ID OSMC_SHIFL Reviewed; 143 AA. AC P0C0L3; P23929; P77655; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-DEC-2008, entry version 29. DE RecName: Full=Peroxiredoxin osmC; DE EC=1.11.1.15; DE AltName: Full=Osmotically-inducible protein C; GN Name=osmC; OrderedLocusNames=SF1743, S1876; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RX DOI=10.1128/IAI.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: Preferentially metabolizes organic hydroperoxides over CC inorganic hydrogen peroxide (By similarity). CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the osmC/ohr 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; AE005674; AAN43315.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17201.1; -; Genomic_DNA. DR RefSeq; NP_707608.1; -. DR RefSeq; NP_837392.1; -. DR SMR; P0C0L3; 1-143. DR GeneID; 1024939; -. DR GeneID; 1078207; -. DR GenomeReviews; AE005674_GR; SF1743. DR GenomeReviews; AE014073_GR; S1876. DR KEGG; sfl:SF1743; -. DR KEGG; sfx:S1876; -. DR HOGENOM; P0C0L3; -. DR BioCyc; SFLE198214:AAN43315.1-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR InterPro; IPR015946; KH-like_a/b. DR InterPro; IPR003718; OsmC. DR Gene3D; G3DSA:3.30.300.20; KH_prok; 1. DR Pfam; PF02566; OsmC; 1. PE 3: Inferred from homology; KW Acetylation; Antioxidant; Complete proteome; Cytoplasm; KW Oxidoreductase; Peroxidase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 143 Peroxiredoxin osmC. FT /FTId=PRO_0000172730. FT MOD_RES 16 16 N6-acetyllysine (By similarity). SQ SEQUENCE 143 AA; 15088 MW; A9096964BC962569 CRC64; MTIHKKGQAH WEGDIKRGKG TVSTESGVLN QQPYGFNTRF EGEKGTNPEE LIGAAHAACF SMALSLMLGE AGFTPTSIDT TADVSLDKVD AGFAITKIAL KSEVAVPGID ASTFDGIIQK AKAGCPVSQV LKAEITLDYQ LKS //