ID   METJ_ECOLI              Reviewed;         105 AA.
AC   P0A8U6; P08338; Q2M8N4;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Met repressor;
DE   AltName: Full=Met regulon regulatory protein MetJ;
GN   Name=metJ; OrderedLocusNames=b3938, JW3909;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6.
RX   PubMed=6094549; DOI=10.1016/s0021-9258(18)89890-8;
RA   Saint-Girons I., Duchange N., Cohen G.C., Zakin M.M.;
RT   "Structure and autoregulation of the metJ regulatory gene in Escherichia
RT   coli.";
RL   J. Biol. Chem. 259:14282-14285(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [3]
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   [4]
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   [5]
RP   VARIANT METJ193.
RX   PubMed=2141834; DOI=10.1128/jb.172.7.3918-3924.1990;
RA   Collier C.D., Johnson J.R.;
RT   "The Escherichia coli K-12 metJ193 allele contains a point mutation which
RT   alters the hydrophobic pocket responsible for in vitro binding of S-
RT   adenosylmethionine: effects on cell growth and induction of met regulon
RT   expression.";
RL   J. Bacteriol. 172:3918-3924(1990).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=2677753; DOI=10.1038/341705a0;
RA   Rafferty J.B., Somers W.S., Saint-Girons I., Phillips S.E.V.;
RT   "Three-dimensional crystal structures of Escherichia coli met repressor
RT   with and without corepressor.";
RL   Nature 341:705-710(1989).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=1406951; DOI=10.1038/359387a0;
RA   Somers W.S., Phillips S.E.V.;
RT   "Crystal structure of the met repressor-operator complex at 2.8-A
RT   resolution reveals DNA recognition by beta-strands.";
RL   Nature 359:387-393(1992).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RA   Garvie C.W., Phillips S.E.V.;
RL   Submitted (JAN-1998) to the PDB data bank.
CC   -!- FUNCTION: This regulatory protein, when combined with SAM (S-
CC       adenosylmethionine) represses the expression of the methionine regulon
CC       and of enzymes involved in SAM synthesis. It is also autoregulated.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P0A8U6; P0AFF6: nusA; NbExp=3; IntAct=EBI-555272, EBI-551571;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Does not bind DNA by a helix-turn-helix motif.
CC   -!- SIMILARITY: Belongs to the MetJ 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; M12869; AAA24163.1; -; Genomic_DNA.
DR   EMBL; L19201; AAB03070.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76920.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77372.1; -; Genomic_DNA.
DR   EMBL; M38202; AAA24162.1; -; Genomic_DNA.
DR   PIR; A22660; RGECMJ.
DR   RefSeq; NP_418373.1; NC_000913.3.
DR   RefSeq; WP_000852812.1; NZ_STEB01000037.1.
DR   PDB; 1CMA; X-ray; 2.80 A; A/B=2-105.
DR   PDB; 1CMB; X-ray; 1.80 A; A/B=2-105.
DR   PDB; 1CMC; X-ray; 1.80 A; A/B=2-105.
DR   PDB; 1MJ2; X-ray; 2.40 A; A/B/C/D=2-105.
DR   PDB; 1MJK; X-ray; 2.15 A; A/B=2-105.
DR   PDB; 1MJL; X-ray; 2.10 A; A/B=2-105.
DR   PDB; 1MJM; X-ray; 2.20 A; A/B=2-105.
DR   PDB; 1MJO; X-ray; 2.10 A; A/B/C/D=2-105.
DR   PDB; 1MJP; X-ray; 3.40 A; A/B=2-105.
DR   PDB; 1MJQ; X-ray; 2.40 A; A/B/C/D/G/H/I/J=2-105.
DR   PDBsum; 1CMA; -.
DR   PDBsum; 1CMB; -.
DR   PDBsum; 1CMC; -.
DR   PDBsum; 1MJ2; -.
DR   PDBsum; 1MJK; -.
DR   PDBsum; 1MJL; -.
DR   PDBsum; 1MJM; -.
DR   PDBsum; 1MJO; -.
DR   PDBsum; 1MJP; -.
DR   PDBsum; 1MJQ; -.
DR   AlphaFoldDB; P0A8U6; -.
DR   SMR; P0A8U6; -.
DR   BioGRID; 4263206; 7.
DR   DIP; DIP-47929N; -.
DR   IntAct; P0A8U6; 1.
DR   STRING; 511145.b3938; -.
DR   jPOST; P0A8U6; -.
DR   PaxDb; P0A8U6; -.
DR   PRIDE; P0A8U6; -.
DR   EnsemblBacteria; AAC76920; AAC76920; b3938.
DR   EnsemblBacteria; BAE77372; BAE77372; BAE77372.
DR   GeneID; 67417544; -.
DR   GeneID; 948435; -.
DR   KEGG; ecj:JW3909; -.
DR   KEGG; eco:b3938; -.
DR   PATRIC; fig|1411691.4.peg.2767; -.
DR   EchoBASE; EB0583; -.
DR   eggNOG; COG3060; Bacteria.
DR   HOGENOM; CLU_142318_0_0_6; -.
DR   OMA; KWNGEYI; -.
DR   PhylomeDB; P0A8U6; -.
DR   BioCyc; EcoCyc:PD04032; -.
DR   EvolutionaryTrace; P0A8U6; -.
DR   PRO; PR:P0A8U6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00490; Met_repressor_MetJ; 1.
DR   Gene3D; 1.10.140.10; -; 1.
DR   HAMAP; MF_00744; MetJ; 1.
DR   InterPro; IPR002084; Met_repressor_MetJ.
DR   InterPro; IPR023453; Met_repressor_MetJ_dom_sf.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   Pfam; PF01340; MetJ; 1.
DR   SUPFAM; SSF47598; SSF47598; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Methionine biosynthesis;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6094549"
FT   CHAIN           2..105
FT                   /note="Met repressor"
FT                   /id="PRO_0000198397"
FT   VARIANT         57
FT                   /note="L -> Q (in metJ193)"
FT   VARIANT         61
FT                   /note="A -> T (hinders dimerization)"
FT   STRAND          11..15
FT                   /evidence="ECO:0007829|PDB:1CMB"
FT   HELIX           18..21
FT                   /evidence="ECO:0007829|PDB:1MJO"
FT   STRAND          22..30
FT                   /evidence="ECO:0007829|PDB:1CMB"
FT   HELIX           31..47
FT                   /evidence="ECO:0007829|PDB:1CMB"
FT   HELIX           54..67
FT                   /evidence="ECO:0007829|PDB:1CMB"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:1CMB"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:1MJL"
FT   HELIX           87..95
FT                   /evidence="ECO:0007829|PDB:1CMB"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:1CMC"
SQ   SEQUENCE   105 AA;  12141 MW;  05B0F54918C697EF CRC64;
     MAEWSGEYIS PYAEHGKKSE QVKKITVSIP LKVLKILTDE RTRRQVNNLR HATNSELLCE
     AFLHAFTGQP LPDDADLRKE RSDEIPEAAK EIMREMGINP ETWEY