2IBM
A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006605 | biological_process | protein targeting |
| A | 0006886 | biological_process | intracellular protein transport |
| A | 0008564 | molecular_function | protein-exporting ATPase activity |
| A | 0015031 | biological_process | protein transport |
| A | 0016020 | cellular_component | membrane |
| A | 0017038 | biological_process | protein import |
| A | 0031522 | cellular_component | cell envelope Sec protein transport complex |
| A | 0043952 | biological_process | protein transport by the Sec complex |
| A | 0045121 | cellular_component | membrane raft |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0065002 | biological_process | intracellular protein transmembrane transport |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006605 | biological_process | protein targeting |
| B | 0006886 | biological_process | intracellular protein transport |
| B | 0008564 | molecular_function | protein-exporting ATPase activity |
| B | 0015031 | biological_process | protein transport |
| B | 0016020 | cellular_component | membrane |
| B | 0017038 | biological_process | protein import |
| B | 0031522 | cellular_component | cell envelope Sec protein transport complex |
| B | 0043952 | biological_process | protein transport by the Sec complex |
| B | 0045121 | cellular_component | membrane raft |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0065002 | biological_process | intracellular protein transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP A 781 |
| Chain | Residue |
| A | MET79 |
| A | ASP492 |
| A | PHE82 |
| A | GLN85 |
| A | LYS101 |
| A | GLY103 |
| A | GLU104 |
| A | GLY105 |
| A | LYS106 |
| A | THR107 |
Functional Information from PROSITE/UniProt
| site_id | PS01312 |
| Number of Residues | 16 |
| Details | SECA SecA family signature. VtIATNMAGRGtDIkL |
| Chain | Residue | Details |
| A | VAL480-LEU495 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:19850053, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:3JV2 |
| Chain | Residue | Details |
| A | MET79 | |
| B | MET79 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:16989859, ECO:0000269|PubMed:19850053, ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM, ECO:0007744|PDB:3JV2 |
| Chain | Residue | Details |
| B | GLN85 | |
| B | GLY103 | |
| A | GLN85 | |
| A | GLY103 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:16989859, ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM |
| Chain | Residue | Details |
| A | ASP492 | |
| B | ASP492 |
