Cdd:PRK09861 161 GKGLLPTALDITDNPRHLQIMELEGAQLPRVLDDPKVDVAIISTTYIQQTGLSPVHDSVFIEDKNSPYVNILVAREDNKN 240
|
250 260 270
....*....|....*....|....*....|..
gi 15833849 241 AENVKEFLQSYQSPEVAKAAETIFNGGAVPGW 272
Cdd:PRK09861 241 AENVKEFLQSYQSPEVAKAAETIFNGGAVPGW 272
|
|
| TIGR00363 |
TIGR00363 |
lipoprotein, YaeC family; This family of putative lipoproteins contains a consensus site for ... |
24-272 |
2.26e-165 |
|
lipoprotein, YaeC family; This family of putative lipoproteins contains a consensus site for lipoprotein signal sequence cleavage. Included in this family is the E. coli hypothetical protein yaeC. About half of the proteins between the noise and trusted cutoffs contain the consensus lipoprotein signature and may belong to this family. [Cell envelope, Other]
Pssm-ID: 129460 Cd Length: 258 Bit Score: 458.21 E-value: 2.26e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 24 CDQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYK 103
Cdd:TIGR00363 10 CKQDKKDPLHIKVGVISGAEQQVAEVAAKVAKEKYGLDVELVEFNDYALPNEAVSKGDLDANAFQHKPYLDQDAKAKGYK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 104 LVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMEL 183
Cdd:TIGR00363 90 LVAVGNTFVYPLAGYSKKIKNVNELQDGAKVAVPNDPTNLGRALLLLQKQGLIKLKDGNGLLPTVLDIVENPKKLNITEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 184 EGAQLPRVLDDPKVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETI 263
Cdd:TIGR00363 170 ETSQLPRALDDPKVDLAVINTTYAGQVGLNPQDDGVFVEDKDSPYVNIIVSREDNKDAENVKDFIQSYQSEEVYQAAQKH 249
|
....*....
gi 15833849 264 FNGGAVPGW 272
Cdd:TIGR00363 250 FNGGAVKGW 258
|
|
| metQ |
PRK11063 |
D-methionine ABC transporter substrate-binding protein MetQ; |
24-272 |
6.21e-137 |
|
D-methionine ABC transporter substrate-binding protein MetQ;
Pssm-ID: 182939 [Multi-domain] Cd Length: 271 Bit Score: 386.81 E-value: 6.21e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 24 CDQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYK 103
Cdd:PRK11063 23 CGQDEKDPNHIKVGVIVGAEQQVAEVAQKVAKEKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYLDQQIKDRGYK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 104 LVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMEL 183
Cdd:PRK11063 103 LVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDIVENPKNLKIVEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 184 EGAQLPRVLDDPKVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETI 263
Cdd:PRK11063 183 EAPQLPRSLDDAQIALAVINTTYASQIGLTPAKDGIFVEDKDSPYVNLIVAREDNKDAENVKKFVQAYQSDEVYEAANKV 262
|
....*....
gi 15833849 264 FNGGAVPGW 272
Cdd:PRK11063 263 FNGGAVKGW 271
|
|
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
25-272 |
6.56e-129 |
|
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: 366.36 E-value: 6.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 25 DQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKL 104
Cdd:COG1464 26 AAAAADKKTIKVGATPGPHAEILEVVKPELAKK-GIDLEIVEFTDYVQPNEALADGEIDANYFQHIPYLDNFNKENGYDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 105 VAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELE 184
Cdd:COG1464 105 VPVGKTHIEPMGLYSKKYKSLDELPDGATIAIPNDPTNQGRALLLLQKAGLIKLKDGVGLLATVKDITENPKNLKFVELD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 185 GAQLPRVLDDpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIF 264
Cdd:COG1464 185 AAQLPRSLDD--VDAAVINGNYALEAGLDPTKDALFLEDKDSPYANIIVVREDDKDDPAIKKLVEAYQSDEVKKFIEEKY 262
|
....*...
gi 15833849 265 NGGAVPGW 272
Cdd:COG1464 263 KGAVVPAW 270
|
|
| PBP2_lipoprotein_IlpA_like |
cd13598 |
Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar ... |
33-262 |
5.39e-117 |
|
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: 334.70 E-value: 5.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 33 HIKVGVINGAEQDVAEVAKKVAKEKYgLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFV 112
Cdd:cd13598 1 PIKVGVIRGPDAQIWEVVQKVAKEKG-LDVELVTFNDYAQPNEALAAGDLDANAFQHKPYLDAQIKARGYKLVIVGNTFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 113 FPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVL 192
Cdd:cd13598 80 YPIGLYSKKIKSLAELPNGATVAIPNDPSNEGRALLLLQKEGLIKLKDGVGLLATVRDIAENPKKLKIVELDAGQLPRAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 193 DDpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAET 262
Cdd:cd13598 160 DD--VDLAAINTDYASKAGLTPARDAIAQEDKRSPYANVIAVREDDKDAPWVKTLVQAYQSEEVKAFALK 227
|
|
| Lipoprotein_9 |
pfam03180 |
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ... |
34-272 |
1.61e-116 |
|
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: 333.85 E-value: 1.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 34 IKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVF 113
Cdd:pfam03180 1 LKVGATPGPHAEILEVAKPLLKKK-GLDLEIVEFTDYVQPNTALADGEIDANYFQHLPYLDQFNKEKGLDLVAVGNVHIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 114 PMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVLD 193
Cdd:pfam03180 80 PMGLYSKKYKSLSELPDGATIAVPNDPSNEGRALLLLQKAGLIKLKDGKGLLATVKDITENPKNLKIKELEAAQLPRALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833849 194 DpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIFNGGAVPGW 272
Cdd:pfam03180 160 D--VDAAVINTNYALEAGLNPKKDALFEEDKDSPYVNIIVVREDDKDDEAVKKLVEAYQSEEVKKFIEKKYGGAVIPAW 236
|
|
| PBP2_lipoprotein_MetQ_like |
cd13526 |
The periplasmic-binding component of ABC-type methionine uptake transporter system and its ... |
33-261 |
5.53e-98 |
|
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: 286.52 E-value: 5.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 33 HIKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFV 112
Cdd:cd13526 1 KLKIGVTAGPSADVVEAAKKEAKKK-GYELELVVFTDYVAPNEALNDGSIDANFFQHVPFLDQFNKERNGDLVKVGKTVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 113 FPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVL 192
Cdd:cd13526 80 APIGLYSKKYKSLDELPDGARIAIPNDPSNGARALLLLEDAGLIKLKDGVGLFATVLDITENPKNLEIVEVDAAQLPRSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 193 DDpkVDVAIISTTYIEQTGLSPVNDSVFIEDK-NSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAE 261
Cdd:cd13526 160 DD--VDAAVINGNYAISAGLDPRKDAIFLEDSdASPYVNVLAVREDNKDDPWVKALVEAYQSEEVRKFLK 227
|
|
| PBP2_lipoprotein_Tp32 |
cd13597 |
The substrate-binding domain of the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum ... |
34-270 |
3.86e-84 |
|
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: 251.81 E-value: 3.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 34 IKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVF 113
Cdd:cd13597 2 LKVGATPVPHAEILEFIKPELKKQ-GIDLEIVEFTDYVQPNTALADGELDANYFQHVPYLESFNKEKGYDLVAVAGVHLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 114 PMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVLD 193
Cdd:cd13597 81 PMGLYSKKYKSLEDLPDGATIAIPNDPTNQGRALLLLEEAGLITLKDGAGLTATVKDIVKNPKNLKFKELEAAQLPRSLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833849 194 DpkVDVAIISTTYIEQTGLSPVNDSVFIEDK-NSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIFNGGAVP 270
Cdd:cd13597 161 D--VDAAVINGNYALEAGLNPKKDALALEDKdNSPYANILVVRKGNEDDPRIKKLAKALQSDEVKDFIEEKYDGAVVP 236
|
|
| PBP2_lipoprotein_GmpC |
cd13596 |
The periplasmic substrate-binding domain of the membrane-associated lipoprotein-9 GmpC; ... |
34-261 |
4.94e-71 |
|
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: 218.00 E-value: 4.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 34 IKVGVInGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVF 113
Cdd:cd13596 2 VKIGVT-GEDTDIWDKIVEEAEEA-GIKLELVNFSDYSQPNKALNDGDIDLNAFQHYAYLVQYNSKNNADLTAIGDTVIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 114 PMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVLD 193
Cdd:cd13596 80 PMGIYSKKITSVDELPDGAKIAIPNDPSNLSRALFILQAAGLIKLKKDAGDFPTVNDITENPKNLEIVPVDADQVYRALN 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833849 194 DpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNS----PYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAE 261
Cdd:cd13596 160 D--VDAAVINNTFALDAGLDPKKDAIFLEDPSSygskPYINLIAVREEDKDNPLYKKLVETYHDERVQKAVE 229
|
|
| PBP2_lipoprotein_like_1 |
cd13600 |
Putative periplasmic-binding component of ABC-type methionine uptake transporter system-like; ... |
34-262 |
1.38e-69 |
|
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: 214.51 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 34 IKVGVINGAEQDVAEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVF 113
Cdd:cd13600 2 LKVATNSGPMTEILEYIAAELAPD-GITIEPVQVSDYVQANRAVAAGEIDANFFQHQPFMEQFNEANGFELVAVQPIYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 114 PMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTAL-DITDNPRHLQIMELEGAQLPRVL 192
Cdd:cd13600 81 AFGFYSKKYKSVEDLPDGAKVAIPNDPANQARALLLLQRAGLITLKPGVDPTTATLaDIVTNPKNLKFTEVDLLALPRAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 193 DDpkVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAET 262
Cdd:cd13600 161 DD--VDLAFGYPSYFDAAGLTPKDGILLEEPDAKRFAIQLVAREDNKDSPKIKKLKEAFTDPRVRKFLET 228
|
|
| PBP2_lipoprotein_Gna1946 |
cd13599 |
The membrane-associated lipoprotein Gna1946 from Neisseria meningitidis; the type 2 ... |
34-260 |
4.06e-56 |
|
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: 179.90 E-value: 4.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 34 IKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVF 113
Cdd:cd13599 2 IVIGFTPGPYGDMVKNGVAPYLEKKGYEVKLKEFTDYVQPNNALANGEIDANVFQHKPYLDAFNKENGLDLVGIVQVPTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 114 PMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEG-KGLLPTALDITDNPRHLQIMELEGAQLPRVL 192
Cdd:cd13599 82 PMGLYSNKHKSLEEVKDGATVAIPNDPSNLARALVMLQDLGWITLKDNiDPLKASVNDIAENPKNIKIVELEAAQLPRSL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833849 193 DDpkVDVAIISTTYIEQTGLSPVNdSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAA 260
Cdd:cd13599 162 DD--VDFAAIQGNFAISSGIKLTS-ALALEEMTDPYVNVVAVKTADKDKQFAKDVTAAYNSDAFKAYI 226
|
|
| TauA |
COG0715 |
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ... |
27-252 |
1.08e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440479 [Multi-domain] Cd Length: 297 Bit Score: 57.71 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 27 SSSDEKHIKVGVINGAEQDVAEVAKkvAK---EKYGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLeqDNQTHGYK 103
Cdd:COG0715 17 AAAEKVTLRLGWLPNTDHAPLYVAK--EKgyfKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPAL--AARAKGAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 104 LVAVGNTFVFPMAGY----SKKIKTVAQIKeGATVAIPNDPTNLGRALLLLQKEKLitlkegkgllptalditdNPRHLQ 179
Cdd:COG0715 93 VKAVAALSQSGGNALvvrkDSGIKSLADLK-GKKVAVPGGSTSHYLLRALLAKAGL------------------DPKDVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 180 IMELEGAQLPRVLDDPKVDVAIISTTY---IEQTG----LSPVNDSVfiedkNSPYVNILVARED--NKNAENVKEFLQS 250
Cdd:COG0715 154 IVNLPPPDAVAALLAGQVDAAVVWEPFesqAEKKGggrvLADSADLV-----PGYPGDVLVASEDflEENPEAVKAFLRA 228
|
..
gi 15833849 251 YQ 252
Cdd:COG0715 229 LL 230
|
|
| PBP2_SsuA_like_6 |
cd13563 |
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ... |
56-251 |
7.41e-04 |
|
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA 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: 270281 [Multi-domain] Cd Length: 208 Bit Score: 39.91 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 56 EKYGLDVELVGFSGSLLPNDATNNGELDANV-------------FQHRPFLEQDNQTHGYKLVAvgntfvfpmagySKKI 122
Cdd:cd13563 25 KKEGLDVELVWFESYSDSMAALASGQIDAAAttlddalamaakgVPVKIVLVLDNSNGADGIVA------------KPGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 123 KTVAQIKeGATVAIPNDPTNlgrALLLLqkekliTLKEGKGLlpTALDITdnprhlqIMELEGAQLPRVLDDPKVDVAII 202
Cdd:cd13563 93 KSIADLK-GKTVAVEEGSVS---HFLLL------NALEKAGL--TEKDVK-------IVNMTAGDAGAAFIAGQVDAAVT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15833849 203 STTYIEQtGLSPVNDSVFIEDKNSP--YVNILVARED--NKNAENVKEFLQSY 251
Cdd:cd13563 154 WEPWLSN-ALKRGKGKVLVSSADTPglIPDVLVVREDfiKKNPEAVKAVVKAW 205
|
|
| OpuAC |
pfam04069 |
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ... |
32-263 |
8.04e-03 |
|
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity multicomponent binding-protein-dependent transport system involved in bacterial osmoregulation. This domain is often fused to the permease component of the transporter complex. Family members are often integral membrane proteins or predicted to be attached to the membrane by a lipid anchor. Glycine betaine is involved in protection from high osmolarity environments for example in Bacillus subtilis. The family member OpuBC is closely related, and involved in choline transport. Choline is necessary for the biosynthesis of glycine betaine. L-carnitine is important for osmoregulation in Listeria monocytogenes. Family also contains proteins binding l-proline (ProX), histidine (HisX) and taurine (TauA).
Pssm-ID: 397954 [Multi-domain] Cd Length: 257 Bit Score: 36.92 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 32 KHIKVGVINGAEQDV-AEVAKKVAKEKyGLDVELVGFSGSLLPNDATNNGELDANVF--------QHRPFLEQDNQTHGY 102
Cdd:pfam04069 1 KTIVIGSKNWTEQEIlANIAAQLLEAL-GYVVELVGLGSSAVLFAALASGDIDLYPEewtgttyeAYKKAVEEKLGLLVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 103 KLVAVGNT--FVFPMAGYSK-KIKTVAQIK-------EGATVAIPNDPTNLGRALLLLQKEKLITLKegkgllptalDIT 172
Cdd:pfam04069 80 GPLGAGNTygLAVPKYVAEKpGIKSISDLAkpaddleLGFKGEFIGRPDGWGCMRSTEGLLKAYGLD----------KYE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833849 173 DNPRHLQIMElegAQLPRVLDDPKVDVAIISTTyieqTGLSPVNDSVFIED-KNS---PYVNILVARednknaenvKEFL 248
Cdd:pfam04069 150 LVEGSEAAMD---ALIYAAYKRGEPDVVYAWTP----DWMIKKYDLVVLEDpKGLfppAYNVVPVVR---------KGFA 213
|
250
....*....|....*
gi 15833849 249 QSYqsPEVAKAAETI 263
Cdd:pfam04069 214 EKH--PEVAAFLNKL 226
|
|
| |
