outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and ...
5-206
4.40e-111
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and beta subdivisions of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. It is required in E. coli for insertion of the major outer lipoprotein (Lpp) into the outer membrane. Lpp is transferred to LolB from the carrier protein LolA in the periplasm. Previously, this protein was thought to play in role in 5-aminolevulinic acid synthesis and was designated HemM. [Protein fate, Protein and peptide secretion and trafficking]
:
Pssm-ID: 129639 Cd Length: 202 Bit Score: 316.14 E-value: 4.40e-111
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and ...
5-206
4.40e-111
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and beta subdivisions of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. It is required in E. coli for insertion of the major outer lipoprotein (Lpp) into the outer membrane. Lpp is transferred to LolB from the carrier protein LolA in the periplasm. Previously, this protein was thought to play in role in 5-aminolevulinic acid synthesis and was designated HemM. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129639 Cd Length: 202 Bit Score: 316.14 E-value: 4.40e-111
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane ...
41-204
2.52e-53
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane lipoprotein receptor, LolB, which catalyzes the last step of lipoprotein transfer from the inner to the outer membrane. 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 transports lipoproteins through the periplasm to LolB, which then localizes them to outer membranes; the protruding loop of LolB has been shown to be essential for the localization of lipoproteins in the anchoring of bacterial triacylated proteins to the outer membrane.
Pssm-ID: 319984 Cd Length: 163 Bit Score: 168.17 E-value: 2.52e-53
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and ...
5-206
4.40e-111
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and beta subdivisions of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. It is required in E. coli for insertion of the major outer lipoprotein (Lpp) into the outer membrane. Lpp is transferred to LolB from the carrier protein LolA in the periplasm. Previously, this protein was thought to play in role in 5-aminolevulinic acid synthesis and was designated HemM. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129639 Cd Length: 202 Bit Score: 316.14 E-value: 4.40e-111
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane ...
41-204
2.52e-53
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane lipoprotein receptor, LolB, which catalyzes the last step of lipoprotein transfer from the inner to the outer membrane. 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 transports lipoproteins through the periplasm to LolB, which then localizes them to outer membranes; the protruding loop of LolB has been shown to be essential for the localization of lipoproteins in the anchoring of bacterial triacylated proteins to the outer membrane.
Pssm-ID: 319984 Cd Length: 163 Bit Score: 168.17 E-value: 2.52e-53
family containing periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
51-206
6.01e-23
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: 90.23 E-value: 6.01e-23
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
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
(labeled illustration) or all hits
(labeled illustration).
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),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
