(data stored in ACNUC7421 zone)

SWISSPROT: AHPC_PSEAB

ID   AHPC_PSEAB              Reviewed;         187 AA.
AC   Q02UU0;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   30-AUG-2017, entry version 61.
DE   RecName: Full=Alkyl hydroperoxide reductase C;
DE            EC=1.11.1.15;
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
GN   Name=ahpC; OrderedLocusNames=PA14_01710;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA   Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT   "Potential of liquid-isoelectric-focusing protein fractionation to
RT   improve phosphoprotein characterization of Pseudomonas aeruginosa
RT   PA14.";
RL   Anal. Bioanal. Chem. 406:6297-6309(2014).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=24965220; DOI=10.1002/pmic.201400190;
RA   Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT   "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT   aeruginosa PA14 strain.";
RL   Proteomics 14:2017-2030(2014).
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       Secreted {ECO:0000269|PubMed:24965220}. Note=Could be present
CC       extracellularly due to cell lysis. {ECO:0000305}.
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; CP000438; ABJ15095.1; -; Genomic_DNA.
DR   RefSeq; WP_003083828.1; NC_008463.1.
DR   ProteinModelPortal; Q02UU0; -.
DR   SMR; Q02UU0; -.
DR   PRIDE; Q02UU0; -.
DR   EnsemblBacteria; ABJ15095; ABJ15095; PA14_01710.
DR   KEGG; pau:PA14_01710; -.
DR   HOGENOM; HOG000022343; -.
DR   KO; K03386; -.
DR   OMA; CPANWEE; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
DR   PRODOM; Q02UU0.
DR   SWISS-2DPAGE; Q02UU0.
KW   Antioxidant; Complete proteome; Cytoplasm; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center; Secreted.
FT   CHAIN         1    187       Alkyl hydroperoxide reductase C.
FT                                /FTId=PRO_0000431344.
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   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;  20541 MW;  A66BCCFACB5FE185 CRC64;
     MSLINTQVQP FKVNAFHNGK FIEVTEESLK GKWSVLIFMP AAFTFNCPTE IEDAANNYGE
     FQKAGAEVYI VTTDTHFSHK VWHETSPAVG KAQFPLIGDP THQLTNAFGV HIPEEGLALR
     GTFVINPEGV IKTVEIHSNE IARDVGETVR KLKAAQYTAA HPGEVCPAKW KEGEKTLAPS
     LDLVGKI
//

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