ID A0A0N7A038_9MICO Unreviewed; 134 AA.
AC A0A0N7A038;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=NI26_14085 {ECO:0000313|EMBL:AIV40936.1};
OS Curtobacterium sp. MR_MD2014.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV40936.1, ECO:0000313|Proteomes:UP000069933};
RN [1] {ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K.;
RT "Isolation and characterization of species affiliated with family
RT Actinomycetaceae.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIV40936.1, ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV40936.1,
RC ECO:0000313|Proteomes:UP000069933};
RX PubMed=26722011;
RA Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K., Dawson S.C.;
RT "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT from Topsoil in Woods Hole, Massachusetts.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP009755; AIV40936.1; -; Genomic_DNA.
DR RefSeq; WP_066656573.1; NZ_CP009755.1.
DR AlphaFoldDB; A0A0N7A038; -.
DR STRING; 1561023.NI26_14085; -.
DR KEGG; cum:NI26_14085; -.
DR PATRIC; fig|1561023.3.peg.2903; -.
DR OrthoDB; 9785497at2; -.
DR Proteomes; UP000069933; Chromosome.
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 B1; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01400};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000069933};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01400}.
FT DOMAIN 9..132
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 134 AA; 14818 MW; 39FCD3CBE71728DC CRC64;
MAYNVDKSDA QWREELSPDQ YAVLRQAGTE RPWTGELLDE ERAGTYTCAA CGAELFQSGT
KFDSGCGWPS FYESVRPEAV QLIEDKSLGM VRTEVRCANC GSHLGHVFPD GFGTPTGDRY
CMNSLSLNFS EQGE
//