ID   BCPB_MYCTO              Reviewed;         154 AA.
AC   P9WID8; L0T7E6; O53911; Q7D8A1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Putative peroxiredoxin MT1643;
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 MT1643 {ECO:0000305};
GN   Name=bcpB; Synonyms=bcp1; OrderedLocusNames=MT1643;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45912.1; -; Genomic_DNA.
DR   PIR; G70819; G70819.
DR   RefSeq; WP_003407974.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WID8; -.
DR   SMR; P9WID8; -.
DR   EnsemblBacteria; AAK45912; AAK45912; MT1643.
DR   GeneID; 45425576; -.
DR   KEGG; mtc:MT1643; -.
DR   PATRIC; fig|83331.31.peg.1766; -.
DR   HOGENOM; CLU_042529_14_2_11; -.
DR   Proteomes; UP000001020; 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; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 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..154
FT                   /note="Putative peroxiredoxin MT1643"
FT                   /id="PRO_0000428024"
FT   DOMAIN          1..153
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        44
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE52"
FT   DISULFID        44..49
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE52"
SQ   SEQUENCE   154 AA;  16894 MW;  44E62411F90946CF CRC64;
     MKTGDTVADF ELPDQTGTPR RLSVLLSDGP VVLFFYPAAM TPGCTKEACH FRDLAKEFAE
     VRASRVGIST DPVRKQAKFA EVRRFDYPLL SDAQGTVAAQ FGVKRGLLGK LMPVKRTTFV
     IDTDRKVLDV ISSEFSMDAH ADKALATLRA IRSG