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Database: UniProt
Entry: A0A2P7EHW2_9SYNE
LinkDB: A0A2P7EHW2_9SYNE
Original site: A0A2P7EHW2_9SYNE 
ID   A0A2P7EHW2_9SYNE        Unreviewed;       127 AA.
AC   A0A2P7EHW2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
DE            EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400,
GN   ECO:0000313|EMBL:PSI02802.1};
GN   ORFNames=C7K08_01180 {ECO:0000313|EMBL:PSI02802.1};
OS   Synechococcus lacustris str. Tous.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1910958 {ECO:0000313|EMBL:PSI02802.1, ECO:0000313|Proteomes:UP000240206};
RN   [1] {ECO:0000313|Proteomes:UP000240206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tous {ECO:0000313|Proteomes:UP000240206};
RA   Cabello-Yeves P.J., Picazo A., Camacho A., Callieri C., Rosselli R.,
RA   Roda-Garcia J., Coutinho F.H., Rodriguez-Valera F.;
RT   "Ecological and genomic features of two cosmopolitan and abundant
RT   freshwater picocyanobacteria.";
RL   Submitted (MAR-2018) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001795, ECO:0000256|HAMAP-
CC         Rule:MF_01400};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01400};
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC       structural integrity of the protein. {ECO:0000256|HAMAP-Rule:MF_01400};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01400}.
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:PSI02802.1}.
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DR   EMBL; PXVC01000002; PSI02802.1; -; Genomic_DNA.
DR   STRING; 1910958.BTM30_03310; -.
DR   Proteomes; UP000240206; Unassembled WGS sequence.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; 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   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   NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR   PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR10173:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B3; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01400};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000240206};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01400}.
FT   DOMAIN          5..127
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   UNSURE          72
FT                   /note="D or N"
FT                   /evidence="ECO:0000313|EMBL:PSI02802.1"
SQ   SEQUENCE   127 AA;  14162 MW;  A03A4E88C1573230 CRC64;
     MKLSPEEWRA KLSQEQYQVA REGGTERAFT GVYWNHKGKG TYRCVCCNSE LFKSEAKFDS
     GTGWPSFWQG VDPAAISIHQ DESHGMVRTE IXCANCDAHL GHVFNDGPAP TGERYCVNSA
     SLNFEAE
//
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