FtsW/RodA/SpoVE family cell cycle protein similar to peptidoglycan glycosyltransferases FtsW that is essential for cell division and RodA that is involved in peptidoglycan cell wall formation
cell division protein FtsW; This family consists of FtsW, an integral membrane protein with ...
18-364
2.01e-111
cell division protein FtsW; This family consists of FtsW, an integral membrane protein with ten transmembrane segments. In general, it is one of two paralogs involved in peptidoglycan biosynthesis, the other being RodA, and is essential for cell division. All members of the seed alignment for this model are encoded in operons for the biosynthesis of UDP-N-acetylmuramoyl-pentapeptide, a precursor of murein (peptidoglycan). The FtsW designation is not used in endospore-forming bacterial (e.g. Bacillus subtilis), where the member of this family is designated SpoVE and three or more RodA/FtsW/SpoVE family paralogs are present. SpoVE acts in spore cortex formation and is dispensible for growth. Biological rolls for FtsW in cell division include recruitment of penicillin-binding protein 3 to the division site. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division]
Pssm-ID: 274232 Cd Length: 356 Bit Score: 329.91 E-value: 2.01e-111
rod shape-determining protein RodA; Proteins of this family are members of the FtsW/RodA/SpoVE ...
25-349
4.83e-22
rod shape-determining protein RodA; Proteins of this family are members of the FtsW/RodA/SpoVE superfamily. It has been reported that RodA proteins play important roles in maintaining cell shape and antibiotic resistance in bacteria.
Pssm-ID: 411566 Cd Length: 415 Bit Score: 96.89 E-value: 4.83e-22
cell division protein FtsW; This family consists of FtsW, an integral membrane protein with ...
18-364
2.01e-111
cell division protein FtsW; This family consists of FtsW, an integral membrane protein with ten transmembrane segments. In general, it is one of two paralogs involved in peptidoglycan biosynthesis, the other being RodA, and is essential for cell division. All members of the seed alignment for this model are encoded in operons for the biosynthesis of UDP-N-acetylmuramoyl-pentapeptide, a precursor of murein (peptidoglycan). The FtsW designation is not used in endospore-forming bacterial (e.g. Bacillus subtilis), where the member of this family is designated SpoVE and three or more RodA/FtsW/SpoVE family paralogs are present. SpoVE acts in spore cortex formation and is dispensible for growth. Biological rolls for FtsW in cell division include recruitment of penicillin-binding protein 3 to the division site. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division]
Pssm-ID: 274232 Cd Length: 356 Bit Score: 329.91 E-value: 2.01e-111
rod shape-determining protein RodA; This protein is a member of the FtsW/RodA/SpoVE family ...
18-365
4.82e-73
rod shape-determining protein RodA; This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division]
Pssm-ID: 274033 Cd Length: 352 Bit Score: 231.25 E-value: 4.82e-73
rod shape-determining protein RodA; Proteins of this family are members of the FtsW/RodA/SpoVE ...
25-349
4.83e-22
rod shape-determining protein RodA; Proteins of this family are members of the FtsW/RodA/SpoVE superfamily. It has been reported that RodA proteins play important roles in maintaining cell shape and antibiotic resistance in bacteria.
Pssm-ID: 411566 Cd Length: 415 Bit Score: 96.89 E-value: 4.83e-22
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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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.
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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,
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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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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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