ID   BCP_BUCAP               Reviewed;         158 AA.
AC   Q9ZHF0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative peroxiredoxin bcp;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P0AE52};
DE   AltName: Full=Bacterioferritin comigratory protein;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin Bcp {ECO:0000305};
GN   Name=bcp; OrderedLocusNames=BUsg_089;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-158.
RX   PubMed=9767718; DOI=10.1007/s002849900392;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes
RT   of histidine biosynthesis.";
RL   Curr. Microbiol. 37:356-358(1998).
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 and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000250|UniProtKB:P0AE52}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P0AE52};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AE52}.
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 atypical 2-Cys
CC       peroxiredoxin, C(R) is present in the same subunit to form an
CC       intramolecular disulfide. The disulfide is subsequently reduced by
CC       thioredoxin. {ECO:0000250|UniProtKB:P0AE52}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE013218; AAM67659.1; -; Genomic_DNA.
DR   EMBL; AF067228; AAC97351.1; -; Genomic_DNA.
DR   RefSeq; WP_011053625.1; NC_004061.1.
DR   AlphaFoldDB; Q9ZHF0; -.
DR   SMR; Q9ZHF0; -.
DR   STRING; 198804.BUsg_089; -.
DR   EnsemblBacteria; AAM67659; AAM67659; BUsg_089.
DR   KEGG; bas:BUsg_089; -.
DR   eggNOG; COG1225; Bacteria.
DR   HOGENOM; CLU_042529_14_1_6; -.
DR   OMA; RVVVYFY; -.
DR   OrthoDB; 1996723at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..158
FT                   /note="Putative peroxiredoxin bcp"
FT                   /id="PRO_0000135133"
FT   DOMAIN          4..157
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        46
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE52"
FT   DISULFID        46..51
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE52"
SQ   SEQUENCE   158 AA;  18138 MW;  7D06D4025FF297B5 CRC64;
     MTTLKPGDIA PKFILPNCID KSIKLSDFLG KKVLVYFYPK AMTPGCTVQA CNIRDNLELF
     KSKKVEVLGI SPDNTNKLLT FVEKKMLNFT LLSDKQNIVS KKFGVWGEKI FMGKKYFGIY
     RTSFLINSSG FIDKIFFKFK CKDHHKIILT YLNSKKSD