MSRA_ECOLI
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 03-AUG-2022, entry version 131.
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; Proteobacteria; 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 PDBsum; 1FF3; -.
DR PDBsum; 2GT3; -.
DR PDBsum; 2IEM; -.
DR PDBsum; 6YEV; -.
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; P0A744; -.
DR PRIDE; P0A744; -.
DR EnsemblBacteria; AAC77176; AAC77176; b4219.
DR EnsemblBacteria; BAE78220; BAE78220; BAE78220.
DR GeneID; 58463647; -.
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; AGPFYYA; -.
DR PhylomeDB; P0A744; -.
DR BioCyc; EcoCyc:EG11433-MON; -.
DR BioCyc; MetaCyc:EG11433-MON; -.
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:0030091; P:protein repair; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 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 137..139
FT /evidence="ECO:0007829|PDB:6YEV"
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"
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
