ID   MSRA_ECOLI              Reviewed;         212 AA.
AC   P0A744; P27110; Q2M686;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE            Short=Protein-methionine-S-oxide reductase;
DE            EC=1.8.4.11 {ECO:0000269|PubMed:10964927};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=msrA; Synonyms=pms; OrderedLocusNames=b4219, JW4178;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-30.
RC   STRAIN=B;
RX   PubMed=1386361; DOI=10.1016/s0021-9258(19)49570-7;
RA   Rahman M.A., Nelson H., Weissbach H., Brot N.;
RT   "Cloning, sequencing, and expression of the Escherichia coli peptide
RT   methionine sulfoxide reductase gene.";
RL   J. Biol. Chem. 267:15549-15551(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, DISULFIDE BOND, AND MUTAGENESIS
RP   OF CYS-52; CYS-87; CYS-199 AND CYS-207.
RX   PubMed=10964927; DOI=10.1074/jbc.m006137200;
RA   Boschi-Muller S., Azza S., Sanglier-Cianferani S., Talfournier F.,
RA   van Dorsselaer A., Branlant G.;
RT   "A sulfenic acid enzyme intermediate is involved in the catalytic mechanism
RT   of peptide methionine sulfoxide reductase from Escherichia coli.";
RL   J. Biol. Chem. 275:35908-35913(2000).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=11080639; DOI=10.1016/s0969-2126(00)00526-8;
RA   Tete-Favier F., Cobessi D., Boschi-Muller S., Azza S., Branlant G.,
RA   Aubry A.;
RT   "Crystal structure of the Escherichia coli peptide methionine sulphoxide
RT   reductase at 1.9-A resolution.";
RL   Structure 8:1167-1178(2000).
CC   -!- FUNCTION: Could have an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins to
CC       methionine. {ECO:0000269|PubMed:10964927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC         Evidence={ECO:0000269|PubMed:10964927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11;
CC         Evidence={ECO:0000269|PubMed:10964927};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; M89992; AAA24399.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97115.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77176.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78220.1; -; Genomic_DNA.
DR   PIR; S56444; S56444.
DR   RefSeq; NP_418640.1; NC_000913.3.
DR   RefSeq; WP_001295196.1; NZ_STEB01000013.1.
DR   PDB; 1FF3; X-ray; 1.90 A; A/B/C=2-212.
DR   PDB; 2GT3; NMR; -; A=1-212.
DR   PDB; 2IEM; NMR; -; A=2-212.
DR   PDB; 6YEV; X-ray; 2.94 A; A/B/C/D=1-212.
DR   PDB; 7OT4; X-ray; 2.19 A; A/B=1-212.
DR   PDBsum; 1FF3; -.
DR   PDBsum; 2GT3; -.
DR   PDBsum; 2IEM; -.
DR   PDBsum; 6YEV; -.
DR   PDBsum; 7OT4; -.
DR   AlphaFoldDB; P0A744; -.
DR   SMR; P0A744; -.
DR   BioGRID; 4259307; 41.
DR   BioGRID; 853026; 1.
DR   IntAct; P0A744; 4.
DR   STRING; 511145.b4219; -.
DR   jPOST; P0A744; -.
DR   PaxDb; 511145-b4219; -.
DR   EnsemblBacteria; AAC77176; AAC77176; b4219.
DR   GeneID; 75202459; -.
DR   GeneID; 948734; -.
DR   KEGG; ecj:JW4178; -.
DR   KEGG; eco:b4219; -.
DR   PATRIC; fig|1411691.4.peg.2482; -.
DR   EchoBASE; EB1403; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_3_6; -.
DR   InParanoid; P0A744; -.
DR   OMA; YCPVHAT; -.
DR   OrthoDB; 4174719at2; -.
DR   PhylomeDB; P0A744; -.
DR   BioCyc; EcoCyc:EG11433-MONOMER; -.
DR   BioCyc; MetaCyc:EG11433-MONOMER; -.
DR   BRENDA; 1.8.4.11; 2026.
DR   EvolutionaryTrace; P0A744; -.
DR   PRO; PR:P0A744; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IDA:EcoCyc.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IMP:EcoCyc.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:EcoCyc.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IDA:EcoCyc.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR   Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   PANTHER; PTHR42799; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR42799:SF2; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1386361"
FT   CHAIN           2..212
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_0000138546"
FT   ACT_SITE        52
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   DISULFID        52..199
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   DISULFID        199..207
FT                   /note="Redox-active; alternate"
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   MUTAGEN         52
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   MUTAGEN         87
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   MUTAGEN         199
FT                   /note="C->S: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   MUTAGEN         207
FT                   /note="C->S: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10964927"
FT   HELIX           6..8
FT                   /evidence="ECO:0007829|PDB:6YEV"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   HELIX           53..61
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          66..77
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   HELIX           83..88
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:2IEM"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   HELIX           108..117
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          123..127
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:7OT4"
FT   HELIX           144..163
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:1FF3"
FT   STRAND          200..203
FT                   /evidence="ECO:0007829|PDB:7OT4"
SQ   SEQUENCE   212 AA;  23315 MW;  B9DC86DC1203BD32 CRC64;
     MSLFDKKHLV SPADALPGRN TPMPVATLHA VNGHSMTNVP DGMEIAIFAM GCFWGVERLF
     WQLPGVYSTA AGYTGGYTPN PTYREVCSGD TGHAEAVRIV YDPSVISYEQ LLQVFWENHD
     PAQGMRQGND HGTQYRSAIY PLTPEQDAAA RASLERFQAA MLAADDDRHI TTEIANATPF
     YYAEDDHQQY LHKNPYGYCG IGGIGVCLPP EA
//