HPRR_MYCGE
ID HPRR_MYCGE Reviewed; 141 AA.
AC P47666;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Hydroperoxide reductase;
DE EC=1.11.1.-;
GN OrderedLocusNames=MG427;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP FUNCTION AS A PEROXIDASE, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=24363346; DOI=10.1128/jb.00954-13;
RA Zhang W., Baseman J.B.;
RT "Functional characterization of osmotically inducible protein C (MG_427)
RT from Mycoplasma genitalium.";
RL J. Bacteriol. 196:1012-1019(2014).
CC -!- FUNCTION: Reduces organic and inorganic peroxide substrates. Protects
CC the cell against oxidative stress. {ECO:0000269|PubMed:24363346}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24363346}. Note=A
CC small fraction is associated with the cell membrane.
CC -!- INDUCTION: Down-regulated by osmotic shock and ethanol. Not induced by
CC oxidative stress. {ECO:0000269|PubMed:24363346}.
CC -!- DISRUPTION PHENOTYPE: Mutant is highly sensitive to killing by tert-
CC butyl hydroperoxide (t-BHP) and H(2)O(2).
CC {ECO:0000269|PubMed:24363346}.
CC -!- SIMILARITY: Belongs to the OsmC/Ohr family. {ECO:0000305}.
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DR EMBL; L43967; AAC72448.1; -; Genomic_DNA.
DR PIR; B64247; B64247.
DR RefSeq; WP_009885605.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47666; -.
DR SMR; P47666; -.
DR STRING; 243273.MG_427; -.
DR EnsemblBacteria; AAC72448; AAC72448; MG_427.
DR KEGG; mge:MG_427; -.
DR eggNOG; COG1765; Bacteria.
DR HOGENOM; CLU_100275_2_1_14; -.
DR OMA; LMGCELS; -.
DR OrthoDB; 1430018at2; -.
DR BioCyc; MGEN243273:G1GJ2-521-MON; -.
DR Proteomes; UP000000807; 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 Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..141
FT /note="Hydroperoxide reductase"
FT /id="PRO_0000210606"
SQ SEQUENCE 141 AA; 15603 MW; CF64701E8AEFE393 CRC64;
MDKKYDITAV LNDDSSINAV SDNFQITLDA RPKEKSKGIN PLSAFLAGLA ACELATANAM
AAAKMITLNK ALINIKGYRL TNPSDGYFGL RELNIHWEIH SPNEEEEIKE FIDFVSKRCP
AHNTLHGTSN FKINISVTLV H