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Conserved domains on  [gi|15830549|ref|NP_309322|]
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hypothetical protein ECs_1295 [Escherichia coli O157:H7 str. Sakai]

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 ...
 28-253 5.75e-42

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: 143.22  E-value: 5.75e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549  28 KALEIIRRADEIRSPNKPFRY-TLTVTEYkagatqpeNKQVLDISMRFMKpqgNEKADARSLVRFIYPPRDKGKIMLSDW 106
Cdd:cd16329   1 SAEEILEKVDDRRRGDSSADVsTMTLTDK--------NGKERTRELRVYS---KDGGDDKSLIRFLSPADVKGTAFLTLD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549 107 Y-----DLWFYTPELRRPMPIS---RQQRLIG-QISNGDVIVTNFEYAYDSTLMGEVTCAEKQCYKLALVRKS-ADITWP 176
Cdd:cd16329  70 YddkddDQWLYLPALRRVRRISssdKSQSFMGsDFSYEDLSRSRLLEDYTYKLLGEEEVDGRDCYVLELTPKDgADSGYS 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830549 177 KVIYYVEKDgDNRPWKAAYYSQDDQLIKEVLYQDFQPVLGKTRPMKITVTDVRHGnNYSVMEYSDVRLES-LPEFHFT 253
Cdd:cd16329 150 KRVLWVDKD-TFLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLLTG-HKTVLEYSDIKFNVgLPDSLFT 225
 
Name Accession Description Interval E-value
LolA_like cd16329
proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
 28-253 5.75e-42

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: 143.22  E-value: 5.75e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549  28 KALEIIRRADEIRSPNKPFRY-TLTVTEYkagatqpeNKQVLDISMRFMKpqgNEKADARSLVRFIYPPRDKGKIMLSDW 106
Cdd:cd16329   1 SAEEILEKVDDRRRGDSSADVsTMTLTDK--------NGKERTRELRVYS---KDGGDDKSLIRFLSPADVKGTAFLTLD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549 107 Y-----DLWFYTPELRRPMPIS---RQQRLIG-QISNGDVIVTNFEYAYDSTLMGEVTCAEKQCYKLALVRKS-ADITWP 176
Cdd:cd16329  70 YddkddDQWLYLPALRRVRRISssdKSQSFMGsDFSYEDLSRSRLLEDYTYKLLGEEEVDGRDCYVLELTPKDgADSGYS 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830549 177 KVIYYVEKDgDNRPWKAAYYSQDDQLIKEVLYQDFQPVLGKTRPMKITVTDVRHGnNYSVMEYSDVRLES-LPEFHFT 253
Cdd:cd16329 150 KRVLWVDKD-TFLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLLTG-HKTVLEYSDIKFNVgLPDSLFT 225
LolA_like pfam17131
Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ...
 84-259 1.09e-40

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: 138.46  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549    84 DARSLVRFIYPPRDKGKIMLSDWY----DLWFYTPELRRPMPIS---RQQRLIGQ-ISNGDVIVTNFEYAYDSTLMGEVT 155
Cdd:pfam17131   2 DDKSLIVFLSPADVKGTAFLTLDYggddDQWLYLPALKRVRRISssdKSQSFMGSdFSYEDLSRSRLVDDYTHELLGEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549   156 CAEKQCYKLALVRKSADITWPKVIYYVEKDgDNRPWKAAYYSQDDQLIKEVLYQDFQPVLGKTRPMKITVTDVRHGnNYS 235
Cdd:pfam17131  82 VGGKDCYVLELTPKDKDVSYSKRVLWVDKE-TYLPLKAEFYDKSGKLLKTLTVSDIEKIDGRWTPTKMEMEDLQTG-HKT 159

                         170       180
                  ....*....|....*....|....*
gi 15830549   236 VMEYSDVRL-ESLPEFHFTKEYIQR 259
Cdd:pfam17131 160 VLEISDIEFdTGLPDKLFTKRYLER 184
LolA COG2834
Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis];
8-213 4.77e-04

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


Pssm-ID: 442082  Cd Length: 211  Bit Score: 40.45  E-value: 4.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549   8 KWFACLWLATSCVQAASTDNKALEIIRRADEIRSPNKPFRYTLTVTEYKAGATQPenkQVLDISMRFMKPqgnekadarS 87
Cdd:COG2834   3 KRLLLLLALLLLLALAGAAQSAEEILDKLQAKLNSIKSLSADFTQTVTDAGGNEP---QTSSGKFWLKRP---------G 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549  88 LVRFIY-PPrdKGKIMLSDWYDLWFYTPELRRP--MPISRQQRLIGQISNGDVIVTNFEYAYDSTLMGevtcaeKQCYKL 164
Cdd:COG2834  71 KFRWEYtKP--YEQLIVSDGKTVWIYDPDLNQVtvIPLSDATPLALLLGDFSDLLKDFTVTLLGEETG------RKAYVL 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15830549 165 ALVRKSADITWPKVIYYVekDGDNRPWKAAYYSQDDQLIkEVLYQDFQP 213
Cdd:COG2834 143 ELTPKDKDSGFGKITLWF--DKETLLRKLEIYDADGQRT-TITFSNVKT 188
 
Name Accession Description Interval E-value
LolA_like cd16329
proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
 28-253 5.75e-42

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: 143.22  E-value: 5.75e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549  28 KALEIIRRADEIRSPNKPFRY-TLTVTEYkagatqpeNKQVLDISMRFMKpqgNEKADARSLVRFIYPPRDKGKIMLSDW 106
Cdd:cd16329   1 SAEEILEKVDDRRRGDSSADVsTMTLTDK--------NGKERTRELRVYS---KDGGDDKSLIRFLSPADVKGTAFLTLD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549 107 Y-----DLWFYTPELRRPMPIS---RQQRLIG-QISNGDVIVTNFEYAYDSTLMGEVTCAEKQCYKLALVRKS-ADITWP 176
Cdd:cd16329  70 YddkddDQWLYLPALRRVRRISssdKSQSFMGsDFSYEDLSRSRLLEDYTYKLLGEEEVDGRDCYVLELTPKDgADSGYS 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830549 177 KVIYYVEKDgDNRPWKAAYYSQDDQLIKEVLYQDFQPVLGKTRPMKITVTDVRHGnNYSVMEYSDVRLES-LPEFHFT 253
Cdd:cd16329 150 KRVLWVDKD-TFLPLKAEYYDRSGKLLKTLTFSDIKKIGGYWRPTRMEMKDLLTG-HKTVLEYSDIKFNVgLPDSLFT 225
LolA_like pfam17131
Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ...
 84-259 1.09e-40

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: 138.46  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549    84 DARSLVRFIYPPRDKGKIMLSDWY----DLWFYTPELRRPMPIS---RQQRLIGQ-ISNGDVIVTNFEYAYDSTLMGEVT 155
Cdd:pfam17131   2 DDKSLIVFLSPADVKGTAFLTLDYggddDQWLYLPALKRVRRISssdKSQSFMGSdFSYEDLSRSRLVDDYTHELLGEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549   156 CAEKQCYKLALVRKSADITWPKVIYYVEKDgDNRPWKAAYYSQDDQLIKEVLYQDFQPVLGKTRPMKITVTDVRHGnNYS 235
Cdd:pfam17131  82 VGGKDCYVLELTPKDKDVSYSKRVLWVDKE-TYLPLKAEFYDKSGKLLKTLTVSDIEKIDGRWTPTKMEMEDLQTG-HKT 159

                         170       180
                  ....*....|....*....|....*
gi 15830549   236 VMEYSDVRL-ESLPEFHFTKEYIQR 259
Cdd:pfam17131 160 VLEISDIEFdTGLPDKLFTKRYLER 184
LolA COG2834
Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis];
8-213 4.77e-04

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


Pssm-ID: 442082  Cd Length: 211  Bit Score: 40.45  E-value: 4.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549   8 KWFACLWLATSCVQAASTDNKALEIIRRADEIRSPNKPFRYTLTVTEYKAGATQPenkQVLDISMRFMKPqgnekadarS 87
Cdd:COG2834   3 KRLLLLLALLLLLALAGAAQSAEEILDKLQAKLNSIKSLSADFTQTVTDAGGNEP---QTSSGKFWLKRP---------G 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830549  88 LVRFIY-PPrdKGKIMLSDWYDLWFYTPELRRP--MPISRQQRLIGQISNGDVIVTNFEYAYDSTLMGevtcaeKQCYKL 164
Cdd:COG2834  71 KFRWEYtKP--YEQLIVSDGKTVWIYDPDLNQVtvIPLSDATPLALLLGDFSDLLKDFTVTLLGEETG------RKAYVL 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15830549 165 ALVRKSADITWPKVIYYVekDGDNRPWKAAYYSQDDQLIkEVLYQDFQP 213
Cdd:COG2834 143 ELTPKDKDSGFGKITLWF--DKETLLRKLEIYDADGQRT-TITFSNVKT 188
 
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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