ID   MSRB_CAUCR              Reviewed;         159 AA.
AC   Q9A6B1;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 51.
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; OrderedLocusNames=CC_2183;
OS   Caulobacter crescentus (Caulobacter vibrioides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=155892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the msrB Met sulfoxide reductase family.
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DR   EMBL; AE005673; AAK24154.1; -; Genomic_DNA.
DR   PIR; F87519; F87519.
DR   RefSeq; NP_420986.1; -.
DR   HSSP; P14930; 1L1D.
DR   GeneID; 943108; -.
DR   GenomeReviews; AE005673_GR; CC_2183.
DR   KEGG; ccr:CC_2183; -.
DR   NMPDR; fig|190650.1.peg.2166; -.
DR   TIGR; CC_2183; -.
DR   HOGENOM; Q9A6B1; -.
DR   OMA; Q9A6B1; ARVLLHH.
DR   BRENDA; 1.8.4.12; 2191.
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   3: Inferred from homology;
KW   Complete proteome; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN         1    159       Peptide methionine sulfoxide reductase
FT                                msrB.
FT                                /FTId=PRO_0000140266.
FT   ACT_SITE    133    133       Nucleophile (By similarity).
FT   METAL        61     61       Zinc (By similarity).
FT   METAL        64     64       Zinc (By similarity).
FT   METAL       110    110       Zinc (By similarity).
FT   METAL       113    113       Zinc (By similarity).
SQ   SEQUENCE   159 AA;  17300 MW;  2DCFA741AF36EE57 CRC64;
     MTDAATLSTA GFDLTPPTEA ERERLEANLT AEEARVLLHH GTEAPFCGGL LGEKSPGVYG
     CRLCGLPLFK HETKFESGTG WPSFYAPFAE DHVVGVRDTS YGMVRIETRC ARCDSHQGHV
     FPDGPAPTRL RYCINSVSLQ FVKAGAPLPD PLHRGDKIT
//