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Conserved domains on  [gi|1083760514|gb|OGI41702|]
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outer membrane lipoprotein-sorting protein, partial [Candidatus Muproteobacteria bacterium RBG_16_62_13]

Protein Classification

outer membrane lipoprotein-sorting protein( domain architecture ID 11611375)

outer membrane lipoprotein-sorting protein similar to periplasmic molecular chaperone LolA that accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB

Gene Ontology:  GO:0009279|GO:0044874|GO:0042953
PubMed:  19307584|30012603
SCOP:  3001964

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LolA_like cd16329
proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
 6-223 9.98e-66

proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains uncharacterized proteins similar to the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB, all of which have similar unclosed beta-barrel structures that resemble a baseball glove-like scaffold consisting of an 11-stranded antiparallel sheet. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. It is proposed that the LolA/LolB complex forms a tunnel-like structure, where the hydrophobic insides of LolA and LolB are connected, which enables lipoproteins to transfer from LolA to LolB. RseB exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. Its structural similarity to LolA and LolB suggests that RseA may act as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response.


:

Pssm-ID: 319986  Cd Length: 225  Bit Score: 202.93  E-value: 9.98e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514   6 DAATIIKRAIDYWRDVSSYSVADMTIRRPD-WTRTMTIRVWTRGQKE--SLVRVTAPAKDAGNATLLLD-----NDMWSY 77
Cdd:cd16329     1 SAEEILEKVDDRRRGDSSADVSTMTLTDKNgKERTRELRVYSKDGGDdkSLIRFLSPADVKGTAFLTLDyddkdDDQWLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  78 TPRINRIIKIPSSMMSQSWMGSDFSNNDLAKaDDLIEHYTHKLLRTETHDGHKVYVVESTPKETAPVVWGREVVLIR-DD 156
Cdd:cd16329    81 LPALRRVRRISSSDKSQSFMGSDFSYEDLSR-SRLLEDYTYKLLGEEEVDGRDCYVLELTPKDGADSGYSKRVLWVDkDT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083760514 157 HLVLEHRFYDQRNVLVKTMKTVRLGQYGGKLVAAHQRMQKAEsPGEWTDIVVKEARFGVTLPAPTFT 223
Cdd:cd16329   160 FLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLL-TGHKTVLEYSDIKFNVGLPDSLFT 225
 
Name Accession Description Interval E-value
LolA_like cd16329
proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
 6-223 9.98e-66

proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains uncharacterized proteins similar to the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB, all of which have similar unclosed beta-barrel structures that resemble a baseball glove-like scaffold consisting of an 11-stranded antiparallel sheet. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. It is proposed that the LolA/LolB complex forms a tunnel-like structure, where the hydrophobic insides of LolA and LolB are connected, which enables lipoproteins to transfer from LolA to LolB. RseB exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. Its structural similarity to LolA and LolB suggests that RseA may act as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response.


Pssm-ID: 319986  Cd Length: 225  Bit Score: 202.93  E-value: 9.98e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514   6 DAATIIKRAIDYWRDVSSYSVADMTIRRPD-WTRTMTIRVWTRGQKE--SLVRVTAPAKDAGNATLLLD-----NDMWSY 77
Cdd:cd16329     1 SAEEILEKVDDRRRGDSSADVSTMTLTDKNgKERTRELRVYSKDGGDdkSLIRFLSPADVKGTAFLTLDyddkdDDQWLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  78 TPRINRIIKIPSSMMSQSWMGSDFSNNDLAKaDDLIEHYTHKLLRTETHDGHKVYVVESTPKETAPVVWGREVVLIR-DD 156
Cdd:cd16329    81 LPALRRVRRISSSDKSQSFMGSDFSYEDLSR-SRLLEDYTYKLLGEEEVDGRDCYVLELTPKDGADSGYSKRVLWVDkDT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083760514 157 HLVLEHRFYDQRNVLVKTMKTVRLGQYGGKLVAAHQRMQKAEsPGEWTDIVVKEARFGVTLPAPTFT 223
Cdd:cd16329   160 FLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLL-TGHKTVLEYSDIKFNVGLPDSLFT 225
LolA_like pfam17131
Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ...
 48-229 3.06e-54

Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane lipoprotein-sorting proteins.


Pssm-ID: 435738 [Multi-domain]  Cd Length: 184  Bit Score: 171.98  E-value: 3.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  48 GQKESLVRVTAPAKDAGNATLLL----DNDMWSYTPRINRIIKIPSSMMSQSWMGSDFSNNDLAKaDDLIEHYTHKLLRT 123
Cdd:pfam17131   1 GDDKSLIVFLSPADVKGTAFLTLdyggDDDQWLYLPALKRVRRISSSDKSQSFMGSDFSYEDLSR-SRLVDDYTHELLGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514 124 ETHDGHKVYVVESTPKeTAPVVWGREVVLIR-DDHLVLEHRFYDQRNVLVKTMKTVRLGQYGGKLVAAHQRMQKAEsPGE 202
Cdd:pfam17131  80 ETVGGKDCYVLELTPK-DKDVSYSKRVLWVDkETYLPLKAEFYDKSGKLLKTLTVSDIEKIDGRWTPTKMEMEDLQ-TGH 157

                         170       180
                  ....*....|....*....|....*..
gi 1083760514 203 WTDIVVKEARFGVTLPAPTFTQANLRN 229
Cdd:pfam17131 158 KTVLEISDIEFDTGLPDKLFTKRYLER 184
LolA COG2834
Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis];
2-167 9.19e-12

Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442082  Cd Length: 211  Bit Score: 62.02  E-value: 9.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514   2 AAEPDAATIIKRAIDYWRDVSSYSvADMTIRRPDW----TRTMTIRVWTRGQKESLVRVTAPAKDagnaTLLLDND-MWS 76
Cdd:COG2834    19 GAAQSAEEILDKLQAKLNSIKSLS-ADFTQTVTDAggnePQTSSGKFWLKRPGKFRWEYTKPYEQ----LIVSDGKtVWI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  77 YTPRINRIIKIPSSMMS-QSWMGSDFSnndlakadDLIEHYTHKLLRTEthDGHKVYVVESTPKETAPVVwGREVVLIRD 155
Cdd:COG2834    94 YDPDLNQVTVIPLSDATpLALLLGDFS--------DLLKDFTVTLLGEE--TGRKAYVLELTPKDKDSGF-GKITLWFDK 162

                         170
                  ....*....|..
gi 1083760514 156 DHLVLEHRFYDQ 167
Cdd:COG2834   163 ETLLRKLEIYDA 174
 
Name Accession Description Interval E-value
LolA_like cd16329
proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
 6-223 9.98e-66

proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains uncharacterized proteins similar to the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB, all of which have similar unclosed beta-barrel structures that resemble a baseball glove-like scaffold consisting of an 11-stranded antiparallel sheet. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. It is proposed that the LolA/LolB complex forms a tunnel-like structure, where the hydrophobic insides of LolA and LolB are connected, which enables lipoproteins to transfer from LolA to LolB. RseB exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. Its structural similarity to LolA and LolB suggests that RseA may act as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response.


Pssm-ID: 319986  Cd Length: 225  Bit Score: 202.93  E-value: 9.98e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514   6 DAATIIKRAIDYWRDVSSYSVADMTIRRPD-WTRTMTIRVWTRGQKE--SLVRVTAPAKDAGNATLLLD-----NDMWSY 77
Cdd:cd16329     1 SAEEILEKVDDRRRGDSSADVSTMTLTDKNgKERTRELRVYSKDGGDdkSLIRFLSPADVKGTAFLTLDyddkdDDQWLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  78 TPRINRIIKIPSSMMSQSWMGSDFSNNDLAKaDDLIEHYTHKLLRTETHDGHKVYVVESTPKETAPVVWGREVVLIR-DD 156
Cdd:cd16329    81 LPALRRVRRISSSDKSQSFMGSDFSYEDLSR-SRLLEDYTYKLLGEEEVDGRDCYVLELTPKDGADSGYSKRVLWVDkDT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083760514 157 HLVLEHRFYDQRNVLVKTMKTVRLGQYGGKLVAAHQRMQKAEsPGEWTDIVVKEARFGVTLPAPTFT 223
Cdd:cd16329   160 FLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLL-TGHKTVLEYSDIKFNVGLPDSLFT 225
LolA_like pfam17131
Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ...
 48-229 3.06e-54

Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane lipoprotein-sorting proteins.


Pssm-ID: 435738 [Multi-domain]  Cd Length: 184  Bit Score: 171.98  E-value: 3.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  48 GQKESLVRVTAPAKDAGNATLLL----DNDMWSYTPRINRIIKIPSSMMSQSWMGSDFSNNDLAKaDDLIEHYTHKLLRT 123
Cdd:pfam17131   1 GDDKSLIVFLSPADVKGTAFLTLdyggDDDQWLYLPALKRVRRISSSDKSQSFMGSDFSYEDLSR-SRLVDDYTHELLGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514 124 ETHDGHKVYVVESTPKeTAPVVWGREVVLIR-DDHLVLEHRFYDQRNVLVKTMKTVRLGQYGGKLVAAHQRMQKAEsPGE 202
Cdd:pfam17131  80 ETVGGKDCYVLELTPK-DKDVSYSKRVLWVDkETYLPLKAEFYDKSGKLLKTLTVSDIEKIDGRWTPTKMEMEDLQ-TGH 157

                         170       180
                  ....*....|....*....|....*..
gi 1083760514 203 WTDIVVKEARFGVTLPAPTFTQANLRN 229
Cdd:pfam17131 158 KTVLEISDIEFDTGLPDKLFTKRYLER 184
LolA COG2834
Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis];
2-167 9.19e-12

Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442082  Cd Length: 211  Bit Score: 62.02  E-value: 9.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514   2 AAEPDAATIIKRAIDYWRDVSSYSvADMTIRRPDW----TRTMTIRVWTRGQKESLVRVTAPAKDagnaTLLLDND-MWS 76
Cdd:COG2834    19 GAAQSAEEILDKLQAKLNSIKSLS-ADFTQTVTDAggnePQTSSGKFWLKRPGKFRWEYTKPYEQ----LIVSDGKtVWI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083760514  77 YTPRINRIIKIPSSMMS-QSWMGSDFSnndlakadDLIEHYTHKLLRTEthDGHKVYVVESTPKETAPVVwGREVVLIRD 155
Cdd:COG2834    94 YDPDLNQVTVIPLSDATpLALLLGDFS--------DLLKDFTVTLLGEE--TGRKAYVLELTPKDKDSGF-GKITLWFDK 162

                         170
                  ....*....|..
gi 1083760514 156 DHLVLEHRFYDQ 167
Cdd:COG2834   163 ETLLRKLEIYDA 174
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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