P76346 · MTFA_ECOLI

Function

function

Involved in the modulation of the activity of the glucose-phosphotransferase system (glucose-PTS) (PubMed:16855233).
Interacts with the transcriptional repressor Mlc, preventing its interaction with DNA and leading to the modulation of expression of genes regulated by Mlc, including ptsG, which encodes the PTS system glucose-specific EIICB component (PubMed:16855233, PubMed:22178967).
Shows zinc-dependent metallopeptidase activity (By similarity).
In vitro, can cleave several artificial substrates (PubMed:22178967).
The greatest activity and specificity is observed for L-alanine fused to 4-nitroanilide (L-alanine-pNA) (PubMed:22178967).
Shows significantly lower activity towards L-arginine-pNA, L-proline-pNA, hippuryl-L-phenylalanine and hippuryl-L-arginine, and cannot use FTC-casein (PubMed:22178967).
Mlc does not appear to be a biologically relevant peptidase substrate (PubMed:22178967).
Biologically relevant targets may have a function in growth transition under changing environmental conditions (PubMed:22178967).

Miscellaneous

The two functions, Mlc binding and proteolysis, are clearly distinct from one another.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Activity regulation

Proteolytic activity is stimulated by interaction with Mlc (PubMed:22178967).
Addition of the chelators EDTA or phenanthroline significantly reduces the peptidase activity, whereas the addition of other protease inhibitors has much less effect (PubMed:22178967).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site111Zn2+ (UniProtKB | ChEBI)
Binding site148Zn2+ (UniProtKB | ChEBI)
Binding site152Zn2+ (UniProtKB | ChEBI)
Binding site211Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionaminopeptidase activity
Molecular Functionmetallopeptidase activity
Molecular Functionzinc ion binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Mlc titration factor A
  • Alternative names
    • Mlc-binding protein
    • Probable zinc metallopeptidase MtfA
      (EC:3.4.11.-
      ) . EC:3.4.11.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      mtfA
    • Synonyms
      yeeI
    • Ordered locus names
      b1976, JW1958

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P76346
  • Secondary accessions
    • Q2MAZ4

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Mutants exhibit increased generation times during growth on glucose, reduced transport of methyl-alpha-D-glucopyranoside, a substrate of the glucose-specific EIICB PTS system, reduced induction of a ptsG-lacZ operon fusion, and reduced catabolite repression in lactose/glucose diauxic growth experiments.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis39Does not affect protease activity with L-alanine-pNA as substrate. No change in interaction with Mlc.
Mutagenesis39Decreases interaction with Mlc.
Mutagenesis39No change in interaction with Mlc.
Mutagenesis69Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis69No change in interaction with Mlc.
Mutagenesis93Retains 45% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis141Decreases interaction with Mlc.
Mutagenesis141Retains 30% of wild-type protease activity with L-alanine-pNA as substrate. Shows reduced Mlc binding.
Mutagenesis144Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis144Decreases interaction with Mlc.
Mutagenesis148Retains 70% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis148Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis149Retains 59% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis149Retains 19% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis152Retains 69% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis152Retains 82% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis155Decreases interaction with Mlc.
Mutagenesis155Retains 67% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis204Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis206Retains 23% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis206Decreases interaction with Mlc.
Mutagenesis211Does not affect protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis211Retains 62% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis213Retains 86% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis215Retains 75% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis215Retains 91% of wild-type protease activity with L-alanine-pNA as substrate. No change in interaction with Mlc.
Mutagenesis217Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis218Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis221Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.
Mutagenesis224Retains 70% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding.
Mutagenesis242Retains 29% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001691081-265Mlc titration factor A

Proteomic databases

Interaction

Subunit

Interacts with Mlc with high affinity.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P76346mlc P504562EBI-1126682, EBI-1116104

Protein-protein interaction databases

Structure

Family & Domains

Domain

The C-terminal part of MtfA is sufficient for Mlc binding.

Sequence similarities

Belongs to the MtfA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    265
  • Mass (Da)
    30,279
  • Last updated
    1998-12-15 v2
  • Checksum
    198E366587CCF8A5
MIKWPWKVQESAHQTALPWQEALSIPLLTCLTEQEQSKLVTLAERFLQQKRLVPLQGFELDSLRSCRIALLFCLPVLELGLEWLDGFHEVLIYPAPFVVDDEWEDDIGLVHNQRIVQSGQSWQQGPIVLNWLDIQDSFDASGFNLIIHEVAHKLDTRNGDRASGVPFIPLREVAGWEHDLHAAMNNIQEEIELVGENAASIDAYAASDPAECFAVLSEYFFSAPELFAPRFPSLWQRFCQFYQQDPLQRLHHANDTDSFSATNVH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U00096
EMBL· GenBank· DDBJ
AAC75041.2
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE76562.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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