Summary: MatE
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This is the Wikipedia entry entitled "Multi antimicrobial extrusion protein". More...
Multi antimicrobial extrusion protein Edit Wikipedia article
| Multi antimicrobial extrusion protein | |||||||||
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| Identifiers | |||||||||
| Symbol | MatE | ||||||||
| Pfam | PF01554 | ||||||||
| Pfam clan | CL0222 | ||||||||
| InterPro | IPR002528 | ||||||||
| TCDB | 2.A.66 | ||||||||
| OPM superfamily | 249 | ||||||||
| OPM protein | 3mkt | ||||||||
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Multi antimicrobial extrusion protein (MATE) also known as multidrug and toxin extrusion or multidrug and toxic compound extrusion is a family of proteins which function as drug/sodium or proton antiporters.[1][2][3]
Contents |
[edit] Function
The MATE proteins in bacteria, archaea and eukaryotes function as fundamental transporters of metabolic and xenobiotic organic cations.[2][3]
[edit] Structure
These proteins are predicted to have 12 alpha-helical transmembrane regions, some of the animal proteins may have an additional C-terminal helix.[4] The X-ray structure of the NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter.[5]
[edit] Discovery
The multidrug efflux transporter NorM from V. parahaemolyticus which mediates resistance to multiple antimicrobial agents (norfloxacin, kanamycin, ethidium bromide etc.) and its homologue from E. coli were identified in 1998.[6] NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter discovered.[7] NorM is a prototype of a new transporter family and Brown et al. named it the multidrug and toxic compound extrusion family.[1] NorM is nicknamed "Last of the multidrug transporters" because it is the last multidrug transporter discovered functionally as well as structurally.[8]
[edit] Genes
The following human genes encode MATE proteins:
[edit] See also
[edit] References
- ^ a b Brown MH, Paulsen IT, Skurray RA (January 1999). "The multidrug efflux protein NorM is a prototype of a new family of transporters". Mol. Microbiol. 31 (1): 394–5. doi:10.1046/j.1365-2958.1999.01162.x. PMID 9987140.
- ^ a b Kuroda T, Tsuchiya T (December 2008). "Multidrug efflux transporters in the MATE family". Biochim. Biophys. Acta 1794 (5): 763–8. doi:10.1016/j.bbapap.2008.11.012. PMID 19100867.
- ^ a b Omote H et al. (2006). "The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations". Trends in pharmacological sciences 27 (11): 587–93. doi:10.1016/j.tips.2006.09.001. PMID 16996621.
- ^ Hvorup RN, Winnen B, Chang AB, Jiang Y, Zhou XF, Saier MH (March 2003). "The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter superfamily". Eur. J. Biochem. 270 (5): 799–813. doi:10.1046/j.1432-1033.2003.03418.x. PMID 12603313.
- ^ He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G (2010). "Structure of a Cation-bound Multidrug and Toxic Compound Extrusion Transporter". Nature 467 (7318): 991–994. doi:10.1038/nature09408. PMC 3152480. PMID 20861838. //www.ncbi.nlm.nih.gov/pmc/articles/PMC3152480/.
- ^ Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T (July 1998). "NorM, a Putative Multidrug Efflux Protein, of Vibrio parahaemolyticus and Its Homolog in Escherichia coli". Antimicrob. Agents Chemother. 42 (7): 1778–82. PMC 105682. PMID 9661020. //www.ncbi.nlm.nih.gov/pmc/articles/PMC105682/.
- ^ Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T (December 2000). "NorM of Vibrio parahaemolyticus Is an Na+-Driven Multidrug Efflux Pump". J. Bacteriol. 182 (23): 6694–7. doi:10.1128/JB.182.23.6694-6697.2000. PMC 111412. PMID 11073914. //www.ncbi.nlm.nih.gov/pmc/articles/PMC111412/.
- ^ van Veen HW (2010). "Structural biology: Last of the multidrug transporters". Nature 467 (7318): 926–7. doi:10.1038/467926a. PMID 20962836.
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This article incorporates text from the public domain Pfam and InterPro IPR002528
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
MatE Provide feedback
The MatE domain
Internal database links
| Similarity to PfamA using HHSearch: | MVIN |
External database links
| PANDIT: | PF01554 |
| Pseudofam: | PF01554 |
| SYSTERS: | MatE |
| Transporter classification: | 2.A.66 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002528
Characterised members of the Multi Antimicrobial Extrusion (MATE) family function as drug/sodium antiporters. These proteins mediate resistance to a wide range of cationic dyes, fluroquinolones, aminoglycosides and other structurally diverse antibodies and drugs. MATE proteins are found in bacteria, archaea and eukaryotes. These proteins are predicted to have 12 alpha-helical transmembrane regions, some of the animal proteins may have an additional C-terminal helix.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | membrane (GO:0016020) |
| Molecular function | drug transmembrane transporter activity (GO:0015238) |
| antiporter activity (GO:0015297) | |
| Biological process | transmembrane transport (GO:0055085) |
| drug transmembrane transport (GO:0006855) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan MviN_MATE (CL0222), which contains the following 6 members:
MatE MVIN Polysacc_synt Polysacc_synt_3 Polysacc_synt_C Rft-1Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (58) |
Full (32381) |
Representative proteomes | NCBI (28954) |
Meta (6802) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (2610) |
RP35 (5153) |
RP55 (6676) |
RP75 (7913) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (58) |
Full (32381) |
Representative proteomes | NCBI (28954) |
Meta (6802) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (2610) |
RP35 (5153) |
RP55 (6676) |
RP75 (7913) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_163 (release 4.0) |
| Previous IDs: | UPF0013; |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 58 |
| Number in full: | 32381 |
| Average length of the domain: | 160.40 aa |
| Average identity of full alignment: | 16 % |
| Average coverage of the sequence by the domain: | 68.74 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 162 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MatE domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence