Chain B, Uncharacterized LolA superfamily protein NE2245
outer membrane lipoprotein-sorting protein( domain architecture ID 12181914)
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
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
LolA_like | pfam17131 | Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ... |
52-227 | 3.16e-58 | ||||
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: 181.99 E-value: 3.16e-58
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Name | Accession | Description | Interval | E-value | ||||
LolA_like | pfam17131 | Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ... |
52-227 | 3.16e-58 | ||||
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: 181.99 E-value: 3.16e-58
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LolA_like | cd16329 | proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ... |
8-221 | 1.09e-49 | ||||
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: 161.71 E-value: 1.09e-49
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LolA | COG2834 | Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis]; |
60-182 | 1.91e-06 | ||||
Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442082 Cd Length: 211 Bit Score: 47.00 E-value: 1.91e-06
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Name | Accession | Description | Interval | E-value | ||||
LolA_like | pfam17131 | Outer membrane lipoprotein-sorting protein; This is likely to be a family of outer-membrane ... |
52-227 | 3.16e-58 | ||||
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: 181.99 E-value: 3.16e-58
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LolA_like | cd16329 | proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein ... |
8-221 | 1.09e-49 | ||||
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: 161.71 E-value: 1.09e-49
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LolA | COG2834 | Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis]; |
60-182 | 1.91e-06 | ||||
Outer membrane lipoprotein-sorting protein [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442082 Cd Length: 211 Bit Score: 47.00 E-value: 1.91e-06
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Blast search parameters | ||||
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