ID A0A411EBT6_9FLAO Unreviewed; 153 AA.
AC A0A411EBT6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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:QBA65004.1};
GN ORFNames=EQY75_10965 {ECO:0000313|EMBL:QBA65004.1};
OS Muriicola soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Muriicola.
OX NCBI_TaxID=2507538 {ECO:0000313|EMBL:QBA65004.1, ECO:0000313|Proteomes:UP000290889};
RN [1] {ECO:0000313|EMBL:QBA65004.1, ECO:0000313|Proteomes:UP000290889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY002 {ECO:0000313|EMBL:QBA65004.1,
RC ECO:0000313|Proteomes:UP000290889};
RA Kang H.J., Kim S.B.;
RT "Muriicola soli sp. nov., isolated from soil.";
RL Submitted (JAN-2019) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP035544; QBA65004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411EBT6; -.
DR KEGG; mur:EQY75_10965; -.
DR OrthoDB; 4174719at2; -.
DR Proteomes; UP000290889; 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 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:UP000290889};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01400}.
FT DOMAIN 26..148
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 153 AA; 17073 MW; E45034C9B2702471 CRC64;
MLNWKDIMHF AVSGNPVPSK RVEKTEAEWK EILTPDQFRI TRKKGTEAPH SGELCSIHEA
GKYACVCCGT PLFDSTIKFE SGTGWPSFTQ PIEENAIKYE KDSSYGMVRV EVMCNTCDAH
LGHVFPDGPQ PSGLRYCINS ESMKLLKKAD VGE
//
