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   16-JUN-2009, entry version 31.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit C;
DE            EC=1.11.1.15;
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Alkyl hydroperoxide reductase protein C22;
DE   AltName: Full=SCRP-23;
DE   AltName: Full=Sulfate starvation-induced protein 8;
DE            Short=SSI8;
GN   Name=ahpC; OrderedLocusNames=c0694;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Directly reduces organic hydroperoxides in its reduced
CC       dithiol form (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By
CC       similarity).
CC   -!- PTM: The Cys-47-SH group is the primary site of oxidation by
CC       H(2)O(2), and the oxidized Cys-47 (probably Cys-SOH) rapidly
CC       reacts with Cys-166-SH of the other subunit to form an
CC       intermolecular disulfide. This disulfide is subsequently reduced
CC       by thioredoxin (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AE014075; AAN79169.1; -; Genomic_DNA.
DR   RefSeq; NP_752625.1; -.
DR   HSSP; P19479; 1N8J.
DR   SMR; P0AE09; 2-187.
DR   GeneID; 1035753; -.
DR   GenomeReviews; AE014075_GR; c0694.
DR   KEGG; ecc:c0694; -.
DR   HOGENOM; P0AE09; -.
DR   OMA; P0AE09; GDLADHY.
DR   BRENDA; 1.11.1.15; 292881.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000866; Alkyl_hydroperoxide_Rdtase.
DR   InterPro; IPR017559; Peroxiredoxin.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   TIGRFAMs; TIGR03137; AhpC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Antioxidant; Complete proteome; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    187       Alkyl hydroperoxide reductase subunit C.
FT                                /FTId=PRO_0000135117.
FT   DOMAIN        2    157       Thioredoxin.
FT   ACT_SITE     47     47       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   MOD_RES      17     17       N6-acetyllysine (By similarity).
FT   MOD_RES      93     93       N6-acetyllysine (By similarity).
FT   MOD_RES     153    153       N6-acetyllysine (By similarity).
FT   MOD_RES     169    169       N6-acetyllysine (By similarity).
FT   MOD_RES     171    171       N6-acetyllysine (By similarity).
FT   DISULFID     47     47       Interchain (with C-166); in linked form
FT                                (By similarity).
FT   DISULFID    166    166       Interchain (with C-47); in linked form
FT                                (By similarity).
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
//