P96123 (CHEA_TREPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 91.
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: Chemotaxis protein CheA EC=2.7.13.3 | ||||
| Gene names |
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| Organism | Treponema pallidum (strain Nichols) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243276 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Treponema |
Protein attributes
| Sequence length | 812 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY By similarity. |
| Catalytic activity | ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | Contains 1 cheW-like domain. Contains 1 histidine kinase domain. Contains 1 HPt domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Chemotaxis Two-component regulatory system |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular component movement Inferred from electronic annotation. Source: InterPro chemotaxisInferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component sensor 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 – 812 | 812 | Chemotaxis protein CheA | PRO_0000074719 | |||||
Regions | |||||||||
| Domain | 1 – 111 | 111 | HPt | ||||||
| Domain | 418 – 661 | 244 | Histidine kinase | ||||||
| Domain | 663 – 798 | 136 | CheW-like | ||||||
Amino acid modifications | |||||||||
| Modified residue | 54 | 1 | Phosphohistidine; by autocatalysis By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 428 | 1 | G → E in AAC45555. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification, sequences, and expression of Treponema pallidum chemotaxis genes." Greene S.R., Stamm L.V., Hardham J.M., Young N.R., Frye J.G. DNA Seq. 7:267-284(1997) [PubMed: 9255518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Nichols. |
| [2] | "Complete genome sequence of Treponema pallidum, the syphilis spirochete." Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., Khalak H.G., Richardson D.L., Howell J.K. Venter J.C.Science 281:375-388(1998) [PubMed: 9665876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nichols. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U61851 Genomic DNA. Translation: AAC45555.1. AE000520 Genomic DNA. Translation: AAC65348.1. |
| PIR | A71335. |
| RefSeq | NP_218803.1. NC_000919.1. |
3D structure databases | |
| ProteinModelPortal | P96123. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2611783. |
| GenomeReviews | Gene locus TP_0363 in contig AE000520_GR. |
| KEGG | tpa:TP0363. |
| NMPDR | fig|243276.1.peg.362. |
| PATRIC | 20530727. VBITrePal57110_0384. |
| TIGR | TP_0363. |
Phylogenomic databases | |
| HOGENOM | HBG705053. |
| OMA | TELNETI. |
| ProtClustDB | CLSK375147. |
Enzyme and pathway databases | |
| BioCyc | TPAL243276:TP_0363-MONOMER. |
| BRENDA | 2.7.13.3. 6429. |
Family and domain databases | |
| InterPro | IPR003594. ATPase-like_ATP-bd. IPR002545. CheW. IPR004358. Sig_transdc_His_kin-like_C. IPR008207. Sig_transdc_His_kin_Hpt_dom. IPR004105. Sig_transdc_His_kin_subgr_dim. IPR005467. Sig_transdc_His_kinase_core. IPR009082. Sig_transdc_His_kinase_dimeric. IPR010808. Sig_transdc_His_kinase_P2-bd. [Graphical view] |
| Gene3D | G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. G3DSA:3.30.70.1110. G3DSA:3.30.70.1110. 1 hit. G3DSA:1.20.120.160. Sig_transdc_His_kin_Hpt_dom. 1 hit. G3DSA:1.10.287.560. Sig_transdc_His_kin_subgr_dim. 1 hit. |
| KO | K03407. |
| Pfam | PF01584. CheW. 1 hit. PF02895. H-kinase_dim. 1 hit. PF02518. HATPase_c. 1 hit. PF01627. Hpt. 1 hit. PF07194. P2. 1 hit. [Graphical view] |
| PRINTS | PR00344. BCTRLSENSOR. |
| SMART | SM00260. CheW. 1 hit. SM00387. HATPase_c. 1 hit. SM00073. HPT. 1 hit. [Graphical view] |
| SUPFAM | SSF55874. ATP_bd_ATPase. 1 hit. SSF50341. CheW. 1 hit. SSF47384. His_kin_homodim. 1 hit. SSF47226. Hpt. 1 hit. |
| PROSITE | PS50851. CHEW. 1 hit. PS50109. HIS_KIN. 1 hit. PS50894. HPT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHEA_TREPA | ||||||||
| Accession | Primary (citable) accession number: P96123 Secondary accession number(s): O83381 | ||||||||
| 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 |

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