MSAB1_STRR6
ID MSAB1_STRR6 Reviewed; 312 AA.
AC P0A3R0; P35593;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB 1;
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=msrAB1; Synonyms=exp3, msrA; OrderedLocusNames=spr1217;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, POSSIBLE FUNCTION IN
RP VIRULENCE, AND DISRUPTION PHENOTYPE.
RX PubMed=8755589; DOI=10.1073/pnas.93.15.7985;
RA Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G., So M.,
RA Weissbach H., Brot N., Masure H.R.;
RT "Peptide methionine sulfoxide reductase contributes to the maintenance of
RT adhesins in three major pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-249.
RX PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
RA Pearce B.J., Yin Y.B., Masure H.R.;
RT "Genetic identification of exported proteins in Streptococcus pneumoniae.";
RL Mol. Microbiol. 9:1037-1050(1993).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation (By similarity). Catalyzes the
CC reversible oxidation-reduction of methionine sulfoxide in proteins to
CC methionine. {ECO:0000250}.
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 Evidence={ECO:0000269|PubMed:8755589};
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 Evidence={ECO:0000269|PubMed:8755589};
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:0000269|PubMed:8755589};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits decreased binding to GalNAcbeta1-
CC 4Gal containing receptors that are present on type II lung cells and
CC vascular endothelial cells. {ECO:0000269|PubMed:8755589}.
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}.
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DR EMBL; U41735; AAC44298.1; -; Genomic_DNA.
DR EMBL; AE007317; AAL00021.1; -; Genomic_DNA.
DR PIR; H98023; H98023.
DR RefSeq; NP_358810.1; NC_003098.1.
DR RefSeq; WP_000818207.1; NC_003098.1.
DR AlphaFoldDB; P0A3R0; -.
DR SMR; P0A3R0; -.
DR STRING; 171101.spr1217; -.
DR EnsemblBacteria; AAL00021; AAL00021; spr1217.
DR GeneID; 60233101; -.
DR KEGG; spr:spr1217; -.
DR PATRIC; fig|171101.6.peg.1321; -.
DR eggNOG; COG0225; Bacteria.
DR eggNOG; COG0229; Bacteria.
DR HOGENOM; CLU_031040_1_0_9; -.
DR OMA; PLRHYVL; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Multifunctional enzyme; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..312
FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB 1"
FT /id="PRO_0000138518"
FT DOMAIN 172..295
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 1..155
FT /note="Peptide methionine sulfoxide reductase"
FT ACT_SITE 10
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT CONFLICT 29
FT /note="V -> G (in Ref. 1; AAC44298)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="K -> E (in Ref. 1; AAC44298)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..57
FT /note="TVQVIY -> AVRVIC (in Ref. 1; AAC44298)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="E -> G (in Ref. 1; AAC44298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35703 MW; 6F3873FCE9C1F6E1 CRC64;
MAEIYLAGGC FWGLEEYFSR ISGVLETSVG YANGQVETTN YQLLKETDHA ETVQVIYDEK
EVSLREILLY YFRVIDPLSI NQQGNDRGRQ YRTGIYYQDE ADLPAIYTVV QEQERMLGRK
IAVEVEQLRH YILAEDYHQD YLRKNPSGYC HIDVTDADKP LIDAANYEKP SQEVLKASLS
EESYRVTQEA ATEAPFTNAY DQTFEEGIYV DITTGEPLFF AKDKFASGCG WPSFSRPISK
ELIHYYKDLS HGMERIEVRS RSGSAHLGHV FTDGPRELGG LRYCINSASL RFVAKDEMEK
AGYGYLLPYL NK
