ID MSRB_LEPIN Reviewed; 132 AA. AC Q8F7W8; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 03-MAR-2009, entry version 37. 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=LA_0824; OS Leptospira interrogans. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=173; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai; RX MEDLINE=22598143; PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., RA Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., RA Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., RA Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., RA Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., RA Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., RA Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira RT interrogans revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). 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. 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; AE010300; AAN48023.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_711005.1; -. DR HSSP; P14930; 1L1D. DR GeneID; 1150167; -. DR GenomeReviews; AE010300_GR; LA_0824. DR KEGG; lil:LA0824; -. DR HOGENOM; Q8F7W8; -. DR BioCyc; LINT189518:LA0824-MON; -. DR BRENDA; 1.8.4.12; 258108. 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 1 132 Peptide methionine sulfoxide reductase FT msrB. FT /FTId=PRO_0000140279. FT ACT_SITE 121 121 Nucleophile (By similarity). FT METAL 49 49 Zinc (By similarity). FT METAL 52 52 Zinc (By similarity). FT METAL 98 98 Zinc (By similarity). FT METAL 101 101 Zinc (By similarity). SQ SEQUENCE 132 AA; 14848 MW; 3B9DA6715CDF55E5 CRC64; MMNYEVNKSD EDWKKELTPE QYRILRQKGT EMAFTGALYK NQDKGTYVCA ACGAVLFSSD TKYESGSGWP SFYQPVKDGV VDKQKDSSHG MERTEILCSK CGGHLGHVFN DGPRPTGLRY CINSASLKFQ KE //