LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA which ...
31-187
7.14e-42
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA which binds to outer-membrane specific lipoproteins and transports them from inner membrane to outer membrane (OM) through LolB, a lipoprotein anchored to outer membranes. 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 OM-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. Studies have shown that hydrophobic surface patches large enough to accommodate acyl chains of the OM lipoproteins and the structural flexibility of LolA are important factors for its role as a periplasmic chaperone.
Pssm-ID: 319983 Cd Length: 166 Bit Score: 139.11 E-value: 7.14e-42
periplasmic chaperone LolA; This protein, LolA, is known so far only in the gamma and beta ...
32-207
7.03e-20
periplasmic chaperone LolA; This protein, LolA, is known so far only in the gamma and beta subdivisions of the Proteobacteria. The E. coli major outer lipoprotein (Lpp) of E. coli is released from the inner membrane as a complex with this chaperone in an energy-requiring process, and is then delivered to LolB for insertion into the outer membrane. LolA is involved in the delivery of lipoproteins generally, rather than just Lpp, and is an essential protein in E. coli, unlike Lpp itself. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129638 Cd Length: 204 Bit Score: 83.56 E-value: 7.03e-20
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA which ...
31-187
7.14e-42
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA which binds to outer-membrane specific lipoproteins and transports them from inner membrane to outer membrane (OM) through LolB, a lipoprotein anchored to outer membranes. 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 OM-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. Studies have shown that hydrophobic surface patches large enough to accommodate acyl chains of the OM lipoproteins and the structural flexibility of LolA are important factors for its role as a periplasmic chaperone.
Pssm-ID: 319983 Cd Length: 166 Bit Score: 139.11 E-value: 7.14e-42
periplasmic chaperone LolA; This protein, LolA, is known so far only in the gamma and beta ...
32-207
7.03e-20
periplasmic chaperone LolA; This protein, LolA, is known so far only in the gamma and beta subdivisions of the Proteobacteria. The E. coli major outer lipoprotein (Lpp) of E. coli is released from the inner membrane as a complex with this chaperone in an energy-requiring process, and is then delivered to LolB for insertion into the outer membrane. LolA is involved in the delivery of lipoproteins generally, rather than just Lpp, and is an essential protein in E. coli, unlike Lpp itself. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129638 Cd Length: 204 Bit Score: 83.56 E-value: 7.03e-20
family containing periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
83-179
3.86e-05
family containing periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the N-terminal domain of 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: 319982 Cd Length: 162 Bit Score: 42.46 E-value: 3.86e-05
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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