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Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase)

 MSRA_ECOLI              Reviewed;         212 AA.
P0A744; P27110; Q2M686;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 106.
RecName: Full=Peptide methionine sulfoxide reductase MsrA;
Short=Protein-methionine-S-oxide reductase;
EC=1.8.4.11;
AltName: Full=Peptide-methionine (S)-S-oxide reductase;
Short=Peptide Met(O) reductase;
Name=msrA; Synonyms=pms; OrderedLocusNames=b4219, JW4178;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-30.
STRAIN=B;
PubMed=1386361;
Rahman M.A., Nelson H., Weissbach H., Brot N.;
"Cloning, sequencing, and expression of the Escherichia coli peptide
methionine sulfoxide reductase gene.";
J. Biol. Chem. 267:15549-15551(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
MUTAGENESIS OF CYS-52; CYS-87; CYS-199 AND CYS-207.
PubMed=10964927; DOI=10.1074/jbc.M006137200;
Boschi-Muller S., Azza S., Sanglier-Cianferani S., Talfournier F.,
van Dorsselaer A., Branlant G.;
"A sulfenic acid enzyme intermediate is involved in the catalytic
mechanism of peptide methionine sulfoxide reductase from Escherichia
coli.";
J. Biol. Chem. 275:35908-35913(2000).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=11080639; DOI=10.1016/S0969-2126(00)00526-8;
Tete-Favier F., Cobessi D., Boschi-Muller S., Azza S., Branlant G.,
Aubry A.;
"Crystal structure of the Escherichia coli peptide methionine
sulphoxide reductase at 1.9-A resolution.";
Structure 8:1167-1178(2000).
-!- FUNCTION: 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 ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (S)-S-oxide + thioredoxin.
-!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
{ECO:0000305}.
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EMBL; M89992; AAA24399.1; -; Genomic_DNA.
EMBL; U14003; AAA97115.1; -; Genomic_DNA.
EMBL; U00096; AAC77176.1; -; Genomic_DNA.
EMBL; AP009048; BAE78220.1; -; Genomic_DNA.
PIR; S56444; S56444.
RefSeq; NP_418640.1; NC_000913.3.
RefSeq; WP_001295196.1; NZ_LN832404.1.
PDB; 1FF3; X-ray; 1.90 A; A/B/C=2-212.
PDB; 2GT3; NMR; -; A=1-212.
PDB; 2IEM; NMR; -; A=2-212.
PDBsum; 1FF3; -.
PDBsum; 2GT3; -.
PDBsum; 2IEM; -.
ProteinModelPortal; P0A744; -.
SMR; P0A744; -.
BioGrid; 4259307; 41.
IntAct; P0A744; 4.
STRING; 316385.ECDH10B_4414; -.
EPD; P0A744; -.
PaxDb; P0A744; -.
PRIDE; P0A744; -.
EnsemblBacteria; AAC77176; AAC77176; b4219.
EnsemblBacteria; BAE78220; BAE78220; BAE78220.
GeneID; 948734; -.
KEGG; ecj:JW4178; -.
KEGG; eco:b4219; -.
PATRIC; fig|1411691.4.peg.2482; -.
EchoBASE; EB1403; -.
EcoGene; EG11433; msrA.
eggNOG; ENOG4107QXP; Bacteria.
eggNOG; COG0225; LUCA.
HOGENOM; HOG000263862; -.
InParanoid; P0A744; -.
KO; K07304; -.
OMA; MRQGGDI; -.
PhylomeDB; P0A744; -.
BioCyc; EcoCyc:EG11433-MONOMER; -.
BioCyc; MetaCyc:EG11433-MONOMER; -.
BRENDA; 1.8.4.11; 2026.
EvolutionaryTrace; P0A744; -.
PRO; PR:P0A744; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IDA:EcoCyc.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IMP:EcoCyc.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:EcoCyc.
GO; GO:0030091; P:protein repair; IDA:EcoCyc.
GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
Gene3D; 3.30.1060.10; -; 1.
HAMAP; MF_01401; MsrA; 1.
InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
Pfam; PF01625; PMSR; 1.
SUPFAM; SSF55068; SSF55068; 1.
TIGRFAMs; TIGR00401; msrA; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Oxidoreductase; Redox-active center;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1386361}.
CHAIN 2 212 Peptide methionine sulfoxide reductase
MsrA.
/FTId=PRO_0000138546.
ACT_SITE 52 52 Cysteine sulfenic acid (-SOH)
intermediate.
DISULFID 52 199 Redox-active; alternate. {ECO:0000305}.
DISULFID 199 207 Redox-active; alternate. {ECO:0000305}.
MUTAGEN 52 52 C->S: Loss of activity.
{ECO:0000269|PubMed:10964927}.
MUTAGEN 87 87 C->S: No effect.
{ECO:0000269|PubMed:10964927}.
MUTAGEN 199 199 C->S: Decrease in activity.
{ECO:0000269|PubMed:10964927}.
MUTAGEN 207 207 C->S: Decrease in activity.
{ECO:0000269|PubMed:10964927}.
HELIX 12 14 {ECO:0000244|PDB:1FF3}.
TURN 30 32 {ECO:0000244|PDB:1FF3}.
STRAND 35 37 {ECO:0000244|PDB:1FF3}.
STRAND 44 49 {ECO:0000244|PDB:1FF3}.
HELIX 53 61 {ECO:0000244|PDB:1FF3}.
STRAND 66 77 {ECO:0000244|PDB:1FF3}.
HELIX 83 88 {ECO:0000244|PDB:1FF3}.
STRAND 89 91 {ECO:0000244|PDB:2IEM}.
STRAND 94 101 {ECO:0000244|PDB:1FF3}.
TURN 103 105 {ECO:0000244|PDB:1FF3}.
HELIX 108 117 {ECO:0000244|PDB:1FF3}.
STRAND 123 127 {ECO:0000244|PDB:1FF3}.
STRAND 130 132 {ECO:0000244|PDB:1FF3}.
HELIX 133 135 {ECO:0000244|PDB:1FF3}.
STRAND 138 140 {ECO:0000244|PDB:2GT3}.
HELIX 144 163 {ECO:0000244|PDB:1FF3}.
STRAND 180 182 {ECO:0000244|PDB:1FF3}.
HELIX 185 187 {ECO:0000244|PDB:1FF3}.
HELIX 190 193 {ECO:0000244|PDB:1FF3}.
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


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