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P0A0B7 (AHPC_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alkyl hydroperoxide reductase subunit C

EC=1.11.1.15
Alternative name(s):
Peroxiredoxin
Thioredoxin peroxidase
Gene names
Name:ahpC
Ordered Locus Names:SAOUHSC_00365
OrganismStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 189188Alkyl hydroperoxide reductase subunit C
PRO_0000135128

Regions

Domain2 – 159158Thioredoxin

Sites

Active site491Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond49Interchain (with C-168); in linked form By similarity
Disulfide bond168Interchain (with C-49); in linked form By similarity

Experimental info

Sequence conflict21S → G AA sequence Ref.1
Sequence conflict171D → DD AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0A0B7 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: B7134A9C84066B73

FASTA18920,977
        10         20         30         40         50         60 
MSLINKEILP FTAQAFDPKK DQFKEVTQED LKGSWSVVCF YPADFSFVCP TELEDLQNQY 

        70         80         90        100        110        120 
EELQKLGVNV FSVSTDTHFV HKAWHDHSDA ISKITYTMIG DPSQTITRNF DVLDEATGLA 

       130        140        150        160        170        180 
QRGTFIIDPD GVVQASEINA DGIGRDASTL AHKIKAAQYV RKNPGEVCPA KWEEGAKTLQ 


PGLDLVGKI 

« Hide

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.
PIRS52934.
RefSeqYP_498954.1. NC_007795.1.

3D structure databases

ProteinModelPortalP0A0B7.
SMRP0A0B7. Positions 2-168.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A0B7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000030036; EBSTAP00000028987; EBSTAG00000030034.
GeneID3919784.
GenomeReviewsGene locus SAOUHSC_00365 in contig CP000253_GR.
KEGGsao:SAOUHSC_00365.
PATRIC19578318. VBIStaAur99865_0335.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeEBGT00050000024736.
HOGENOMHBG493509.
OMAGDLADHY.
ProtClustDBCLSK884603.

Enzyme and pathway databases

BioCycSAUR93061:SAOUHSC_00365-MONOMER.

Family and domain databases

InterProIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK03386.
PANTHERPTHR10681:SF7. PTHR10681:SF7. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMsTIGR03137. AhpC. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAHPC_STAA8
AccessionPrimary (citable) accession number: P0A0B7
Secondary accession number(s): Q2G0Z6, Q53647
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families