MSRAB_STRGC
ID MSRAB_STRGC Reviewed; 311 AA.
AC Q9LAM9; A8AUY7;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE Short=Protein-methionine-S-oxide reductase;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB;
DE EC=1.8.4.12;
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN Name=msrAB; Synonyms=msrA; OrderedLocusNames=SGO_0278;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10678908; DOI=10.1128/iai.68.3.1061-1068.2000;
RA Vriesema A.J.M., Dankert J., Zaat S.A.J.;
RT "A shift from oral to blood pH is a stimulus for adaptive gene expression
RT of Streptococcus gordonii CH1 and induces protection against oxidative
RT stress and enhanced bacterial growth by expression of msrA.";
RL Infect. Immun. 68:1061-1068(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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 (By similarity). Involved in protection against oxidative stress when
CC the bacterium enters the host bloodstream and required for maximal
CC growth under aerobic and anaerobic conditions. {ECO:0000250,
CC ECO:0000269|PubMed:10678908}.
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 -!- 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 -!- 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 -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC sulfoxide reductase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC sulfoxide reductase family. {ECO:0000305}.
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; AF128264; AAF36477.1; -; Genomic_DNA.
DR EMBL; CP000725; ABV11083.1; -; Genomic_DNA.
DR RefSeq; WP_011999808.1; NC_009785.1.
DR AlphaFoldDB; Q9LAM9; -.
DR SMR; Q9LAM9; -.
DR STRING; 467705.SGO_0278; -.
DR EnsemblBacteria; ABV11083; ABV11083; SGO_0278.
DR KEGG; sgo:SGO_0278; -.
DR eggNOG; COG0225; Bacteria.
DR eggNOG; COG0229; Bacteria.
DR HOGENOM; CLU_031040_1_0_9; -.
DR OMA; PLRHYVL; -.
DR BRENDA; 1.8.4.12; 5934.
DR Proteomes; UP000001131; Chromosome.
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-UniRule.
DR GO; GO:0008113; F:peptide-methionine (S)-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; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR HAMAP; MF_01400; MsrB; 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 PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01625; PMSR; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome.
FT CHAIN 1..311
FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB"
FT /id="PRO_0000138516"
FT DOMAIN 172..295
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 1..155
FT /note="Peptide methionine sulfoxide reductase A"
FT ACT_SITE 10
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ SEQUENCE 311 AA; 35672 MW; 7D4B7CAF81DBE692 CRC64;
MAEIYLAGGC FWGLEEYFSR IEGVKKTTVG YANGQVESTN YQLIHQTDHA ETVHLIYDEK
RVSLREILLY YFRVIDPLSV NKQGNDVGRQ YRTGVYYTNQ ADKAVIEQVF AEQEKQLGQK
IAVELEPLRH YVLAEDYHQD YLKKNPGGYC HINVNDAYQP LVDPGQYEKP TDAELKEQLT
QEQYQVTQLS ATERPFHNAY NATFEEGIYV DVTTGEPLFF AGDKFESGCG WPSFSRPIAR
EVLRYYEDKS HGMERIEVRS RSGNAHLGHV FTDGPESAGG LRYCINSAAL RFIPKEKMEA
EGYAYLLQHM K
