P23388 (PTFAX_RHOCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 92.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Multiphosphoryl transfer protein Short name=MTP Including the following 3 domains: | ||
| Gene names |
| ||
| Organism | Rhodobacter capsulatus (Rhodopseudomonas capsulata) | ||
| Taxonomic identifier | 1061 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter |
Protein attributes
| Sequence length | 827 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in fructose transport By similarity. |
| Catalytic activity | Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine. |
| Subcellular location | Cytoplasm Potential. |
| Domain | The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain. |
| Sequence similarities | Belongs to the PEP-utilizing enzyme family. Contains 1 HPr domain. Contains 1 PTS EIIA type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phosphotransferase system Sugar transport Transport |
| Cellular component | Cytoplasm |
| Molecular function | Kinase Transferase |
| Gene Ontology (GO) | |
| Biological process | phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | kinase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activityInferred from electronic annotation. Source: EC sugar:hydrogen symporter activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 827 | 827 | Multiphosphoryl transfer protein | PRO_0000186512 | |||||
Regions | |||||||||
| Domain | 2 – 142 | 141 | PTS EIIA type-2 | ||||||
| Domain | 157 – 245 | 89 | HPr | ||||||
| Region | 270 – 827 | 558 | PTS EI | ||||||
Sites | |||||||||
| Active site | 62 | 1 | Tele-phosphohistidine intermediate; for EIIA activity By similarity | ||||||
| Active site | 171 | 1 | Pros-phosphohistidine intermediate; for HPr activity By similarity | ||||||
| Active site | 457 | 1 | Tele-phosphohistidine intermediate; for PTS EI activity By similarity | ||||||
Sequences
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References
| [1] | "Structure and evolution of a multidomain multiphosphoryl transfer protein. Nucleotide sequence of the fruB(HI) gene in Rhodobacter capsulatus and comparisons with homologous genes from other organisms." Wu L.-F., Tomich J.M., Saier M.H. Jr. J. Mol. Biol. 213:687-703(1990) [PubMed: 2193161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 938 / 37b4. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X53150 Genomic DNA. Translation: CAA37301.1. |
| PIR | S10639. |
3D structure databases | |
| ProteinModelPortal | P23388. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR008279. PEP-util_enz_mobile_dom. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR006318. PEP_util_enz. IPR016152. PTrfase/Anion_transptr. IPR002178. PTS_EIIA_2. IPR001020. PTS_HPr_His_P_site. IPR005698. PTS_HPr_prot. IPR000032. PTS_HPr_prot-like. IPR002114. PTS_HPr_Ser_P_site. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view] |
| Gene3D | G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit. G3DSA:3.30.1340.10. PTS_HPr_protein. 1 hit. G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| Pfam | PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF00381. PTS-HPr. 1 hit. PF00359. PTS_EIIA_2. 1 hit. [Graphical view] |
| PRINTS | PR00107. PHOSPHOCPHPR. PR01736. PHPHTRNFRASE. |
| SUPFAM | SSF55594. HPr_protein. 1 hit. SSF47831. PEP-utilisers_N. 1 hit. SSF52009. PEP_mobile. 1 hit. SSF55804. PTrfase/Anion_transptr. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| TIGRFAMs | TIGR01003. PTS_HPr_family. 1 hit. TIGR01417. PTS_I_fam. 1 hit. |
| PROSITE | PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. PS51094. PTS_EIIA_TYPE_2. 1 hit. PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit. PS51350. PTS_HPR_DOM. 1 hit. PS00369. PTS_HPR_HIS. 1 hit. PS00589. PTS_HPR_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PTFAX_RHOCA | ||||||||
| Accession | Primary (citable) accession number: P23388 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with