P0C0L2 (OSMC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin osmC
EC=1.11.1.15

Alternative name(s):
Osmotically-inducible protein C

Gene names

Name:	osmC
Ordered Locus Names:	b1482, JW1477

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	143 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide. Ref.7
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subcellular location	Cytoplasm.
Induction	By elevated osmotic pressure in the growth medium.
Sequence similarities	Belongs to the osmC/ohr family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	response to stress Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 143

142

Peroxiredoxin osmC

PRO_0000172729

Amino acid modifications

Modified residue

16

1

N6-acetyllysine Ref.6

Secondary structure

1

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143

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Turn

15 – 17

3

Beta strand

19 – 34

16

Helix

36 – 40

5

Helix

48 – 69

22

Turn

70 – 72

3

Beta strand

76 – 89

14

Beta strand

92 – 105

14

Helix

111 – 124

14

Helix

126 – 130

5

Beta strand

133 – 142

10

Sequences

	Sequence		Length	Mass (Da)
	P0C0L2 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A9096964BC962569	FASTA	143	15,088
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Osmotic induction of gene osmC expression in Escherichia coli K12." Gutierrez C., Devedjian J.C. J. Mol. Biol. 220:959-973(1991) [PubMed: 1715407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139. Strain: K12.
[2]	"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." 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. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9298646] [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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, 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: 14627744] [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: 15103136] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57433 Genomic DNA. Translation: CAA40680.1.
U00096 Genomic DNA. Translation: AAC74555.1.
AP009048 Genomic DNA. Translation: BAA15128.1.

PIR

E64901.

RefSeq

NP_415999.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NYE	X-ray	2.40	A/B/C/D/E/F	1-143	[»]
1QWI	X-ray	1.80	A/B/C/D	1-143	[»]

ProteinModelPortal

P0C0L2.

SMR

P0C0L2. Positions 1-143.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48058N.

IntAct

P0C0L2. 9 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003606; EBESCP00000003606; EBESCG00000002942.
EBESCT00000003607; EBESCP00000003607; EBESCG00000002942.
EBESCT00000015884; EBESCP00000015175; EBESCG00000014944.

GeneID

946043.

GenomeReviews

Gene locus JW1477 in contig AP009048_GR.
Gene locus b1482 in contig U00096_GR.

KEGG

ecj:JW1477.
eco:b1482.

PATRIC

32118258. VBIEscCol129921_1549.

Organism-specific databases

EchoBASE

EB0674.

EcoGene

EG10680. osmC.

Phylogenomic databases

eggNOG

COG1764.

GeneTree

EBGT00050000011708.

HOGENOM

HBG672134.

OMA

PGSNPEE.

PhylomeDB

P0C0L2.

ProtClustDB

CLSK880045.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10680-MONOMER.

Gene expression databases

Genevestigator

P0C0L2.

Family and domain databases

InterPro

IPR015946. KH_dom-like_a/b.
IPR003718. Peroxiredoxin_OsmC-like.
IPR019904. Peroxiredoxin_OsmC_subgr.
[Graphical view]

Gene3D

G3DSA:3.30.300.20. KH_prok. 1 hit.

KO

K04063.

Pfam

PF02566. OsmC. 1 hit.
[Graphical view]

SUPFAM

SSF82784. OsmC. 1 hit.

TIGRFAMs

TIGR03562. Osmo_induc_OsmC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

OSMC_ECOLI

Accession

Primary (citable) accession number: P0C0L2
Secondary accession number(s): P23929, P77655

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program