MATE (multidrug and toxic compound extrusion) family efflux transporter functions in protecting cells against oxidative stress and bile salts and may be part of the SOS system
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane ...
27-483
1.66e-108
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.
The actual alignment was detected with superfamily member pfam03023:
Pssm-ID: 447704 [Multi-domain] Cd Length: 451 Bit Score: 329.64 E-value: 1.66e-108
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of ...
27-483
1.66e-108
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride ion in the central cavity and a zinc ion at the beginning of TM 7 might be functionally important.
Pssm-ID: 397249 [Multi-domain] Cd Length: 451 Bit Score: 329.64 E-value: 1.66e-108
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
10-439
9.54e-106
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240528 [Multi-domain] Cd Length: 420 Bit Score: 321.32 E-value: 9.54e-106
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously ...
2-433
8.25e-77
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously MviN), a family of integral membrane proteins predicted to have ten or more transmembrane regions. Members have been suggested to act as a lipid II flippase, translocated a precursor of murein. However, it appears FtsW has that activity. Flippase activity for MurJ has not been shown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273763 [Multi-domain] Cd Length: 502 Bit Score: 249.16 E-value: 8.25e-77
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of ...
27-483
1.66e-108
Lipid II flippase MurJ; Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride ion in the central cavity and a zinc ion at the beginning of TM 7 might be functionally important.
Pssm-ID: 397249 [Multi-domain] Cd Length: 451 Bit Score: 329.64 E-value: 1.66e-108
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
10-439
9.54e-106
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240528 [Multi-domain] Cd Length: 420 Bit Score: 321.32 E-value: 9.54e-106
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously ...
2-433
8.25e-77
murein biosynthesis integral membrane protein MurJ; This model represents MurJ (previously MviN), a family of integral membrane proteins predicted to have ten or more transmembrane regions. Members have been suggested to act as a lipid II flippase, translocated a precursor of murein. However, it appears FtsW has that activity. Flippase activity for MurJ has not been shown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273763 [Multi-domain] Cd Length: 502 Bit Score: 249.16 E-value: 8.25e-77
Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
2-436
6.31e-07
Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli Wzx and related proteins from other gram-negative bacteria are thought to act as flippases, assisting in the membrane translocation of lipopolysaccharides including those containing O-antigens. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240533 [Multi-domain] Cd Length: 402 Bit Score: 51.39 E-value: 6.31e-07
Stage V sporulation protein B, also known as Stage III sporulation protein F, and related ...
204-412
2.51e-05
Stage V sporulation protein B, also known as Stage III sporulation protein F, and related proteins; The integral membrane protein SpoVB has been implicated in the biosynthesis of the peptidoglycan component of the spore cortex in Bacillus subtilis. This model represents a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).
Pssm-ID: 240529 [Multi-domain] Cd Length: 434 Bit Score: 46.69 E-value: 2.51e-05
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane ...
11-406
3.01e-03
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.
Pssm-ID: 240527 [Multi-domain] Cd Length: 420 Bit Score: 40.00 E-value: 3.01e-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).
Modify your query to search against a different database and/or use advanced search options
