P76346 · MTFA_ECOLI
- ProteinMlc titration factor A
- GenemtfA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids265 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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
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).
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aminopeptidase activity | |
Molecular Function | metallopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMlc titration factor A
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP76346
- Secondary accessions
Proteomes
Subcellular Location
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 39 | Does not affect protease activity with L-alanine-pNA as substrate. No change in interaction with Mlc. | ||||
Sequence: L → A | ||||||
Mutagenesis | 39 | Decreases interaction with Mlc. | ||||
Sequence: L → E | ||||||
Mutagenesis | 39 | No change in interaction with Mlc. | ||||
Sequence: L → T | ||||||
Mutagenesis | 69 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: A → D | ||||||
Mutagenesis | 69 | No change in interaction with Mlc. | ||||
Sequence: A → S | ||||||
Mutagenesis | 93 | Retains 45% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: Y → S | ||||||
Mutagenesis | 141 | Decreases interaction with Mlc. | ||||
Sequence: S → A | ||||||
Mutagenesis | 141 | Retains 30% of wild-type protease activity with L-alanine-pNA as substrate. Shows reduced Mlc binding. | ||||
Sequence: S → F | ||||||
Mutagenesis | 144 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: N → D | ||||||
Mutagenesis | 144 | Decreases interaction with Mlc. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 148 | Retains 70% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: H → K | ||||||
Mutagenesis | 148 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 149 | Retains 59% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: E → D | ||||||
Mutagenesis | 149 | Retains 19% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 152 | Retains 69% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: H → K | ||||||
Mutagenesis | 152 | Retains 82% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 155 | Decreases interaction with Mlc. | ||||
Sequence: D → E | ||||||
Mutagenesis | 155 | Retains 67% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: D → N | ||||||
Mutagenesis | 204 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: Y → S | ||||||
Mutagenesis | 206 | Retains 23% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: A → D | ||||||
Mutagenesis | 206 | Decreases interaction with Mlc. | ||||
Sequence: A → S | ||||||
Mutagenesis | 211 | Does not affect protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: E → D | ||||||
Mutagenesis | 211 | Retains 62% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 213 | Retains 86% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: F → M | ||||||
Mutagenesis | 215 | Retains 75% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: V → D | ||||||
Mutagenesis | 215 | Retains 91% of wild-type protease activity with L-alanine-pNA as substrate. No change in interaction with Mlc. | ||||
Sequence: V → L | ||||||
Mutagenesis | 217 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: S → A | ||||||
Mutagenesis | 218 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: E → D or Q | ||||||
Mutagenesis | 221 | Does not affect protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: F → M | ||||||
Mutagenesis | 224 | Retains 70% of wild-type protease activity with L-alanine-pNA as substrate. Does not affect Mlc binding. | ||||
Sequence: P → S | ||||||
Mutagenesis | 242 | Retains 29% of wild-type protease activity with L-alanine-pNA as substrate. Decreases interaction with Mlc. | ||||
Sequence: Y → S |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000169108 | 1-265 | Mlc titration factor A | |||
Sequence: MIKWPWKVQESAHQTALPWQEALSIPLLTCLTEQEQSKLVTLAERFLQQKRLVPLQGFELDSLRSCRIALLFCLPVLELGLEWLDGFHEVLIYPAPFVVDDEWEDDIGLVHNQRIVQSGQSWQQGPIVLNWLDIQDSFDASGFNLIIHEVAHKLDTRNGDRASGVPFIPLREVAGWEHDLHAAMNNIQEEIELVGENAASIDAYAASDPAECFAVLSEYFFSAPELFAPRFPSLWQRFCQFYQQDPLQRLHHANDTDSFSATNVH |
Proteomic databases
Interaction
Subunit
Interacts with Mlc with high affinity.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P76346 | mlc P50456 | 2 | EBI-1126682, EBI-1116104 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length265
- Mass (Da)30,279
- Last updated1998-12-15 v2
- Checksum198E366587CCF8A5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00096 EMBL· GenBank· DDBJ | AAC75041.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76562.1 EMBL· GenBank· DDBJ | Genomic DNA |