AHPC_STAA8
ID AHPC_STAA8 Reviewed; 189 AA.
AC P0A0B7; Q2G0Z6; Q53647;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Alkyl hydroperoxide reductase C;
DE EC=1.11.1.26 {ECO:0000250|UniProtKB:P0A251};
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=Thioredoxin peroxidase;
GN Name=ahpC; OrderedLocusNames=SAOUHSC_00365;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, AND INDUCTION
RP BY OSMOTIC UPSHOCK.
RX PubMed=7551034; DOI=10.1099/13500872-141-7-1655;
RA Armstrong-Buisseret L., Cole M.B., Stewart G.S.A.B.;
RT "A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is
RT induced by osmotic upshock in Staphylococcus aureus.";
RL Microbiology 141:1655-1661(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP INDUCTION BY METALS, AND REGULATION BY FUR AND PERR.
RX PubMed=14742543; DOI=10.1128/iai.72.2.972-979.2004;
RA Morrissey J.A., Cockayne A., Brummell K., Williams P.;
RT "The staphylococcal ferritins are differentially regulated in response to
RT iron and manganese and via perR and fur.";
RL Infect. Immun. 72:972-979(2004).
RN [4]
RP FUNCTION, AND REGULATION BY PERR.
RX PubMed=17114262; DOI=10.1128/jb.01524-06;
RA Cosgrove K., Coutts G., Jonsson I.-M., Tarkowski A., Kokai-Kun J.F.,
RA Mond J.J., Foster S.J.;
RT "Catalase (katA) and alkyl hydroperoxide reductase (ahpC) have compensatory
RT roles in peroxide stress resistance and are required for survival,
RT persistence and nasal colonization in Staphylococcus aureus.";
RL J. Bacteriol. 189:1025-1035(2007).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. Is important for survival under desiccation
CC conditions. Not required for virulence although is necessary for nasal
CC colonization. {ECO:0000269|PubMed:17114262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.11.1.26;
CC Evidence={ECO:0000250|UniProtKB:P0A251};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer. {ECO:0000250|UniProtKB:P0A251}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
CC -!- INDUCTION: Induced by iron and osmotic shock. Repressed under metal-
CC depleted growth conditions and by manganese-rich growth conditions.
CC Negatively regulated by the ferric uptake regulator (Fur) and PerR.
CC {ECO:0000269|PubMed:14742543, ECO:0000269|PubMed:7551034}.
CC -!- MISCELLANEOUS: In S.aureus, the removal of hydrogen peroxide appears to
CC occur predominately via KatA, with AhpC acting as an alternative.
CC {ECO:0000305|PubMed:17114262}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by AhpF.
CC {ECO:0000250|UniProtKB:P0A251}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U92441; AAB51151.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29531.1; -; Genomic_DNA.
DR PIR; S52934; S52934.
DR RefSeq; WP_000052781.1; NZ_LS483365.1.
DR RefSeq; YP_498954.1; NC_007795.1.
DR AlphaFoldDB; P0A0B7; -.
DR SMR; P0A0B7; -.
DR STRING; 1280.SAXN108_0431; -.
DR EnsemblBacteria; ABD29531; ABD29531; SAOUHSC_00365.
DR GeneID; 3919784; -.
DR KEGG; sao:SAOUHSC_00365; -.
DR PATRIC; fig|93061.5.peg.335; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_9; -.
DR OMA; FWYPKDF; -.
DR PRO; PR:P0A0B7; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0102039; F:alkylhydroperoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR017559; AhpC.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR03137; AhpC; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:7551034"
FT CHAIN 2..189
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000135128"
FT DOMAIN 2..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A251"
FT DISULFID 49
FT /note="Interchain (with C-168); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P0A251"
FT DISULFID 168
FT /note="Interchain (with C-49); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P0A251"
FT CONFLICT 2
FT /note="S -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="D -> DD (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 20977 MW; B7134A9C84066B73 CRC64;
MSLINKEILP FTAQAFDPKK DQFKEVTQED LKGSWSVVCF YPADFSFVCP TELEDLQNQY
EELQKLGVNV FSVSTDTHFV HKAWHDHSDA ISKITYTMIG DPSQTITRNF DVLDEATGLA
QRGTFIIDPD GVVQASEINA DGIGRDASTL AHKIKAAQYV RKNPGEVCPA KWEEGAKTLQ
PGLDLVGKI
