ID   HPRR_MYCPN              Reviewed;         141 AA.
AC   P75170;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Hydroperoxide reductase;
DE            EC=1.11.1.-;
GN   OrderedLocusNames=MPN_625; ORFNames=C12_orf141, MP217;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND SUBUNIT.
RX   PubMed=12943365; DOI=10.1023/a:1024625122089;
RA   Choi I.G., Shin D.H., Brandsen J., Jancarik J., Busso D., Yokota H.,
RA   Kim R., Kim S.H.;
RT   "Crystal structure of a stress inducible protein from Mycoplasma pneumoniae
RT   at 2.85 A resolution.";
RL   J. Struct. Funct. Genomics 4:31-34(2003).
CC   -!- FUNCTION: Reduces organic and inorganic peroxide substrates. Protects
CC       the cell against oxidative stress (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12943365}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OsmC/Ohr family. {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; U00089; AAB95865.1; -; Genomic_DNA.
DR   PIR; S73543; S73543.
DR   RefSeq; NP_110314.1; NC_000912.1.
DR   RefSeq; WP_010874982.1; NC_000912.1.
DR   PDB; 1LQL; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J=1-141.
DR   PDBsum; 1LQL; -.
DR   AlphaFoldDB; P75170; -.
DR   SMR; P75170; -.
DR   STRING; 272634.MPN_625; -.
DR   EnsemblBacteria; AAB95865; AAB95865; MPN_625.
DR   GeneID; 66608689; -.
DR   KEGG; mpn:MPN_625; -.
DR   PATRIC; fig|272634.6.peg.689; -.
DR   HOGENOM; CLU_1862951_0_0_14; -.
DR   OMA; LMGCELS; -.
DR   BioCyc; MPNE272634:G1GJ3-1005-MON; -.
DR   EvolutionaryTrace; P75170; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.20; -; 1.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR003718; OsmC/Ohr_fam.
DR   InterPro; IPR036102; OsmC/Ohrsf.
DR   Pfam; PF02566; OsmC; 1.
DR   SUPFAM; SSF82784; SSF82784; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..141
FT                   /note="Hydroperoxide reductase"
FT                   /id="PRO_0000210607"
FT   STRAND          3..11
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   STRAND          17..21
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   HELIX           41..64
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   STRAND          69..79
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   STRAND          89..100
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   HELIX           105..118
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   HELIX           120..126
FT                   /evidence="ECO:0007829|PDB:1LQL"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:1LQL"
SQ   SEQUENCE   141 AA;  15469 MW;  07958C371E69A0A4 CRC64;
     MDKKYDITAV LNEDSSMTAI SDQFQITLDA RPKHTAKGFG PLAALLSGLA ACELATANLM
     APAKMITINK LLMNVTGSRS TNPTDGYFGL REINLHWEIH SPNSETEIKE FIDFVSKRCP
     AHNTLQGVSQ LKINVNVTLV H