AHPC_ECO57
ID AHPC_ECO57 Reviewed; 187 AA.
AC P0AE10; P26427;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=Z0749, ECs0644;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54940.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34067.1; -; Genomic_DNA.
DR PIR; D90709; D90709.
DR PIR; H85559; H85559.
DR RefSeq; NP_308671.1; NC_002695.1.
DR RefSeq; WP_000052796.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AE10; -.
DR SMR; P0AE10; -.
DR STRING; 155864.EDL933_0677; -.
DR EnsemblBacteria; AAG54940; AAG54940; Z0749.
DR EnsemblBacteria; BAB34067; BAB34067; ECs_0644.
DR GeneID; 66671119; -.
DR GeneID; 917003; -.
DR KEGG; ece:Z0749; -.
DR KEGG; ecs:ECs_0644; -.
DR PATRIC; fig|386585.9.peg.755; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_6; -.
DR OMA; FWYPKDF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..187
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000135116"
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
