P0AE09 (AHPC_ECOL6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 49.
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): Alkyl hydroperoxide reductase protein C22 Peroxiredoxin SCRP-23 Sulfate starvation-induced protein 8 Short name=SSI8 Thioredoxin peroxidase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 187 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Directly reduces organic hydroperoxides in its reduced dithiol form By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homodimer; disulfide-linked, upon oxidation By similarity. |
| Post-translational modification | The Cys-47-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-47 (probably Cys-SOH) rapidly reacts with Cys-166-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin By similarity. |
| Sequence similarities | Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Acetylation Disulfide bond |
| Technical term | Complete 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 By similarity | ||||||
| Chain | 2 – 187 | 186 | Alkyl hydroperoxide reductase subunit C | PRO_0000135117 | |||||
Regions | |||||||||
| Domain | 2 – 157 | 156 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 47 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 17 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 93 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 153 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 169 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 171 | 1 | N6-acetyllysine By similarity | ||||||
| Disulfide bond | 47 | Interchain (with C-166); in linked form By similarity | |||||||
| Disulfide bond | 166 | Interchain (with C-47); in linked form By similarity | |||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN79169.1. |
| RefSeq | NP_752625.1. NC_004431.1. |
3D structure databases | |
| ProteinModelPortal | P0AE09. |
| SMR | P0AE09. Positions 2-169. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0AE09. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000040763; EBESCP00000039112; EBESCG00000039813. |
| GeneID | 1035753. |
| GenomeReviews | Gene locus c0694 in contig AE014075_GR. |
| KEGG | ecc:c0694. |
| PATRIC | 18279431. VBIEscCol75197_0659. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000010351. |
| HOGENOM | HBG493509. |
| OMA | GDLADHY. |
| ProtClustDB | PRK10382. |
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_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0AE09 Secondary accession number(s): P26427 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with