ID MSRB_ECOLI Reviewed; 137 AA. AC P0A746; P39903; P76232; P76912; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 16-JUN-2009, entry version 38. DE RecName: Full=Peptide methionine sulfoxide reductase msrB; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase; GN Name=msrB; Synonyms=yeaA; OrderedLocusNames=b1778, JW1767; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48. RX MEDLINE=85257641; PubMed=2990926; RX DOI=10.1111/j.1432-1033.1985.tb08988.x; RA Branlant G., Branlant C.; RT "Nucleotide sequence of the Escherichia coli gap gene. Different RT evolutionary behavior of the NAD+-binding domain and of the catalytic RT domain of D-glyceraldehyde-3-phosphate dehydrogenase."; RL Eur. J. Biochem. 150:61-66(1985). RN [5] RP IDENTIFICATION. RX MEDLINE=95075659; PubMed=7984428; DOI=10.1093/nar/22.22.4756; RA Borodovsky M., Rudd K.E., Koonin E.V.; RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial RT genome."; RL Nucleic Acids Res. 22:4756-4767(1994). RN [6] RP FUNCTION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=11677230; DOI=10.1074/jbc.M105509200; RA Grimaud R., Ezraty B., Mitchell J.K., Lafitte D., Briand C., RA Derrick P.J., Barras F.; RT "Repair of oxidized proteins. Identification of a new methionine RT sulfoxide reductase."; RL J. Biol. Chem. 276:48915-48920(2001). RN [7] RP CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY, AND MUTAGENESIS OF RP CYS-46; CYS-49; CYS-95 AND CYS-98. RC STRAIN=K12; RX PubMed=16251365; DOI=10.1110/ps.051711105; RA Olry A., Boschi-Muller S., Yu H., Burnel D., Branlant G.; RT "Insights into the role of the metal binding site in methionine-R- RT sulfoxide reductases B."; RL Protein Sci. 14:2828-2837(2005). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- COFACTOR: Binds 1 zinc ion per subunit. The zinc ion is important CC for the structural integrity of the protein. CC -!- MASS SPECTROMETRY: Mass=15319; Mass_error=1; Method=Electrospray; CC Range=2-137; Source=PubMed:16251365; CC -!- SIMILARITY: Belongs to the msrB Met sulfoxide reductase family. CC -!- SEQUENCE CAUTION: CC Sequence=X02662; Type=Frameshift; Positions=5; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00096; AAC74848.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15575.2; -; Genomic_DNA. DR EMBL; X02662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; B64938; B64938. DR RefSeq; AP_002397.1; -. DR RefSeq; NP_416292.1; -. DR HSSP; P14930; 1L1D. DR GeneID; 947188; -. DR GenomeReviews; AP009048_GR; JW1767. DR GenomeReviews; U00096_GR; b1778. DR KEGG; ecj:JW1767; -. DR KEGG; eco:b1778; -. DR EchoBASE; EB2295; -. DR EcoGene; EG12394; msrB. DR HOGENOM; P0A746; -. DR OMA; P0A746; FTGRYWD. DR BioCyc; EcoCyc:EG12394-MON; -. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase ac...; IEA:EC. DR GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01400; -; 1. DR InterPro; IPR002579; Methionine_sulphoxide_MsrB. DR Gene3D; G3DSA:2.170.150.20; MsrB; 1. DR Pfam; PF01641; SelR; 1. DR ProDom; PD004057; DUF25; 1. DR TIGRFAMs; TIGR00357; MsrB; 1. PE 1: Evidence at protein level; KW Complete proteome; Metal-binding; Oxidoreductase; Zinc. FT INIT_MET 1 1 Removed. FT CHAIN 2 137 Peptide methionine sulfoxide reductase FT msrB. FT /FTId=PRO_0000140271. FT ACT_SITE 118 118 Nucleophile (By similarity). FT METAL 46 46 Zinc. FT METAL 49 49 Zinc. FT METAL 95 95 Zinc. FT METAL 98 98 Zinc. FT MUTAGEN 46 46 C->D: Loss of activity; when associated FT with S-49; S-95 and S-98. FT MUTAGEN 49 49 C->S: Loss of activity; when associated FT with S-46; S-95 and S-98. FT MUTAGEN 95 95 C->S: Loss of activity; when associated FT with S-46; S-49 and S-98. FT MUTAGEN 98 98 C->S: Loss of activity; when associated FT with S-46; S-49 and S-95. SQ SEQUENCE 137 AA; 15451 MW; 7B9B783DBEBE0F71 CRC64; MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN SASLRFTDGE NGEEING //