ID   C1CUX7_DEIDV            Unreviewed;       195 AA.
AC   C1CUX7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   04-NOV-2026, entry version 88.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000256|HAMAP-Rule:MF_01401,
GN   ECO:0000313|EMBL:ACO45994.1};
GN   OrderedLocusNames=Deide_10980 {ECO:0000313|EMBL:ACO45994.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45994.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO45994.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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       {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-
CC         methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol;
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         Evidence={ECO:0000256|ARBA:ARBA00047806, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + L-methionine + H2O = L-methionine
CC         (S)-S-oxide + [thioredoxin]-dithiol; 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         Evidence={ECO:0000256|ARBA:ARBA00048782, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401}.
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; CP001114; ACO45994.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1CUX7; -.
DR   STRING; 546414.Deide_10980; -.
DR   PaxDb; 546414-Deide_10980; -.
DR   KEGG; ddr:Deide_10980; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_0_0; -.
DR   OMA; AAEPYHQ; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0033744; F:L-methionine (S)-S-oxide reductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   PANTHER; PTHR43774; PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43774:SF1; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA 2; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01401}; Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   Signal {ECO:0000256|PROSITE-ProRule:PRU00303}.
FT   CHAIN           29..195
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5049999406"
FT   DOMAIN          21..190
FT                   /note="Peptide methionine sulphoxide reductase MsrA"
FT                   /evidence="ECO:0000259|Pfam:PF01625"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
FT   LIPID           29
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           29
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   195 AA;  21781 MW;  0EFC6CB0F5B4E954 CRC64;
     MRVFCRRQNA AMTDTAMQGM QQAILAGGCF WCTEAVMKDL RGVHKVESGY IGGHTARPDY
     RSVCSGTTGY AEAVRVTFDP AQVSFRDLLG LFFATHDPTT LNRQGADVGT QYRSAVFPLT
     PEQERETREM IADLNAQNIF EAPIVTTIEP ASEFFVAEAY HQDYYANNPN DGYCRAVIAP
     KVAKLRQYYG EKLRA
//