ID   MSRA_ACIC5              Reviewed;         156 AA.
AC   C1F1B8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000255|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000255|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000255|HAMAP-Rule:MF_01401}; OrderedLocusNames=ACP_2424;
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC   13165 / 161;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(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:0000255|HAMAP-Rule:MF_01401}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000255|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; CP001472; ACO31447.1; -; Genomic_DNA.
DR   RefSeq; WP_015897508.1; NC_012483.1.
DR   AlphaFoldDB; C1F1B8; -.
DR   SMR; C1F1B8; -.
DR   STRING; 240015.ACP_2424; -.
DR   EnsemblBacteria; ACO31447; ACO31447; ACP_2424.
DR   KEGG; aca:ACP_2424; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_0_0; -.
DR   OMA; GYCAFVV; -.
DR   OrthoDB; 1554384at2; -.
DR   Proteomes; UP000002207; Chromosome.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..156
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_1000184557"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   156 AA;  17808 MW;  D49F03A425CC9D8D CRC64;
     MAKATFGAGC FWGVEASFRQ LHGVQDVAAG YEGGKLDNPT YRDVCTDLTG HAEVVEIDFN
     PDEIRFEQLL EAFFGLHDPT QLNRQGPDWG TQYRSVIFYH SPEQQTVAQA FIDRLTAEKR
     FPRPIVTQVV PAATFWRAEE YHQRYLEKRG LATCHI