ID   TPX_LISMF               Reviewed;         165 AA.
AC   Q71Z84;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE            Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE            EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00269};
DE   AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
DE            Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00269};
GN   Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269};
GN   OrderedLocusNames=LMOf2365_1605;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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. {ECO:0000255|HAMAP-Rule:MF_00269}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00269};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269}.
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:0000255|HAMAP-Rule:MF_00269}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00269}.
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DR   EMBL; AE017262; AAT04380.1; -; Genomic_DNA.
DR   RefSeq; WP_003727378.1; NC_002973.6.
DR   AlphaFoldDB; Q71Z84; -.
DR   SMR; Q71Z84; -.
DR   KEGG; lmf:LMOf2365_1605; -.
DR   HOGENOM; CLU_042529_12_0_9; -.
DR   OMA; ITQEPNY; -.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03014; PRX_Atyp2cys; 1.
DR   HAMAP; MF_00269; Tpx; 1.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR002065; TPX.
DR   InterPro; IPR018219; Tpx_CS.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   PROSITE; PS01265; TPX; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..165
FT                   /note="Thiol peroxidase"
FT                   /id="PRO_0000187886"
FT   DOMAIN          18..164
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT   ACT_SITE        60
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
FT   DISULFID        60..94
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00269"
SQ   SEQUENCE   165 AA;  18091 MW;  B6A05B7CD2050DEF CRC64;
     MTQVTFKHNP VTLVGTERKV GDKAPNFTVV NRDLEEVTLH DYDGKVRLIS VVPSIDTSVC
     STQTRKFNEE ASNLDNTVVL TISVDLPFAQ KKWCAAEGLP NAITLSDHRD LSFGEAYGVV
     MKELRLLARS VFVVNAAGEI VYTEVVPEGS DHPNYEAAIE AAKKA