2LP4
Solution structure of P1-CheY/P2 complex in bacterial chemotaxis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| Y | 0000156 | molecular_function | phosphorelay response regulator activity |
| Y | 0000160 | biological_process | phosphorelay signal transduction system |
| Y | 0000287 | molecular_function | magnesium ion binding |
| Y | 0005515 | molecular_function | protein binding |
| Y | 0005737 | cellular_component | cytoplasm |
| Y | 0005829 | cellular_component | cytosol |
| Y | 0006935 | biological_process | chemotaxis |
| Y | 0007165 | biological_process | signal transduction |
| Y | 0009288 | cellular_component | bacterial-type flagellum |
| Y | 0009433 | cellular_component | bacterial-type flagellum basal body, C ring |
| Y | 0009454 | biological_process | aerotaxis |
| Y | 0016407 | molecular_function | acetyltransferase activity |
| Y | 0018393 | biological_process | internal peptidyl-lysine acetylation |
| Y | 0043052 | biological_process | thermotaxis |
| Y | 0046872 | molecular_function | metal ion binding |
| Y | 0050920 | biological_process | regulation of chemotaxis |
| Y | 0071977 | biological_process | bacterial-type flagellum-dependent swimming motility |
| Y | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
| Y | 0120107 | cellular_component | bacterial-type flagellum rotor complex |
| Y | 1902021 | biological_process | regulation of bacterial-type flagellum-dependent cell motility |
Functional Information from PROSITE/UniProt
| site_id | PS00039 |
| Number of Residues | 9 |
| Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. FFDEADElL |
| Chain | Residue | Details |
| A | PHE12-LEU20 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 104 |
| Details | Domain: {"description":"HPt","evidences":[{"source":"PROSITE-ProRule","id":"PRU00110","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphohistidine; by autocatalysis","evidences":[{"source":"PROSITE-ProRule","id":"PRU00107","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2832069","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 117 |
| Details | Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8176739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CHN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1869568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2689446","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11359578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
