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Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase)

 MSRB_ECOLI              Reviewed;         137 AA.
P0A746; P39903; P76232; P76912;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
25-APR-2018, entry version 108.
RecName: Full=Peptide methionine sulfoxide reductase MsrB;
EC=1.8.4.12;
AltName: Full=Peptide-methionine (R)-S-oxide reductase;
Name=msrB; Synonyms=yeaA; OrderedLocusNames=b1778, JW1767;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[2]
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
PubMed=2990926; DOI=10.1111/j.1432-1033.1985.tb08988.x;
Branlant G., Branlant C.;
"Nucleotide sequence of the Escherichia coli gap gene. Different
evolutionary behavior of the NAD+-binding domain and of the catalytic
domain of D-glyceraldehyde-3-phosphate dehydrogenase.";
Eur. J. Biochem. 150:61-66(1985).
[5]
IDENTIFICATION.
PubMed=7984428; DOI=10.1093/nar/22.22.4756;
Borodovsky M., Rudd K.E., Koonin E.V.;
"Intrinsic and extrinsic approaches for detecting genes in a bacterial
genome.";
Nucleic Acids Res. 22:4756-4767(1994).
[6]
FUNCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=11677230; DOI=10.1074/jbc.M105509200;
Grimaud R., Ezraty B., Mitchell J.K., Lafitte D., Briand C.,
Derrick P.J., Barras F.;
"Repair of oxidized proteins. Identification of a new methionine
sulfoxide reductase.";
J. Biol. Chem. 276:48915-48920(2001).
[7]
CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY, AND MUTAGENESIS OF
CYS-46; CYS-49; CYS-95 AND CYS-98.
STRAIN=K12;
PubMed=16251365; DOI=10.1110/ps.051711105;
Olry A., Boschi-Muller S., Yu H., Burnel D., Branlant G.;
"Insights into the role of the metal binding site in methionine-R-
sulfoxide reductases B.";
Protein Sci. 14:2828-2837(2005).
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
{ECO:0000269|PubMed:16251365}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16251365};
Note=Binds 1 zinc ion per subunit. The zinc ion is important for
the structural integrity of the protein.
{ECO:0000269|PubMed:16251365};
-!- MASS SPECTROMETRY: Mass=15319; Mass_error=1; Method=Electrospray;
Range=2-137; Evidence={ECO:0000269|PubMed:16251365};
-!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=X02662; Type=Frameshift; Positions=5; Evidence={ECO:0000305};
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EMBL; U00096; AAC74848.1; -; Genomic_DNA.
EMBL; AP009048; BAA15575.2; -; Genomic_DNA.
EMBL; X02662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; B64938; B64938.
RefSeq; NP_416292.1; NC_000913.3.
RefSeq; WP_001284618.1; NZ_LN832404.1.
ProteinModelPortal; P0A746; -.
SMR; P0A746; -.
BioGrid; 4260307; 54.
DIP; DIP-48167N; -.
IntAct; P0A746; 4.
STRING; 316385.ECDH10B_1916; -.
PaxDb; P0A746; -.
PRIDE; P0A746; -.
EnsemblBacteria; AAC74848; AAC74848; b1778.
EnsemblBacteria; BAA15575; BAA15575; BAA15575.
GeneID; 947188; -.
KEGG; ecj:JW1767; -.
KEGG; eco:b1778; -.
PATRIC; fig|1411691.4.peg.476; -.
EchoBASE; EB2295; -.
EcoGene; EG12394; msrB.
eggNOG; ENOG4105E0X; Bacteria.
eggNOG; COG0229; LUCA.
HOGENOM; HOG000243425; -.
InParanoid; P0A746; -.
KO; K07305; -.
OMA; YKASHKF; -.
PhylomeDB; P0A746; -.
BioCyc; EcoCyc:EG12394-MONOMER; -.
BioCyc; MetaCyc:EG12394-MONOMER; -.
BRENDA; 1.8.4.12; 2026.
PRO; PR:P0A746; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0005506; F:iron ion binding; IDA:EcoliWiki.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:EcoliWiki.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0030091; P:protein repair; IDA:EcoCyc.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
HAMAP; MF_01400; MsrB; 1.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like_sf.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
TIGRFAMs; TIGR00357; TIGR00357; 1.
PROSITE; PS51790; MSRB; 1.
1: Evidence at protein level;
Complete proteome; Metal-binding; Oxidoreductase; Reference proteome;
Zinc.
INIT_MET 1 1 Removed.
CHAIN 2 137 Peptide methionine sulfoxide reductase
MsrB.
/FTId=PRO_0000140271.
DOMAIN 7 129 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
ACT_SITE 118 118 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 46 46 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 49 49 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 95 95 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 98 98 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
MUTAGEN 46 46 C->D: Loss of activity; when associated
with S-49; S-95 and S-98.
{ECO:0000269|PubMed:16251365}.
MUTAGEN 49 49 C->S: Loss of activity; when associated
with S-46; S-95 and S-98.
{ECO:0000269|PubMed:16251365}.
MUTAGEN 95 95 C->S: Loss of activity; when associated
with S-46; S-49 and S-98.
{ECO:0000269|PubMed:16251365}.
MUTAGEN 98 98 C->S: Loss of activity; when associated
with S-46; S-49 and S-95.
{ECO:0000269|PubMed:16251365}.
SEQUENCE 137 AA; 15451 MW; 7B9B783DBEBE0F71 CRC64;
MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY
DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN
SASLRFTDGE NGEEING


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