ID   MSRAB_CAMFE             Reviewed;         337 AA.
AC   Q93KF3;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB;
DE   Includes:
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;
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase MsrB;
DE              EC=1.8.4.12;
DE     AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN   Name=msrAB; Synonyms=msrA;
OS   Campylobacter fetus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27374 / CIP 5396 / DSM 5361 / LMG 6442 / NCTC 10842;
RA   Thies F.L., Trotha R., Koenig W.;
RT   "Identification of genes encoding exported proteins in Campylobacter jejuni
RT   and C. fetus.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC         ChEBI:CHEBI:50058; EC=1.8.4.12;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC       sulfoxide reductase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC       sulfoxide reductase family. {ECO:0000305}.
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DR   EMBL; AJ312325; CAC42492.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93KF3; -.
DR   SMR; Q93KF3; -.
DR   STRING; 983328.AFGH01000027_gene742; -.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   HAMAP; MF_01400; MsrB; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   PANTHER; PTHR10173; PTHR10173; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme; Oxidoreductase.
FT   CHAIN           1..337
FT                   /note="Peptide methionine sulfoxide reductase MsrA/MsrB"
FT                   /id="PRO_0000138512"
FT   DOMAIN          198..321
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   REGION          28..181
FT                   /note="Peptide methionine sulfoxide reductase A"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   337 AA;  38342 MW;  4406FA3CC4BC236F CRC64;
     MKKILFVVAT IFMALFLNAK ENDMRNLKDI YLAGGCFWGT QAYFDKIRGV IKTDVGYANG
     KSDKTDYHSL HYSGHAETVH ITFDENIVSL AEILAHYFRI IDPFSVNKQG NDVGSQYRTG
     IYYNDSSLKN SISEFIKHEQ TKYDKKIAVE VEPLKNYVLA EDYHQKYLDK NPGGYCHVDL
     SLADKPLYNE SKFKAPSKDE LKAKLSDLQY SVTQEKATER PYSSEYDKFD KKGIYVDIVS
     KKPLFSSSDK FDAGCGWPSF TKPITTDALG YNRDLSHGME RVEVTSNLAN SHLGHVFTDG
     PKDKGGLRYC INGASLKFIP LEDMEKEGYK DYIIYVK