ID   TPX_STREE               Reviewed;          50 AA.
AC   P42365;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Thiol peroxidase;
DE            Short=Tpx;
DE            EC=1.11.1.24 {ECO:0000269|PubMed:9141476};
DE   AltName: Full=Peroxiredoxin tpx;
DE            Short=Prx;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin;
DE   Flags: Fragment;
GN   Name=tpx;
OS   Streptococcus pneumoniae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R36A;
RX   PubMed=7505262; DOI=10.1128/iai.62.1.319-324.1994;
RA   Sampson J.S., O'Connor S.P., Stinson A.R., Tharpe J.A., Russell H.;
RT   "Cloning and nucleotide sequence analysis of psaA, the Streptococcus
RT   pneumoniae gene encoding a 37-kilodalton protein homologous to previously
RT   reported Streptococcus sp. adhesins.";
RL   Infect. Immun. 62:319-324(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-14, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=R36A;
RX   PubMed=9141476; DOI=10.1016/s0014-5793(97)00302-5;
RA   Wan X.Y., Zhou Y., Yan Z.Y., Wang H.L., Hou Y.D., Jin D.Y.;
RT   "Scavengase p20: a novel family of bacterial antioxidant enzymes.";
RL   FEBS Lett. 407:32-36(1997).
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:0000269|PubMed:9141476}.
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:0000269|PubMed:9141476};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A862}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L19055; AAA16799.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P42365; -.
DR   SMR; P42365; -.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Direct protein sequencing; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9141476"
FT   CHAIN           2..>50
FT                   /note="Thiol peroxidase"
FT                   /id="PRO_0000187914"
FT   NON_TER         50
SQ   SEQUENCE   50 AA;  5355 MW;  4FF8FB857F648B33 CRC64;
     MTTFLGNPVT FTGSQLQVGD TAHDFSLTTP NLEKKSLADF AGKKKVLSVI