(data stored in ACNUC7421 zone)

SWISSPROT: 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   30-AUG-2017, entry version 79.
DE   RecName: Full=Alkyl hydroperoxide reductase C;
DE            EC=1.11.1.15;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
CC       of hydrogen peroxide and organic hydroperoxides to water and
CC       alcohols, respectively. Plays a role in cell protection against
CC       oxidative stress by detoxifying peroxides.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC       assemble to form a ring-like decamer.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active
CC       cysteine residue, the peroxidatic cysteine (C(P)), which makes the
CC       nucleophilic attack on the peroxide substrate. The peroxide
CC       oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
CC       then reacts with another cysteine residue, the resolving cysteine
CC       (C(R)), to form a disulfide bridge. The disulfide is subsequently
CC       reduced by an appropriate electron donor to complete the catalytic
CC       cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
CC       the other dimeric subunit to form an intersubunit disulfide. The
CC       disulfide is subsequently reduced by AhpF.
CC       {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
CC       subfamily. {ECO:0000305}.
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_MWVM01000011.1.
DR   ProteinModelPortal; P0AE10; -.
DR   SMR; P0AE10; -.
DR   STRING; 155864.Z0749; -.
DR   PRIDE; P0AE10; -.
DR   EnsemblBacteria; AAG54940; AAG54940; Z0749.
DR   EnsemblBacteria; BAB34067; BAB34067; BAB34067.
DR   GeneID; 917003; -.
DR   KEGG; ece:Z0749; -.
DR   KEGG; ecs:ECs0644; -.
DR   PATRIC; fig|386585.9.peg.755; -.
DR   eggNOG; ENOG4105D3R; Bacteria.
DR   eggNOG; COG0450; LUCA.
DR   HOGENOM; HOG000022343; -.
DR   KO; K03386; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; 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; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF128; PTHR10681:SF128; 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;
DR   PRODOM; P0AE10.
DR   SWISS-2DPAGE; P0AE10.
KW   Acetylation; Antioxidant; Complete proteome; Cytoplasm;
KW   Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    187       Alkyl hydroperoxide reductase C.
FT                                /FTId=PRO_0000135116.
FT   DOMAIN        2    157       Thioredoxin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   ACT_SITE     47     47       Cysteine sulfenic acid (-SOH)
FT                                intermediate.
FT                                {ECO:0000250|UniProtKB:P0A251}.
FT   MOD_RES      17     17       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      93     93       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     153    153       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     169    169       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     171    171       N6-acetyllysine. {ECO:0000250}.
FT   DISULFID     47     47       Interchain (with C-166); in linked form.
FT                                {ECO:0000250|UniProtKB:P0A251}.
FT   DISULFID    166    166       Interchain (with C-47); in linked form.
FT                                {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
//

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