P0C0L2 (OSMC_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peroxiredoxin osmC EC=1.11.1.15 Alternative name(s): Osmotically-inducible protein C | ||||
| Gene names |
| ||||
| 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 | |
| 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 activityInferred 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 | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| 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
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References
| « Hide '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. 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 |
| ||||||||||||||||||
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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