OSMC_ECOLI
ID OSMC_ECOLI Reviewed; 143 AA.
AC P0C0L2; P23929; P77655;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Peroxiredoxin OsmC;
DE EC=1.11.1.-;
DE AltName: Full=Osmotically-inducible protein C;
GN Name=osmC; OrderedLocusNames=b1482, JW1477;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
RC STRAIN=K12;
RX PubMed=1715407; DOI=10.1016/0022-2836(91)90366-e;
RA Gutierrez C., Devedjian J.C.;
RT "Osmotic induction of gene osmC expression in Escherichia coli K12.";
RL J. Mol. Biol. 220:959-973(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX 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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND FUNCTION.
RX PubMed=14627744; DOI=10.1110/ps.03375603;
RA Lesniak J., Barton W.A., Nikolov D.B.;
RT "Structural and functional features of the Escherichia coli hydroperoxide
RT resistance protein OsmC.";
RL Protein Sci. 12:2838-2843(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=15103136; DOI=10.1107/s0907444904005013;
RA Shin D.H., Choi I.G., Busso D., Jancarik J., Yokota H., Kim R., Kim S.H.;
RT "Structure of OsmC from Escherichia coli: a salt-shock-induced protein.";
RL Acta Crystallogr. D 60:903-911(2004).
CC -!- FUNCTION: Preferentially metabolizes organic hydroperoxides over
CC inorganic hydrogen peroxide. {ECO:0000269|PubMed:14627744}.
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.
CC -!- INDUCTION: By elevated osmotic pressure in the growth medium.
CC -!- SIMILARITY: Belongs to the OsmC/Ohr family. {ECO:0000305}.
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DR EMBL; X57433; CAA40680.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74555.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15128.1; -; Genomic_DNA.
DR PIR; E64901; E64901.
DR RefSeq; NP_415999.1; NC_000913.3.
DR RefSeq; WP_000152305.1; NZ_STEB01000054.1.
DR PDB; 1NYE; X-ray; 2.40 A; A/B/C/D/E/F=1-143.
DR PDB; 1QWI; X-ray; 1.80 A; A/B/C/D=1-143.
DR PDBsum; 1NYE; -.
DR PDBsum; 1QWI; -.
DR AlphaFoldDB; P0C0L2; -.
DR SMR; P0C0L2; -.
DR BioGRID; 4260206; 234.
DR BioGRID; 850404; 3.
DR DIP; DIP-48058N; -.
DR IntAct; P0C0L2; 11.
DR STRING; 511145.b1482; -.
DR iPTMnet; P0C0L2; -.
DR jPOST; P0C0L2; -.
DR PaxDb; P0C0L2; -.
DR PRIDE; P0C0L2; -.
DR DNASU; 946043; -.
DR EnsemblBacteria; AAC74555; AAC74555; b1482.
DR EnsemblBacteria; BAA15128; BAA15128; BAA15128.
DR GeneID; 60900296; -.
DR GeneID; 66674666; -.
DR GeneID; 946043; -.
DR KEGG; ecj:JW1477; -.
DR KEGG; eco:b1482; -.
DR PATRIC; fig|1411691.4.peg.785; -.
DR EchoBASE; EB0674; -.
DR eggNOG; COG1764; Bacteria.
DR HOGENOM; CLU_106355_1_0_6; -.
DR InParanoid; P0C0L2; -.
DR OMA; ANCPVSQ; -.
DR PhylomeDB; P0C0L2; -.
DR BioCyc; EcoCyc:EG10680-MON; -.
DR BioCyc; MetaCyc:EG10680-MON; -.
DR EvolutionaryTrace; P0C0L2; -.
DR PRO; PR:P0C0L2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004601; F:peroxidase activity; IDA:EcoCyc.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:EcoCyc.
DR GO; GO:0006972; P:hyperosmotic response; IEP:EcoCyc.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Oxidoreductase; Peroxidase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..143
FT /note="Peroxiredoxin OsmC"
FT /id="PRO_0000172729"
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:0000269|PubMed:18723842"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1QWI"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1QWI"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1QWI"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:1QWI"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:1QWI"
FT HELIX 48..70
FT /evidence="ECO:0007829|PDB:1QWI"
FT STRAND 76..89
FT /evidence="ECO:0007829|PDB:1QWI"
FT STRAND 92..105
FT /evidence="ECO:0007829|PDB:1QWI"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1QWI"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:1QWI"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:1QWI"
SQ SEQUENCE 143 AA; 15088 MW; A9096964BC962569 CRC64;
MTIHKKGQAH WEGDIKRGKG TVSTESGVLN QQPYGFNTRF EGEKGTNPEE LIGAAHAACF
SMALSLMLGE AGFTPTSIDT TADVSLDKVD AGFAITKIAL KSEVAVPGID ASTFDGIIQK
AKAGCPVSQV LKAEITLDYQ LKS
