Reviewed, UniProtKB/Swiss-Prot P0A0B7 (AHPC_STAA8)

Names and origin

Protein names

Recommended 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

Organism

Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP]

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.4 Ref.1 Ref.3
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
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 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

	Sequence		Length	Mass (Da)
	P0A0B7-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: B7134A9C84066B73	FASTA	189	20,977
	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

References

	« Hide 'large scale' referencesShow '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].
[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.

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.
3D structure databases
SMR	P0A0B7. Positions 2-168.
ModBase	Search...
Protein-protein interaction databases
STRING	P0A0B7.
Genome annotation databases
GeneID	3919784.
GenomeReviews	Gene locus SAOUHSC_00365 in contig CP000253_GR.
KEGG	sao:SAOUHSC_00365.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0450.
HOGENOM	HBG493509.
OMA	GDLADHY.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_00365-MONOMER.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR017559. Peroxiredoxin. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
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

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)