Reviewed,
UniProtKB/Swiss-Prot O84340 (PT1_CHLTR)
Last modified
November 3, 2009.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phosphoenolpyruvate-protein phosphotransferase EC=2.7.3.9 Alternative name(s): Phosphotransferase system, enzyme I | ||||
| Gene names |
| ||||
| Organism | Chlamydia trachomatis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 813 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 571 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | General (non sugar-specific) component 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. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) By similarity. |
| Catalytic activity | Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. |
| Cofactor | Magnesium By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity. |
| Miscellaneous | The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity. |
| Sequence similarities | Belongs to the PEP-utilizing enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phosphotransferase system Sugar transport Transport |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW phosphorylationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred 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 – 571 | 571 | Phosphoenolpyruvate-protein phosphotransferase | PRO_0000147066 | |||||
Sites | |||||||||
| Active site | 207 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 506 | 1 | Proton donor By similarity | ||||||
| Metal binding | 435 | 1 | Magnesium By similarity | ||||||
| Metal binding | 459 | 1 | Magnesium By similarity | ||||||
| Binding site | 312 | 1 | Substrate By similarity | ||||||
| Binding site | 348 | 1 | Substrate By similarity | ||||||
| Binding site | 435 | 1 | Substrate By similarity | ||||||
| Binding site | 456 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 457 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 458 | 1 | Substrate By similarity | ||||||
| Binding site | 459 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx. |
Cross-references
Sequence databases | |
|---|---|
| AE001273 Genomic DNA. Translation: AAC67931.1. | |
| PIR | C71528. |
| RefSeq | NP_219843.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 884783. |
| GenomeReviews | Gene locus CT_336 in contig AE001273_GR. |
| KEGG | ctr:CT336. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O84340. |
| OMA | IFRASHY. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:CT336-MON. |
| BRENDA | 2.7.3.9. 108. |
Family and domain databases | |
| InterPro | IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. IPR000121. PEP_utilizers. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view] |
| Gene3D | G3DSA:3.50.30.10. PEP_mobile. 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. [Graphical view] |
| PRINTS | PR01736. PHPHTRNFRASE. |
| ProDom | PD000940. PEP_utilizers. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01417. PTS_I_fam. 1 hit. |
| PROSITE | PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PT1_CHLTR | ||||||||
| Accession | Primary (citable) accession number: O84340 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


