AHPC_ECOL6
ID AHPC_ECOL6 Reviewed; 187 AA.
AC P0AE09; P26427;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Alkyl hydroperoxide reductase C;
DE EC=1.11.1.26 {ECO:0000250|UniProtKB:P0A251};
DE AltName: Full=Alkyl hydroperoxide reductase protein C22;
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=SCRP-23;
DE AltName: Full=Sulfate starvation-induced protein 8;
DE Short=SSI8;
DE AltName: Full=Thioredoxin peroxidase;
GN Name=ahpC; OrderedLocusNames=c0694;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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. {ECO:0000250|UniProtKB:P0A251}.
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 -!- 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}.
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DR EMBL; AE014075; AAN79169.1; -; Genomic_DNA.
DR RefSeq; WP_000052796.1; NC_004431.1.
DR AlphaFoldDB; P0AE09; -.
DR SMR; P0AE09; -.
DR STRING; 199310.c0694; -.
DR EnsemblBacteria; AAN79169; AAN79169; c0694.
DR GeneID; 66671119; -.
DR KEGG; ecc:c0694; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_6; -.
DR OMA; FWYPKDF; -.
DR BioCyc; ECOL199310:C0694-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 3: Inferred from homology;
KW Acetylation; Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase;
KW Peroxidase; Redox-active center.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..187
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000135117"
FT DOMAIN 2..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A251"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT DISULFID 47
FT /note="Interchain (with C-166); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P0A251"
FT DISULFID 166
FT /note="Interchain (with C-47); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P0A251"
SQ SEQUENCE 187 AA; 20761 MW; 40AB796E6F5CC2D6 CRC64;
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS
LDLVGKI
