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Protein

Peroxiredoxin OsmC

Gene

osmC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

GO - Molecular functioni

  • peroxidase activity Source: EcoCyc
  • peroxiredoxin activity Source: EcoCyc

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • hyperosmotic response Source: EcoCyc
  • response to hydroperoxide Source: EcoCyc
  • response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciEcoCyc:EG10680-MONOMER.
ECOL316407:JW1477-MONOMER.
RETL1328306-WGS:GSTH-3765-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin OsmC (EC:1.11.1.15)
Alternative name(s):
Osmotically-inducible protein C
Gene namesi
Name:osmC
Ordered Locus Names:b1482, JW1477
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10680. osmC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 143142Peroxiredoxin OsmCPRO_0000172729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0C0L2.
PaxDbiP0C0L2.
PRIDEiP0C0L2.

Expressioni

Inductioni

By elevated osmotic pressure in the growth medium.

Interactioni

Protein-protein interaction databases

BioGridi4260206. 228 interactions.
DIPiDIP-48058N.
IntActiP0C0L2. 11 interactions.
STRINGi511145.b1482.

Structurei

Secondary structure

1
143
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311Combined sources
Beta strandi15 – 173Combined sources
Beta strandi19 – 246Combined sources
Beta strandi27 – 348Combined sources
Helixi36 – 405Combined sources
Helixi48 – 7023Combined sources
Beta strandi76 – 8914Combined sources
Beta strandi92 – 10514Combined sources
Helixi111 – 12414Combined sources
Helixi126 – 1305Combined sources
Beta strandi133 – 14210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYEX-ray2.40A/B/C/D/E/F1-143[»]
1QWIX-ray1.80A/B/C/D1-143[»]
ProteinModelPortaliP0C0L2.
SMRiP0C0L2. Positions 1-143.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0L2.

Family & Domainsi

Sequence similaritiesi

Belongs to the OsmC/Ohr family.Curated

Phylogenomic databases

eggNOGiENOG4108Z9K. Bacteria.
COG1764. LUCA.
HOGENOMiHOG000060052.
InParanoidiP0C0L2.
KOiK04063.
OMAiWQGGIKD.
OrthoDBiEOG6Q5NWH.
PhylomeDBiP0C0L2.

Family and domain databases

Gene3Di3.30.300.20. 1 hit.
InterProiIPR015946. KH_dom-like_a/b.
IPR003718. OsmC/Ohr_fam.
IPR019904. Peroxiredoxin_OsmC.
[Graphical view]
PfamiPF02566. OsmC. 1 hit.
[Graphical view]
SUPFAMiSSF82784. SSF82784. 1 hit.
TIGRFAMsiTIGR03562. osmo_induc_OsmC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0L2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIHKKGQAH WEGDIKRGKG TVSTESGVLN QQPYGFNTRF EGEKGTNPEE
60 70 80 90 100
LIGAAHAACF SMALSLMLGE AGFTPTSIDT TADVSLDKVD AGFAITKIAL
110 120 130 140
KSEVAVPGID ASTFDGIIQK AKAGCPVSQV LKAEITLDYQ LKS
Length:143
Mass (Da):15,088
Last modified:January 23, 2007 - v2
Checksum:iA9096964BC962569
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57433 Genomic DNA. Translation: CAA40680.1.
U00096 Genomic DNA. Translation: AAC74555.1.
AP009048 Genomic DNA. Translation: BAA15128.1.
PIRiE64901.
RefSeqiNP_415999.1. NC_000913.3.
WP_000152305.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74555; AAC74555; b1482.
BAA15128; BAA15128; BAA15128.
GeneIDi946043.
KEGGiecj:JW1477.
eco:b1482.
PATRICi32118258. VBIEscCol129921_1549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57433 Genomic DNA. Translation: CAA40680.1.
U00096 Genomic DNA. Translation: AAC74555.1.
AP009048 Genomic DNA. Translation: BAA15128.1.
PIRiE64901.
RefSeqiNP_415999.1. NC_000913.3.
WP_000152305.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYEX-ray2.40A/B/C/D/E/F1-143[»]
1QWIX-ray1.80A/B/C/D1-143[»]
ProteinModelPortaliP0C0L2.
SMRiP0C0L2. Positions 1-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260206. 228 interactions.
DIPiDIP-48058N.
IntActiP0C0L2. 11 interactions.
STRINGi511145.b1482.

Proteomic databases

EPDiP0C0L2.
PaxDbiP0C0L2.
PRIDEiP0C0L2.

Protocols and materials databases

DNASUi946043.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74555; AAC74555; b1482.
BAA15128; BAA15128; BAA15128.
GeneIDi946043.
KEGGiecj:JW1477.
eco:b1482.
PATRICi32118258. VBIEscCol129921_1549.

Organism-specific databases

EchoBASEiEB0674.
EcoGeneiEG10680. osmC.

Phylogenomic databases

eggNOGiENOG4108Z9K. Bacteria.
COG1764. LUCA.
HOGENOMiHOG000060052.
InParanoidiP0C0L2.
KOiK04063.
OMAiWQGGIKD.
OrthoDBiEOG6Q5NWH.
PhylomeDBiP0C0L2.

Enzyme and pathway databases

BioCyciEcoCyc:EG10680-MONOMER.
ECOL316407:JW1477-MONOMER.
RETL1328306-WGS:GSTH-3765-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0C0L2.
PROiP0C0L2.

Family and domain databases

Gene3Di3.30.300.20. 1 hit.
InterProiIPR015946. KH_dom-like_a/b.
IPR003718. OsmC/Ohr_fam.
IPR019904. Peroxiredoxin_OsmC.
[Graphical view]
PfamiPF02566. OsmC. 1 hit.
[Graphical view]
SUPFAMiSSF82784. SSF82784. 1 hit.
TIGRFAMsiTIGR03562. osmo_induc_OsmC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Osmotic induction of gene osmC expression in Escherichia coli K12."
    Gutierrez C., Devedjian J.C.
    J. Mol. Biol. 220:959-973(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  6. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  7. "Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC."
    Lesniak J., Barton W.A., Nikolov D.B.
    Protein Sci. 12:2838-2843(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), FUNCTION.
  8. "Structure of OsmC from Escherichia coli: a salt-shock-induced protein."
    Shin D.H., Choi I.G., Busso D., Jancarik J., Yokota H., Kim R., Kim S.H.
    Acta Crystallogr. D 60:903-911(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiOSMC_ECOLI
AccessioniPrimary (citable) accession number: P0C0L2
Secondary accession number(s): P23929, P77655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.