OSMC_SHIFL
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 25-MAY-2022, entry version 102.
DE RecName: Full=Peroxiredoxin OsmC;
DE EC=1.11.1.-;
DE AltName: Full=Osmotically-inducible protein C;
GN Name=osmC; OrderedLocusNames=SF1743, S1876;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., 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 PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Preferentially metabolizes organic hydroperoxides over
CC inorganic hydrogen peroxide. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OsmC/Ohr family. {ECO:0000305}.
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DR EMBL; AE005674; AAN43315.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17201.1; -; Genomic_DNA.
DR RefSeq; NP_707608.1; NC_004337.2.
DR RefSeq; WP_000152305.1; NZ_WPGW01000136.1.
DR AlphaFoldDB; P0C0L3; -.
DR SMR; P0C0L3; -.
DR STRING; 198214.SF1743; -.
DR PRIDE; P0C0L3; -.
DR EnsemblBacteria; AAN43315; AAN43315; SF1743.
DR EnsemblBacteria; AAP17201; AAP17201; S1876.
DR GeneID; 1024939; -.
DR GeneID; 60900296; -.
DR GeneID; 66674666; -.
DR KEGG; sfl:SF1743; -.
DR KEGG; sfx:S1876; -.
DR PATRIC; fig|198214.7.peg.2066; -.
DR HOGENOM; CLU_106355_1_0_6; -.
DR OMA; ANCPVSQ; -.
DR OrthoDB; 1655733at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:RHEA.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 3.30.300.20; -; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR003718; OsmC/Ohr_fam.
DR InterPro; IPR036102; OsmC/Ohrsf.
DR InterPro; IPR019904; Peroxiredoxin_OsmC.
DR Pfam; PF02566; OsmC; 1.
DR SUPFAM; SSF82784; SSF82784; 1.
DR TIGRFAMs; TIGR03562; osmo_induc_OsmC; 1.
PE 3: Inferred from homology;
KW Acetylation; Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..143
FT /note="Peroxiredoxin OsmC"
FT /id="PRO_0000172730"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 143 AA; 15088 MW; A9096964BC962569 CRC64;
MTIHKKGQAH WEGDIKRGKG TVSTESGVLN QQPYGFNTRF EGEKGTNPEE LIGAAHAACF
SMALSLMLGE AGFTPTSIDT TADVSLDKVD AGFAITKIAL KSEVAVPGID ASTFDGIIQK
AKAGCPVSQV LKAEITLDYQ LKS
