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Database: UniProt
Entry: D5ASW0_RHOCB
LinkDB: D5ASW0_RHOCB
Original site: D5ASW0_RHOCB 
ID   D5ASW0_RHOCB            Unreviewed;       148 AA.
AC   D5ASW0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
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=msrB2 {ECO:0000313|EMBL:ADE87201.1};
GN   Synonyms=msrB {ECO:0000256|HAMAP-Rule:MF_01400};
GN   OrderedLocusNames=RCAP_rcc03477 {ECO:0000313|EMBL:ADE87201.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE87201.1, ECO:0000313|Proteomes:UP000002361};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SB1003;
RA   Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA   Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA   Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA   Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT   "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADE87201.1, ECO:0000313|Proteomes:UP000002361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC   {ECO:0000313|Proteomes:UP000002361};
RX   PubMed=20418398; DOI=10.1128/JB.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01400}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}.
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DR   EMBL; CP001312; ADE87201.1; -; Genomic_DNA.
DR   RefSeq; WP_013069173.1; NC_014034.1.
DR   AlphaFoldDB; D5ASW0; -.
DR   STRING; 272942.RCAP_rcc03477; -.
DR   GeneID; 31492259; -.
DR   KEGG; rcp:RCAP_rcc03477; -.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_8_5_5; -.
DR   OMA; KCKLDMS; -.
DR   OrthoDB; 9785497at2; -.
DR   Proteomes; UP000002361; Chromosome.
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   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:SF59; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA/MSRB 1; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000002361}.
FT   DOMAIN          8..131
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        120
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ   SEQUENCE   148 AA;  16661 MW;  D2B85FC5982AEE0E CRC64;
     MDKKYRKTPE ALARLTAEQF RVTQESGTER AFTGAFWNTT DPGLYVDVVS GEPLFSSRDK
     FESGCGWPSF TRPVVPAHVT EHRDVSHGMI RTEVRSMHGD SHLGHVFPDG PRDRGGLRYC
     INSASLRFIP KDRMEAEGYG DWLAELEG
//
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