MlaD family protein similar to MlaD, which is a component of the Mla pathway, an ABC transport system that functions to maintain the asymmetry of the outer membrane, and to mce (mammalian cell entry) proteins from Mycobacterium tuberculosis, virulence proteins required for invasion of non-phagocytic cells
virulence factor Mce family protein; Members of this paralogous family are found as six tandem ...
22-301
1.77e-32
virulence factor Mce family protein; Members of this paralogous family are found as six tandem homologous proteins in the same orientation per cassette, in four separate cassettes in Mycobacterium tuberculosis. The six members of each cassette represent six subfamilies. One subfamily includes the protein mce (mycobacterial cell entry), a virulence protein required for invasion of non-phagocytic cells. [Cellular processes, Pathogenesis]
Pssm-ID: 273384 [Multi-domain] Cd Length: 291 Bit Score: 123.94 E-value: 1.77e-32
MlaD protein; This family of proteins contains MlaD, which is a component of the Mla pathway, ...
52-126
8.87e-12
MlaD protein; This family of proteins contains MlaD, which is a component of the Mla pathway, an ABC transport system that functions to maintain the asymmetry of the outer membrane. The family also contains the mce (mammalian cell entry) proteins from Mycobacterium tuberculosis. The archetype (Rv0169), was isolated as being necessary for colonization of, and survival within, the macrophage. This family contains proteins of unknown function from other bacteria.
Pssm-ID: 426790 [Multi-domain] Cd Length: 81 Bit Score: 60.67 E-value: 8.87e-12
virulence factor Mce family protein; Members of this paralogous family are found as six tandem ...
22-301
1.77e-32
virulence factor Mce family protein; Members of this paralogous family are found as six tandem homologous proteins in the same orientation per cassette, in four separate cassettes in Mycobacterium tuberculosis. The six members of each cassette represent six subfamilies. One subfamily includes the protein mce (mycobacterial cell entry), a virulence protein required for invasion of non-phagocytic cells. [Cellular processes, Pathogenesis]
Pssm-ID: 273384 [Multi-domain] Cd Length: 291 Bit Score: 123.94 E-value: 1.77e-32
MlaD protein; This family of proteins contains MlaD, which is a component of the Mla pathway, ...
52-126
8.87e-12
MlaD protein; This family of proteins contains MlaD, which is a component of the Mla pathway, an ABC transport system that functions to maintain the asymmetry of the outer membrane. The family also contains the mce (mammalian cell entry) proteins from Mycobacterium tuberculosis. The archetype (Rv0169), was isolated as being necessary for colonization of, and survival within, the macrophage. This family contains proteins of unknown function from other bacteria.
Pssm-ID: 426790 [Multi-domain] Cd Length: 81 Bit Score: 60.67 E-value: 8.87e-12
outer membrane lipid asymmetry maintenance protein MlaD; Members of this protein family are ...
23-156
1.80e-10
outer membrane lipid asymmetry maintenance protein MlaD; Members of this protein family are the MlaD (maintenance of Lipid Asymmetry D) protein of an ABC transport system that seems to remove phospholipid from the outer leaflet of the Gram-negative bacterial outer membrane (OM), leaving only lipopolysaccharide in the outer leaflet. The Mla locus has long been associated with toluene tolerance, consistent with the proposed role in retrograde transport of phospholipid and therefore with maintaining the integrity of the OM as a protective barrier.
Pssm-ID: 275223 [Multi-domain] Cd Length: 146 Bit Score: 58.64 E-value: 1.80e-10
Cholesterol uptake porter CUP1 of Mce4, putative; Mce4_CUP1 is a family of putative Mce4 ...
134-300
9.82e-03
Cholesterol uptake porter CUP1 of Mce4, putative; Mce4_CUP1 is a family of putative Mce4 transporters of cholesterol. The domain is found associated with pfam02470. The full TCDB classification for this family in conjunction with PF02470 is TC:3.A.1.27.4.
Pssm-ID: 432164 Cd Length: 222 Bit Score: 37.16 E-value: 9.82e-03
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
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
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).
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