zinc-dependent metallopeptidase similar to DgsA anti-repressor MtfA that functions as a regulator of the phosphoenolpyruvate (PEP)-dependent:glucose phosphotransferase system (ptsG) by binding and inactivating DgsA (aka Mlc), a repressor of ptsG; belongs to the M90 peptidase family
Glucose-regulated metallo-peptidase M90; MtfA (earlier known as YeeI) is a transcription ...
5-257
1.56e-89
Glucose-regulated metallo-peptidase M90; MtfA (earlier known as YeeI) is a transcription factor A that binds Mlc (make large colonies), itself a repressor of glucose and hence a protein important in regulation of the phosphoenolpyruvate:glucose-phosphotransferase (ptsG) system, the major glucose transporter in E.coli. Mlc is a repressor of ptsG, and MtfA is found to bind and inactivate Mlc with high affinity. The membrane-bound protein EIICBGlc encoded by the ptsG gene is the major glucose transporter in Escherichia coli. MtfA is found to be a glucose-regulated peptidase, whose activity is regulated by binding to Mlc available in the cytoplasm, which in turn has been released from EIICBGlc during times when no glucose is taken up. A physiologically relevant target for this peptidase is not yet known.
Pssm-ID: 428801 Cd Length: 243 Bit Score: 265.54 E-value: 1.56e-89
Mlc titration factor A (MtfA) is a zinc metallopeptidase (M90 peptidase); This subfamily ...
44-256
1.60e-76
Mlc titration factor A (MtfA) is a zinc metallopeptidase (M90 peptidase); This subfamily includes the Mlc Titration Factor A (MtfA; also known as YeeI or DgsA anti-repressor MtfA) which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). It can cleave synthetic substrates of both carboxypeptidases and aminopeptidases, with strongest activity towards the latter. Its biologically relevant substrate has yet to be identified. Although it interacts with the transcription repressor Mlc, it does not cleave it. However, Mlc seems to activate the peptidase activity of MtfA. MtfA is related to the catalytic domain of the anthrax lethal factor which is a zinc-dependent metalloprotease, targeting mitogen-activated protein kinase kinases (MAPKKs), and resulting in apoptosis, as well as the Mop (modulation of pathogenesis) protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site.
Pssm-ID: 380912 Cd Length: 208 Bit Score: 230.88 E-value: 1.60e-76
Glucose-regulated metallo-peptidase M90; MtfA (earlier known as YeeI) is a transcription ...
5-257
1.56e-89
Glucose-regulated metallo-peptidase M90; MtfA (earlier known as YeeI) is a transcription factor A that binds Mlc (make large colonies), itself a repressor of glucose and hence a protein important in regulation of the phosphoenolpyruvate:glucose-phosphotransferase (ptsG) system, the major glucose transporter in E.coli. Mlc is a repressor of ptsG, and MtfA is found to bind and inactivate Mlc with high affinity. The membrane-bound protein EIICBGlc encoded by the ptsG gene is the major glucose transporter in Escherichia coli. MtfA is found to be a glucose-regulated peptidase, whose activity is regulated by binding to Mlc available in the cytoplasm, which in turn has been released from EIICBGlc during times when no glucose is taken up. A physiologically relevant target for this peptidase is not yet known.
Pssm-ID: 428801 Cd Length: 243 Bit Score: 265.54 E-value: 1.56e-89
Mlc titration factor A (MtfA) is a zinc metallopeptidase (M90 peptidase); This subfamily ...
44-256
1.60e-76
Mlc titration factor A (MtfA) is a zinc metallopeptidase (M90 peptidase); This subfamily includes the Mlc Titration Factor A (MtfA; also known as YeeI or DgsA anti-repressor MtfA) which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). It can cleave synthetic substrates of both carboxypeptidases and aminopeptidases, with strongest activity towards the latter. Its biologically relevant substrate has yet to be identified. Although it interacts with the transcription repressor Mlc, it does not cleave it. However, Mlc seems to activate the peptidase activity of MtfA. MtfA is related to the catalytic domain of the anthrax lethal factor which is a zinc-dependent metalloprotease, targeting mitogen-activated protein kinase kinases (MAPKKs), and resulting in apoptosis, as well as the Mop (modulation of pathogenesis) protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site.
Pssm-ID: 380912 Cd Length: 208 Bit Score: 230.88 E-value: 1.60e-76
uncharacterized M90 peptidase family-like proteins; This subfamily contains uncharacterized ...
47-254
8.50e-19
uncharacterized M90 peptidase family-like proteins; This subfamily contains uncharacterized M90 peptidase-like domains, similar to the Mlc Titration Factor A (MtfA) peptidase from Escherichia coli, also known as the YeeI gene product, which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). E. coli MtfA has been shown to have aminopeptidase activity with the presence of a single zinc ion in the active site ligated by two histidines in an HEXXH motif. MtfA is related to the catalytic domain of the anthrax lethal factor and the Mop protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site.
Pssm-ID: 380913 Cd Length: 210 Bit Score: 82.16 E-value: 8.50e-19
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).
Modify your query to search against a different database and/or use advanced search options
