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Database: UniProt
Entry: A0A139NJI3_9STRE
LinkDB: A0A139NJI3_9STRE
Original site: A0A139NJI3_9STRE 
ID   A0A139NJI3_9STRE        Unreviewed;       311 AA.
AC   A0A139NJI3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=STRDD12_00696 {ECO:0000313|EMBL:KXT76200.1};
OS   Streptococcus sp. DD12.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT76200.1, ECO:0000313|Proteomes:UP000070638};
RN   [1] {ECO:0000313|EMBL:KXT76200.1, ECO:0000313|Proteomes:UP000070638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD12 {ECO:0000313|EMBL:KXT76200.1,
RC   ECO:0000313|Proteomes:UP000070638};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) 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       {ECO:0000256|HAMAP-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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001063, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
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         Evidence={ECO:0000256|ARBA:ARBA00001795};
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         Evidence={ECO:0000256|ARBA:ARBA00001497, 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   -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC       sulfoxide reductase family. {ECO:0000256|ARBA:ARBA00008076}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC       sulfoxide reductase family. {ECO:0000256|ARBA:ARBA00011017}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT76200.1}.
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DR   EMBL; LQRG01000009; KXT76200.1; -; Genomic_DNA.
DR   RefSeq; WP_066915173.1; NZ_KQ969495.1.
DR   AlphaFoldDB; A0A139NJI3; -.
DR   STRING; 1777880.STRDD12_00696; -.
DR   PATRIC; fig|1777880.3.peg.718; -.
DR   OrthoDB; 4174719at2; -.
DR   Proteomes; UP000070638; Unassembled WGS sequence.
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-EC.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036211; P:protein modification process; 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; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
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   InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR   PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR10173:SF59; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA/MSRB 1; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01401}; Reference proteome {ECO:0000313|Proteomes:UP000070638}.
FT   DOMAIN          172..295
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   311 AA;  35161 MW;  D8D0F722CEA8DB37 CRC64;
     MAEIYLAGGC FWGLQAYFER IPGVEKTSVG YANGQVTTTN YQLIKETDHA ETVQVIYDAK
     QVSLRELLLY YFRVIDPLSV NRQGNDQGRQ YRTGVYYTDD ADRPIIAAVF SEEEAQLGRK
     LAVELEPLRH YVLAEDYHQD YLKKNPSGYC HIDVTQADQP LIDPAAYPRP SQEELKTTLS
     KEAYQVTQEG ATEAPFQNAY DQTFEEGLYV DVTTGEPLFL AKDKFASACG WPSFSRPIAK
     EVVQYLEDKS YGMDRIEVRS RSGRAHLGHV FPDGPDDRGG LRYCINSAAL KFIPKDEMAE
     KGYGDLLQVM N
//
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