MSRB_ECOLI
ID MSRB_ECOLI Reviewed; 137 AA.
AC P0A746; P39903; P76232; P76912;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=msrB; Synonyms=yeaA; OrderedLocusNames=b1778, JW1767;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RX PubMed=2990926; DOI=10.1111/j.1432-1033.1985.tb08988.x;
RA Branlant G., Branlant C.;
RT "Nucleotide sequence of the Escherichia coli gap gene. Different
RT evolutionary behavior of the NAD+-binding domain and of the catalytic
RT domain of D-glyceraldehyde-3-phosphate dehydrogenase.";
RL Eur. J. Biochem. 150:61-66(1985).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11677230; DOI=10.1074/jbc.m105509200;
RA Grimaud R., Ezraty B., Mitchell J.K., Lafitte D., Briand C., Derrick P.J.,
RA Barras F.;
RT "Repair of oxidized proteins. Identification of a new methionine sulfoxide
RT reductase.";
RL J. Biol. Chem. 276:48915-48920(2001).
RN [7]
RP CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-46;
RP CYS-49; CYS-95 AND CYS-98.
RC STRAIN=K12;
RX PubMed=16251365; DOI=10.1110/ps.051711105;
RA Olry A., Boschi-Muller S., Yu H., Burnel D., Branlant G.;
RT "Insights into the role of the metal binding site in methionine-R-sulfoxide
RT reductases B.";
RL Protein Sci. 14:2828-2837(2005).
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:16251365};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16251365};
CC Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC structural integrity of the protein. {ECO:0000269|PubMed:16251365};
CC -!- MASS SPECTROMETRY: Mass=15319; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16251365};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X02662; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74848.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15575.2; -; Genomic_DNA.
DR EMBL; X02662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B64938; B64938.
DR RefSeq; NP_416292.1; NC_000913.3.
DR RefSeq; WP_001284618.1; NZ_SSZK01000001.1.
DR PDB; 6SYM; X-ray; 1.63 A; A/B=1-137.
DR PDBsum; 6SYM; -.
DR AlphaFoldDB; P0A746; -.
DR SMR; P0A746; -.
DR BioGRID; 4260307; 54.
DR BioGRID; 851520; 1.
DR DIP; DIP-48167N; -.
DR IntAct; P0A746; 4.
DR STRING; 511145.b1778; -.
DR jPOST; P0A746; -.
DR PaxDb; P0A746; -.
DR PRIDE; P0A746; -.
DR DNASU; 947188; -.
DR EnsemblBacteria; AAC74848; AAC74848; b1778.
DR EnsemblBacteria; BAA15575; BAA15575; BAA15575.
DR GeneID; 58462326; -.
DR GeneID; 947188; -.
DR KEGG; ecj:JW1767; -.
DR KEGG; eco:b1778; -.
DR PATRIC; fig|1411691.4.peg.476; -.
DR EchoBASE; EB2295; -.
DR eggNOG; COG0229; Bacteria.
DR HOGENOM; CLU_031040_8_5_6; -.
DR InParanoid; P0A746; -.
DR OMA; DEQWRAE; -.
DR PhylomeDB; P0A746; -.
DR BioCyc; EcoCyc:EG12394-MON; -.
DR BioCyc; MetaCyc:EG12394-MON; -.
DR BRENDA; 1.8.4.12; 2026.
DR PRO; PR:P0A746; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoliWiki.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:EcoliWiki.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0030091; P:protein repair; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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 PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..137
FT /note="Peptide methionine sulfoxide reductase MsrB"
FT /id="PRO_0000140271"
FT DOMAIN 7..129
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT MUTAGEN 46
FT /note="C->D: Loss of activity; when associated with S-49;
FT S-95 and S-98."
FT /evidence="ECO:0000269|PubMed:16251365"
FT MUTAGEN 49
FT /note="C->S: Loss of activity; when associated with S-46;
FT S-95 and S-98."
FT /evidence="ECO:0000269|PubMed:16251365"
FT MUTAGEN 95
FT /note="C->S: Loss of activity; when associated with S-46;
FT S-49 and S-98."
FT /evidence="ECO:0000269|PubMed:16251365"
FT MUTAGEN 98
FT /note="C->S: Loss of activity; when associated with S-46;
FT S-49 and S-95."
FT /evidence="ECO:0000269|PubMed:16251365"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:6SYM"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:6SYM"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6SYM"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6SYM"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6SYM"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6SYM"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:6SYM"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:6SYM"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6SYM"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6SYM"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6SYM"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6SYM"
SQ SEQUENCE 137 AA; 15451 MW; 7B9B783DBEBE0F71 CRC64;
MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY
DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN
SASLRFTDGE NGEEING
