MSRA_MYCGE
ID MSRA_MYCGE Reviewed; 157 AA.
AC P47648;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE Short=Protein-methionine-S-oxide reductase;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
GN Name=msrA; Synonyms=pmsR; OrderedLocusNames=MG408;
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 POSSIBLE FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=11544227; DOI=10.1128/jb.183.19.5645-5650.2001;
RA Dhandayuthapani S., Blaylock M.W., Bebear C.M., Rasmussen W.G.,
RA Baseman J.B.;
RT "Peptide methionine sulfoxide reductase (MsrA) is a virulence determinant
RT in Mycoplasma genitalium.";
RL J. Bacteriol. 183:5645-5650(2001).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
CC -!- DISRUPTION PHENOTYPE: Decreased agglutination to sheep erythrocytes and
CC survival in hamster lungs and increased sensitivity to hydrogen
CC peroxide. {ECO:0000269|PubMed:11544227}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; L43967; AAC71636.1; -; Genomic_DNA.
DR PIR; B64245; B64245.
DR RefSeq; WP_010869470.1; NC_000908.2.
DR AlphaFoldDB; P47648; -.
DR SMR; P47648; -.
DR STRING; 243273.MG_408; -.
DR PRIDE; P47648; -.
DR EnsemblBacteria; AAC71636; AAC71636; MG_408.
DR KEGG; mge:MG_408; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_2_14; -.
DR OMA; GYCAFVV; -.
DR OrthoDB; 1554384at2; -.
DR BioCyc; MGEN243273:G1GJ2-505-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..157
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_0000138556"
FT ACT_SITE 10
FT /evidence="ECO:0000250"
SQ SEQUENCE 157 AA; 18415 MW; 1938A53365982705 CRC64;
MKEIYFGGGC FWGIEKYFQL IKGVKKTSVG YLNSRIRNPS YEQVCSGYTN AVEAVKVEYE
EKEISLSELI EALFEVIDPT IRNRQGNDIG TQYRTGIYWT DSSDEKIIND KFLKLQKNYS
KPIVTENKKV ENYYLAEEYH QDYLKKNPNG YCHIKFD
