P77439 · PTFX1_ECOLI
- ProteinMultiphosphoryl transfer protein 1
- GenefryA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids831 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Multifunctional protein that includes general (non sugar-specific) and sugar-specific components of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FryABC PTS system is involved in fructose transport.
Catalytic activity
- L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 15 | Pros-phosphohistidine intermediate; for HPr activity | ||||
Sequence: H | ||||||
Active site | 298 | Tele-phosphohistidine intermediate; for PTS EI activity | ||||
Sequence: H | ||||||
Binding site | 405 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 441 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 540 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 563-564 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: ND | ||||||
Binding site | 564 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 574 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 611 | Proton donor; for EI activity | ||||
Sequence: C | ||||||
Active site | 747 | Tele-phosphohistidine intermediate; for PTS EIIA activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoenolpyruvate-protein phosphotransferase activity | |
Molecular Function | protein-N(PI)-phosphohistidine-sugar phosphotransferase activity | |
Biological Process | phosphoenolpyruvate-dependent sugar phosphotransferase system |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMultiphosphoryl transfer protein 1
- Short namesMTP 1
- Alternative names
Including 3 domains:
- Recommended namePhosphoenolpyruvate-protein phosphotransferase
- EC number
- Alternative names
- Recommended namePhosphocarrier protein HPr
- Short namesProtein H
- Recommended namePTS system fructose-like EIIA component
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP77439
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147097 | 1-831 | Multiphosphoryl transfer protein 1 | |||
Sequence: MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINHRQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYIQVRFIDSDSVQPTQAELTAHPLPRSLSRLNPDLLYGNVLASGVGVGTLTLLQSDSLDSYRAIPASAQDSTRLEHSLATLAEQLNQQLRERDGESKTILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPELKPRNKLVLEKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYYQVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQEIEALLTAFTPEEDVRPLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGWQSEMGEVELVIMLTLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETELTF | ||||||
Modified residue | 15 | Phosphohistidine; by EI | ||||
Sequence: H | ||||||
Modified residue | 298 | Phosphohistidine; by autocatalysis | ||||
Sequence: H | ||||||
Modified residue | 747 | Phosphohistidine; by HPr | ||||
Sequence: H |
Keywords
- PTM
Proteomic databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P77439 | aceE P0AFG8 | 2 | EBI-545399, EBI-542683 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-90 | HPr | ||||
Sequence: MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINHRQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYIQVRFIDS | ||||||
Region | 119-650 | PTS EI | ||||
Sequence: GNVLASGVGVGTLTLLQSDSLDSYRAIPASAQDSTRLEHSLATLAEQLNQQLRERDGESKTILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPELKPRNKLVLEKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYYQVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLD | ||||||
Domain | 685-828 | PTS EIIA type-2 | ||||
Sequence: PLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGWQSEMGEVELVIMLTLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE |
Domain
The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
In contrast to classical PTS systems, the fructose-like PTS has no requirement for HPr and Enzyme I; FryA combines a IIA domain with an Enzyme I and a HPr domains.
Sequence similarities
Belongs to the PEP-utilizing enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length831
- Mass (Da)92,130
- Last updated1997-02-01 v1
- ChecksumB9F3E3B6D4EAB597
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00096 EMBL· GenBank· DDBJ | AAC75442.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA16253.1 EMBL· GenBank· DDBJ | Genomic DNA |