MSRC_ECOLI
ID MSRC_ECOLI Reviewed; 165 AA.
AC P76270; O07976; O07978;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Free methionine-R-sulfoxide reductase;
DE Short=fRMsr;
DE EC=1.8.4.14;
GN Name=msrC; Synonyms=yebR; OrderedLocusNames=b1832, JW1821;
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=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=17535911; DOI=10.1073/pnas.0703774104;
RA Lin Z., Johnson L.C., Weissbach H., Brot N., Lively M.O., Lowther W.T.;
RT "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a
RT new GAF domain function.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9597-9602(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Catalyzes the reversible oxidation-reduction of the R-
CC enantiomer of free methionine sulfoxide to methionine. Specific for
CC free L-methionine-(R)-S-oxide. {ECO:0000269|PubMed:17535911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, 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:58773; EC=1.8.4.14;
CC Evidence={ECO:0000269|PubMed:17535911};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 mM for L-methionine-(R)-S-oxide {ECO:0000269|PubMed:17535911};
CC KM=9.8 uM for thioredoxin {ECO:0000269|PubMed:17535911};
CC -!- SIMILARITY: Belongs to the free Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA15640.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74902.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15640.1; ALT_INIT; Genomic_DNA.
DR PIR; H64944; H64944.
DR RefSeq; NP_416346.4; NC_000913.3.
DR RefSeq; WP_001043877.1; NZ_LN832404.1.
DR PDB; 1VHM; X-ray; 2.10 A; A/B=1-165.
DR PDBsum; 1VHM; -.
DR AlphaFoldDB; P76270; -.
DR SMR; P76270; -.
DR BioGRID; 4259156; 23.
DR DIP; DIP-11813N; -.
DR IntAct; P76270; 8.
DR STRING; 511145.b1832; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR SWISS-2DPAGE; P76270; -.
DR jPOST; P76270; -.
DR PaxDb; P76270; -.
DR PRIDE; P76270; -.
DR EnsemblBacteria; AAC74902; AAC74902; b1832.
DR EnsemblBacteria; BAA15640; BAA15640; BAA15640.
DR GeneID; 946086; -.
DR KEGG; ecj:JW1821; -.
DR KEGG; eco:b1832; -.
DR PATRIC; fig|511145.12.peg.1910; -.
DR EchoBASE; EB3774; -.
DR eggNOG; COG1956; Bacteria.
DR HOGENOM; CLU_077738_2_0_6; -.
DR InParanoid; P76270; -.
DR PhylomeDB; P76270; -.
DR BioCyc; EcoCyc:G7005-MON; -.
DR BioCyc; MetaCyc:G7005-MON; -.
DR BRENDA; 1.8.4.14; 2026.
DR SABIO-RK; P76270; -.
DR EvolutionaryTrace; P76270; -.
DR PRO; PR:P76270; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IDA:EcoCyc.
DR GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IBA:GO_Central.
DR Gene3D; 3.30.450.40; -; 1.
DR InterPro; IPR000614; FRMsr_CS.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR Pfam; PF13185; GAF_2; 1.
DR SMART; SM00065; GAF; 1.
DR PROSITE; PS01320; UPF0067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..165
FT /note="Free methionine-R-sulfoxide reductase"
FT /id="PRO_0000171553"
FT DOMAIN 49..149
FT /note="GAF"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1VHM"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1VHM"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1VHM"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:1VHM"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:1VHM"
FT HELIX 134..152
FT /evidence="ECO:0007829|PDB:1VHM"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1VHM"
SQ SEQUENCE 165 AA; 18122 MW; B49F1D1740DD5D43 CRC64;
MNKTEFYADL NRDFNALMAG ETSFLATLAN TSALLYERLT DINWAGFYLL EDDTLVLGPF
QGKIACVRIP VGRGVCGTAV ARNQVQRIED VHVFDGHIAC DAASNSEIVL PLVVKNQIIG
VLDIDSTVFG RFTDEDEQGL RQLVAQLEKV LATTDYKKFF ASVAG
