ID   MSRB_ENTFT              Reviewed;         145 AA.
AC   E6ESW1; Q9XB39;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400};
DE            EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400};
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400}; Synonyms=csrA;
GN   ORFNames=HMPREF9496_02734;
OS   Enterococcus faecalis (strain TX4000 / JH2-2).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=749493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND PROTEIN SEQUENCE OF 1-25.
RC   STRAIN=TX4000 / JH2-2;
RX   PubMed=10919327; DOI=10.1007/s002530000350;
RA   Laplace J.M., Hartke A., Giard J.-C., Auffray Y.;
RT   "Cloning, characterization and expression of an Enterococcus faecalis gene
RT   responsive to heavy metals.";
RL   Appl. Microbiol. Biotechnol. 53:685-689(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX4000 / JH2-2;
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01400};
CC   -!- INDUCTION: By cadmium, lead, mercury, copper and manganese.
CC       {ECO:0000269|PubMed:10919327}.
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01400}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFT40245.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ243482; CAB46979.1; -; Genomic_DNA.
DR   EMBL; AEBB01000072; EFT40245.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002354871.1; NZ_GL476298.1.
DR   AlphaFoldDB; E6ESW1; -.
DR   SMR; E6ESW1; -.
DR   GeneID; 60892404; -.
DR   PATRIC; fig|749493.3.peg.2585; -.
DR   HOGENOM; CLU_031040_8_5_9; -.
DR   GO; GO:0033743; F:peptide-methionine (R)-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   HAMAP; MF_01400; MsrB; 1.
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; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Stress response.
FT   CHAIN           1..145
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_0000422421"
FT   DOMAIN          6..129
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   CONFLICT        136..145
FT                   /note="GYGEYLSLFK -> AMANTFLYSNNPHFLDKYDKIVRKKATFDEYLV (in
FT                   Ref. 1; CAB46979)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   145 AA;  16351 MW;  827563D046ED213E CRC64;
     MTKPTEEELK QTLTDLQYAV TQENATERPF SGEYDDFYQD GIYVDIVSGE PLFSSLDKYD
     AGCGWPSFTK PIEKRGVKEK ADFSHGMHRV EVRSQEADSH LGHVFTDGPL QEGGLRYCIN
     AAALRFVPVA DLEKEGYGEY LSLFK