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P0A744

- MSRA_ECOLI

UniProt

P0A744 - MSRA_ECOLI

Protein

Peptide methionine sulfoxide reductase MsrA

Gene

msrA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.

    Catalytic activityi

    Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
    L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediate

    GO - Molecular functioni

    1. peptide-methionine (S)-S-oxide reductase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB-HAMAP
    2. protein repair Source: InterPro
    3. response to oxidative stress Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11433-MONOMER.
    ECOL316407:JW4178-MONOMER.
    MetaCyc:EG11433-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide methionine sulfoxide reductase MsrA (EC:1.8.4.11)
    Short name:
    Protein-methionine-S-oxide reductase
    Alternative name(s):
    Peptide-methionine (S)-S-oxide reductase
    Short name:
    Peptide Met(O) reductase
    Gene namesi
    Name:msrA
    Synonyms:pms
    Ordered Locus Names:b4219, JW4178
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11433. msrA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521C → S: Loss of activity. 1 Publication
    Mutagenesisi87 – 871C → S: No effect. 1 Publication
    Mutagenesisi199 – 1991C → S: Decrease in activity. 1 Publication
    Mutagenesisi207 – 2071C → S: Decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 212211Peptide methionine sulfoxide reductase MsrAPRO_0000138546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 199Redox-active; alternateCurated
    Disulfide bondi199 ↔ 207Redox-active; alternateCurated

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP0A744.
    PRIDEiP0A744.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A744.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    lrpP0ACJ01EBI-1129240,EBI-1113316

    Protein-protein interaction databases

    IntActiP0A744. 4 interactions.
    STRINGi511145.b4219.

    Structurei

    Secondary structure

    1
    212
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 143
    Turni30 – 323
    Beta strandi35 – 373
    Beta strandi44 – 496
    Helixi53 – 619
    Beta strandi66 – 7712
    Helixi83 – 886
    Beta strandi89 – 913
    Beta strandi94 – 1018
    Turni103 – 1053
    Helixi108 – 11710
    Beta strandi123 – 1275
    Beta strandi130 – 1323
    Helixi133 – 1353
    Beta strandi138 – 1403
    Helixi144 – 16320
    Beta strandi180 – 1823
    Helixi185 – 1873
    Helixi190 – 1934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FF3X-ray1.90A/B/C2-212[»]
    2GT3NMR-A1-212[»]
    2IEMNMR-A2-212[»]
    ProteinModelPortaliP0A744.
    SMRiP0A744. Positions 2-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A744.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0225.
    HOGENOMiHOG000263862.
    KOiK07304.
    OMAiNVEFAIF.
    OrthoDBiEOG6091JX.
    PhylomeDBiP0A744.

    Family and domain databases

    Gene3Di3.30.1060.10. 1 hit.
    HAMAPiMF_01401. MsrA.
    InterProiIPR028427. Met_Sox_Rdtase.
    IPR002569. Met_Sox_Rdtase_MsrA.
    [Graphical view]
    PANTHERiPTHR10173. PTHR10173. 1 hit.
    PfamiPF01625. PMSR. 1 hit.
    [Graphical view]
    SUPFAMiSSF55068. SSF55068. 1 hit.
    TIGRFAMsiTIGR00401. msrA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A744-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLFDKKHLV SPADALPGRN TPMPVATLHA VNGHSMTNVP DGMEIAIFAM    50
    GCFWGVERLF WQLPGVYSTA AGYTGGYTPN PTYREVCSGD TGHAEAVRIV 100
    YDPSVISYEQ LLQVFWENHD PAQGMRQGND HGTQYRSAIY PLTPEQDAAA 150
    RASLERFQAA MLAADDDRHI TTEIANATPF YYAEDDHQQY LHKNPYGYCG 200
    IGGIGVCLPP EA 212
    Length:212
    Mass (Da):23,315
    Last modified:January 23, 2007 - v2
    Checksum:iB9DC86DC1203BD32
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M89992 Genomic DNA. Translation: AAA24399.1.
    U14003 Genomic DNA. Translation: AAA97115.1.
    U00096 Genomic DNA. Translation: AAC77176.1.
    AP009048 Genomic DNA. Translation: BAE78220.1.
    PIRiS56444.
    RefSeqiNP_418640.1. NC_000913.3.
    YP_492361.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77176; AAC77176; b4219.
    BAE78220; BAE78220; BAE78220.
    GeneIDi12930313.
    948734.
    KEGGiecj:Y75_p4105.
    eco:b4219.
    PATRICi32124013. VBIEscCol129921_4351.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M89992 Genomic DNA. Translation: AAA24399.1 .
    U14003 Genomic DNA. Translation: AAA97115.1 .
    U00096 Genomic DNA. Translation: AAC77176.1 .
    AP009048 Genomic DNA. Translation: BAE78220.1 .
    PIRi S56444.
    RefSeqi NP_418640.1. NC_000913.3.
    YP_492361.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FF3 X-ray 1.90 A/B/C 2-212 [» ]
    2GT3 NMR - A 1-212 [» ]
    2IEM NMR - A 2-212 [» ]
    ProteinModelPortali P0A744.
    SMRi P0A744. Positions 2-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A744. 4 interactions.
    STRINGi 511145.b4219.

    Proteomic databases

    PaxDbi P0A744.
    PRIDEi P0A744.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77176 ; AAC77176 ; b4219 .
    BAE78220 ; BAE78220 ; BAE78220 .
    GeneIDi 12930313.
    948734.
    KEGGi ecj:Y75_p4105.
    eco:b4219.
    PATRICi 32124013. VBIEscCol129921_4351.

    Organism-specific databases

    EchoBASEi EB1403.
    EcoGenei EG11433. msrA.

    Phylogenomic databases

    eggNOGi COG0225.
    HOGENOMi HOG000263862.
    KOi K07304.
    OMAi NVEFAIF.
    OrthoDBi EOG6091JX.
    PhylomeDBi P0A744.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11433-MONOMER.
    ECOL316407:JW4178-MONOMER.
    MetaCyc:EG11433-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A744.
    PROi P0A744.

    Gene expression databases

    Genevestigatori P0A744.

    Family and domain databases

    Gene3Di 3.30.1060.10. 1 hit.
    HAMAPi MF_01401. MsrA.
    InterProi IPR028427. Met_Sox_Rdtase.
    IPR002569. Met_Sox_Rdtase_MsrA.
    [Graphical view ]
    PANTHERi PTHR10173. PTHR10173. 1 hit.
    Pfami PF01625. PMSR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55068. SSF55068. 1 hit.
    TIGRFAMsi TIGR00401. msrA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene."
      Rahman M.A., Nelson H., Weissbach H., Brot N.
      J. Biol. Chem. 267:15549-15551(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30.
      Strain: B.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli."
      Boschi-Muller S., Azza S., Sanglier-Cianferani S., Talfournier F., van Dorsselaer A., Branlant G.
      J. Biol. Chem. 275:35908-35913(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-52; CYS-87; CYS-199 AND CYS-207.
    6. "Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9-A resolution."
      Tete-Favier F., Cobessi D., Boschi-Muller S., Azza S., Branlant G., Aubry A.
      Structure 8:1167-1178(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

    Entry informationi

    Entry nameiMSRA_ECOLI
    AccessioniPrimary (citable) accession number: P0A744
    Secondary accession number(s): P27110, Q2M686
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3