8RTB
Extended inner membrane complex (IMC) protomer structure (TrwM/VirB3-TrwK/VirB4-TrwI/VirB6-TrwG/VirB8-TrwE/VirB10) from the fully-assembled R388 type IV secretion system determined by cryo-EM.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0016020 | cellular_component | membrane |
| E | 0005515 | molecular_function | protein binding |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0016020 | cellular_component | membrane |
| F | 0005515 | molecular_function | protein binding |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0016020 | cellular_component | membrane |
| G | 0005515 | molecular_function | protein binding |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0016020 | cellular_component | membrane |
| H | 0005515 | molecular_function | protein binding |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0009279 | cellular_component | cell outer membrane |
| J | 0005515 | molecular_function | protein binding |
| J | 0005886 | cellular_component | plasma membrane |
| J | 0030255 | biological_process | protein secretion by the type IV secretion system |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 74 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"35732732","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35732732","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OIU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"35732732","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 44 |
| Details | Transmembrane: {"evidences":[{"source":"PubMed","id":"35732732","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OIU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 92 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35732732","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"38886579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35732732","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38886579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
