P0A0B7 (AHPC_STAA8) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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: Alkyl hydroperoxide reductase subunit C EC=1.11.1.15 Alternative name(s): Peroxiredoxin Thioredoxin peroxidase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain NCTC 8325) | ||||
| Taxonomic identifier | 93061 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 189 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 | Directly reduces organic hydroperoxides in its reduced dithiol form. Possesses broad-spectrum activity, being involved in hydrogen peroxide, cumene hydroperoxide, tert-butyl hydroperoxide, paraquat and peroxynitrite resistance. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. Ref.4 |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homodimer; disulfide-linked, upon oxidation By similarity. |
| Induction | Induced by iron and osmotic shock. Repressed under metal-depleted growth conditions and by manganese-rich growth conditions. Negatively regulated by the ferric uptake regulator (Fur) and PerR. Ref.1 Ref.3 Ref.4 |
| Post-translational modification | The Cys-49-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-49 (probably Cys-SOH) rapidly reacts with Cys-168-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin By similarity. |
| Miscellaneous | In S.aureus, the removal of hydrogen peroxide appears to occur predominately via KatA, with AhpC acting as an alternative. |
| Sequence similarities | Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Disulfide bond |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| 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 Probable | ||||||
| Chain | 2 – 189 | 188 | Alkyl hydroperoxide reductase subunit C | PRO_0000135128 | |||||
Regions | |||||||||
| Domain | 2 – 159 | 158 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 49 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 49 | Interchain (with C-168); in linked form By similarity | |||||||
| Disulfide bond | 168 | Interchain (with C-49); in linked form By similarity | |||||||
Experimental info | |||||||||
| Sequence conflict | 2 | 1 | S → G AA sequence Ref.1 | ||||||
| Sequence conflict | 17 | 1 | D → DD AA sequence Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus." Armstrong-Buisseret L., Cole M.B., Stewart G.S.A.B. Microbiology 141:1655-1661(1995) [PubMed: 7551034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, INDUCTION BY OSMOTIC UPSHOCK. |
| [2] | "The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 8325. |
| [3] | "The staphylococcal ferritins are differentially regulated in response to iron and manganese and via perR and fur." Morrissey J.A., Cockayne A., Brummell K., Williams P. Infect. Immun. 72:972-979(2004) [PubMed: 14742543] [Abstract] Cited for: INDUCTION BY METALS, REGULATION BY FUR AND PERR. |
| [4] | "Catalase (katA) and alkyl hydroperoxide reductase (ahpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence and nasal colonization in Staphylococcus aureus." Cosgrove K., Coutts G., Jonsson I.-M., Tarkowski A., Kokai-Kun J.F., Mond J.J., Foster S.J. J. Bacteriol. 189:1025-1035(2007) [PubMed: 17114262] [Abstract] Cited for: FUNCTION, REGULATION BY PERR. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U92441 Genomic DNA. Translation: AAB51151.1. CP000253 Genomic DNA. Translation: ABD29531.1. |
| PIR | S52934. |
| RefSeq | YP_498954.1. NC_007795.1. |
3D structure databases | |
| ProteinModelPortal | P0A0B7. |
| SMR | P0A0B7. Positions 2-168. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P0A0B7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000030036; EBSTAP00000028987; EBSTAG00000030034. |
| GeneID | 3919784. |
| GenomeReviews | Gene locus SAOUHSC_00365 in contig CP000253_GR. |
| KEGG | sao:SAOUHSC_00365. |
| PATRIC | 19578318. VBIStaAur99865_0335. |
Phylogenomic databases | |
| eggNOG | COG0450. |
| GeneTree | EBGT00050000024736. |
| HOGENOM | HBG493509. |
| OMA | GDLADHY. |
| ProtClustDB | CLSK884603. |
Enzyme and pathway databases | |
| BioCyc | SAUR93061:SAOUHSC_00365-MONOMER. |
Family and domain databases | |
| InterPro | IPR017559. AhpC. IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| KO | K03386. |
| PANTHER | PTHR10681:SF7. PTHR10681:SF7. 1 hit. |
| Pfam | PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| PIRSF | PIRSF000239. AHPC. 1 hit. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| TIGRFAMs | TIGR03137. AhpC. 1 hit. |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AHPC_STAA8 | ||||||||
| Accession | Primary (citable) accession number: P0A0B7 Secondary accession number(s): Q2G0Z6, Q53647 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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