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Protein

Met repressor

Gene

metJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD04032.
ECOL316407:JW3909-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Met repressor
Alternative name(s):
Met regulon regulatory protein MetJ
Gene namesi
Name:metJ
Ordered Locus Names:b3938, JW3909
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10588. metJ.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 105104Met repressorPRO_0000198397Add
BLAST

Proteomic databases

PaxDbiP0A8U6.
PRIDEiP0A8U6.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4263206. 4 interactions.
DIPiDIP-47929N.
IntActiP0A8U6. 1 interaction.
MINTiMINT-1265451.
STRINGi511145.b3938.

Chemistry

BindingDBiP0A8U6.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 155Combined sources
Helixi18 – 214Combined sources
Beta strandi22 – 309Combined sources
Helixi31 – 4717Combined sources
Helixi54 – 6714Combined sources
Helixi74 – 774Combined sources
Beta strandi79 – 813Combined sources
Helixi87 – 959Combined sources
Turni100 – 1023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMAX-ray2.80A/B2-105[»]
1CMBX-ray1.80A/B2-105[»]
1CMCX-ray1.80A/B2-105[»]
1MJ2X-ray2.40A/B/C/D2-105[»]
1MJKX-ray2.15A/B2-105[»]
1MJLX-ray2.10A/B2-105[»]
1MJMX-ray2.20A/B2-105[»]
1MJOX-ray2.10A/B/C/D2-105[»]
1MJPX-ray3.40A/B2-105[»]
1MJQX-ray2.40A/B/C/D/G/H/I/J2-105[»]
ProteinModelPortaliP0A8U6.
SMRiP0A8U6. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8U6.

Family & Domainsi

Domaini

Does not bind DNA by a helix-turn-helix motif.

Sequence similaritiesi

Belongs to the MetJ family.Curated

Phylogenomic databases

eggNOGiCOG3060. LUCA.
HOGENOMiHOG000271582.
KOiK03764.
OMAiLRKERHD.
OrthoDBiEOG6V1M74.

Family and domain databases

Gene3Di1.10.140.10. 1 hit.
HAMAPiMF_00744. MetJ.
InterProiIPR002084. Met_repressor_MetJ.
IPR023453. Met_repressor_MetJ_dom.
IPR010985. Ribbon_hlx_hlx.
[Graphical view]
PfamiPF01340. MetJ. 1 hit.
[Graphical view]
ProDomiPD020365. Met_repressor_MetJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47598. SSF47598. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A8U6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEWSGEYIS PYAEHGKKSE QVKKITVSIP LKVLKILTDE RTRRQVNNLR
60 70 80 90 100
HATNSELLCE AFLHAFTGQP LPDDADLRKE RSDEIPEAAK EIMREMGINP

ETWEY
Length:105
Mass (Da):12,141
Last modified:January 23, 2007 - v2
Checksum:i05B0F54918C697EF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571L → Q in metJ193.
Natural varianti61 – 611A → T Hinders dimerization.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12869 Genomic DNA. Translation: AAA24163.1.
L19201 Genomic DNA. Translation: AAB03070.1.
U00096 Genomic DNA. Translation: AAC76920.1.
AP009048 Genomic DNA. Translation: BAE77372.1.
M38202 Genomic DNA. Translation: AAA24162.1.
PIRiA22660. RGECMJ.
RefSeqiNP_418373.1. NC_000913.3.
WP_000852812.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76920; AAC76920; b3938.
BAE77372; BAE77372; BAE77372.
GeneIDi948435.
KEGGiecj:JW3909.
eco:b3938.
PATRICi32123395. VBIEscCol129921_4058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12869 Genomic DNA. Translation: AAA24163.1.
L19201 Genomic DNA. Translation: AAB03070.1.
U00096 Genomic DNA. Translation: AAC76920.1.
AP009048 Genomic DNA. Translation: BAE77372.1.
M38202 Genomic DNA. Translation: AAA24162.1.
PIRiA22660. RGECMJ.
RefSeqiNP_418373.1. NC_000913.3.
WP_000852812.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMAX-ray2.80A/B2-105[»]
1CMBX-ray1.80A/B2-105[»]
1CMCX-ray1.80A/B2-105[»]
1MJ2X-ray2.40A/B/C/D2-105[»]
1MJKX-ray2.15A/B2-105[»]
1MJLX-ray2.10A/B2-105[»]
1MJMX-ray2.20A/B2-105[»]
1MJOX-ray2.10A/B/C/D2-105[»]
1MJPX-ray3.40A/B2-105[»]
1MJQX-ray2.40A/B/C/D/G/H/I/J2-105[»]
ProteinModelPortaliP0A8U6.
SMRiP0A8U6. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263206. 4 interactions.
DIPiDIP-47929N.
IntActiP0A8U6. 1 interaction.
MINTiMINT-1265451.
STRINGi511145.b3938.

Chemistry

BindingDBiP0A8U6.

Proteomic databases

PaxDbiP0A8U6.
PRIDEiP0A8U6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76920; AAC76920; b3938.
BAE77372; BAE77372; BAE77372.
GeneIDi948435.
KEGGiecj:JW3909.
eco:b3938.
PATRICi32123395. VBIEscCol129921_4058.

Organism-specific databases

EchoBASEiEB0583.
EcoGeneiEG10588. metJ.

Phylogenomic databases

eggNOGiCOG3060. LUCA.
HOGENOMiHOG000271582.
KOiK03764.
OMAiLRKERHD.
OrthoDBiEOG6V1M74.

Enzyme and pathway databases

BioCyciEcoCyc:PD04032.
ECOL316407:JW3909-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A8U6.
PROiP0A8U6.

Family and domain databases

Gene3Di1.10.140.10. 1 hit.
HAMAPiMF_00744. MetJ.
InterProiIPR002084. Met_repressor_MetJ.
IPR023453. Met_repressor_MetJ_dom.
IPR010985. Ribbon_hlx_hlx.
[Graphical view]
PfamiPF01340. MetJ. 1 hit.
[Graphical view]
ProDomiPD020365. Met_repressor_MetJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47598. SSF47598. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and autoregulation of the metJ regulatory gene in Escherichia coli."
    Saint-Girons I., Duchange N., Cohen G.C., Zakin M.M.
    J. Biol. Chem. 259:14282-14285(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6.
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The Escherichia coli K-12 metJ193 allele contains a point mutation which alters the hydrophobic pocket responsible for in vitro binding of S-adenosylmethionine: effects on cell growth and induction of met regulon expression."
    Collier C.D., Johnson J.R.
    J. Bacteriol. 172:3918-3924(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT METJ193.
  6. "Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor."
    Rafferty J.B., Somers W.S., Saint-Girons I., Phillips S.E.V.
    Nature 341:705-710(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  7. "Crystal structure of the met repressor-operator complex at 2.8-A resolution reveals DNA recognition by beta-strands."
    Somers W.S., Phillips S.E.V.
    Nature 359:387-393(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  8. Garvie C.W., Phillips S.E.V.
    Submitted (JAN-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

Entry informationi

Entry nameiMETJ_ECOLI
AccessioniPrimary (citable) accession number: P0A8U6
Secondary accession number(s): P08338, Q2M8N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.