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UniProtKB/Swiss-Prot entry P0C0L2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name OSMC_ECOLI
Primary accession number P0C0L2
Secondary accession numbers P23929 P77655
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 34)
Name and origin of the protein
Protein name Peroxiredoxin osmC
Synonyms EC 1.11.1.15
Osmotically-inducible protein C
Gene name
Name: osmC
OrderedLocusNames: b1482, JW1477
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
STRAIN=K12;
DOI=10.1016/0022-2836(91)90366-E; PubMed=1715407 [NCBI, ExPASy, EBI, Israel, Japan]
Gutierrez C., Devedjian J.C.;
"Osmotic induction of gene osmC expression in Escherichia coli K12.";
J. Mol. Biol. 220:959-973(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PARTIAL PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND FUNCTION.
DOI=10.1110/ps.03375603; PubMed=14627744 [NCBI, ExPASy, EBI, Israel, Japan]
Lesniak J., Barton W.A., Nikolov D.B.;
"Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC.";
Protein Sci. 12:2838-2843(2003).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1107/S0907444904005013; PubMed=15103136 [NCBI, ExPASy, EBI, Israel, Japan]
Shin D.H., Choi I.G., Busso D., Jancarik J., Yokota H., Kim R., Kim S.H.;
"Structure of OsmC from Escherichia coli: a salt-shock-induced protein.";
Acta Crystallogr. D 60:903-911(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X57433; CAA40680.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74555.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15128.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E64901; E64901.
RefSeq AP_002105.1; -.
NP_415999.1; -.
3D structure databases
PDB
1NYE; X-ray; 2.40 A; A/B/C/D/E/F=1-143.[ExPASy / RCSB / EBI]
1QWI; X-ray; 1.80 A; A/B/C/D=1-143.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NYE; -.
1QWI; -.
ModBase P0C0L2.
Enzyme and pathway databases
BioCyc EcoCyc:EG10680-MON; -.
Organism-specific databases
EchoBASE EB0674; -.
EcoGene EG10680; osmC.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR015946; KH-like_a/b.
IPR003718; OsmC.
Graphical view of domain structure.
Gene3D G3DSA:3.30.300.20; KH_prok; 1.
Pfam PF02566; OsmC; 1.
Pfam graphical view of domain structure.
Genome annotation databases
GeneID 946043; -.
GenomeReviews AP009048_GR; JW1477.
U00096_GR; b1482.
KEGG ecj:JW1477; -.
eco:b1482; -.
Phylogenomic databases
HOGENOM P0C0L2; -.
Other
LinkHub P0C0L2; -.
Genome annotation databases
CMR P0C0L2; b1482.
Other
ProtoNet P0C0L2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   143  142     Peroxiredoxin osmC. PRO_0000172729
MOD_RES   16    16        N6-acetyllysine. 
STRAND   3    13  11      
TURN   15    17  3      
STRAND   19    34  16      
HELIX   36    40  5      
HELIX   48    69  22      
TURN   70    72  3      
STRAND   76    89  14      
STRAND   92   105  14      
HELIX   111   124  14      
HELIX   126   130  5      
STRAND   133   142  10      
Sequence information
Length: 143 AA [This is the length of the unprocessed precursor] Molecular weight: 15088 Da [This is the MW of the unprocessed precursor] CRC64: A9096964BC962569 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTIHKKGQAH WEGDIKRGKG TVSTESGVLN QQPYGFNTRF EGEKGTNPEE LIGAAHAACF 

        70         80         90        100        110        120 
SMALSLMLGE AGFTPTSIDT TADVSLDKVD AGFAITKIAL KSEVAVPGID ASTFDGIIQK 

       130        140 
AKAGCPVSQV LKAEITLDYQ LKS 

P0C0L2 in FASTA format

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