Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue ATP A 401 |
| Chain | Residue |
| A | LEU110 |
| A | ARG278 |
| A | PRO132 |
| A | THR133 |
| A | GLY134 |
| A | SER135 |
| A | GLY136 |
| A | LYS137 |
| A | SER138 |
| A | THR139 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue ATP B 401 |
| Chain | Residue |
| B | LEU110 |
| B | PRO132 |
| B | THR133 |
| B | GLY134 |
| B | SER135 |
| B | GLY136 |
| B | LYS137 |
| B | SER138 |
| B | THR139 |
| B | ARG278 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue ATP C 401 |
| Chain | Residue |
| C | LEU110 |
| C | PRO132 |
| C | THR133 |
| C | GLY134 |
| C | SER135 |
| C | GLY136 |
| C | LYS137 |
| C | SER138 |
| C | THR139 |
| C | ARG278 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue ATP D 401 |
| Chain | Residue |
| D | LEU110 |
| D | PRO132 |
| D | THR133 |
| D | GLY134 |
| D | SER135 |
| D | GLY136 |
| D | LYS137 |
| D | SER138 |
| D | THR139 |
| D | ARG278 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ATP E 401 |
| Chain | Residue |
| E | LEU110 |
| E | PRO132 |
| E | THR133 |
| E | GLY134 |
| E | SER135 |
| E | GLY136 |
| E | LYS137 |
| E | SER138 |
| E | THR139 |
| E | ARG278 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue ATP F 401 |
| Chain | Residue |
| F | LEU110 |
| F | PRO132 |
| F | THR133 |
| F | GLY134 |
| F | SER135 |
| F | GLY136 |
| F | LYS137 |
| F | SER138 |
| F | THR139 |
| F | ARG278 |
Functional Information from PROSITE/UniProt
| site_id | PS00662 |
| Number of Residues | 15 |
| Details | T2SP_E Bacterial type II secretion system protein E signature. LRqdPDvVLVGELRD |
| Chain | Residue | Details |
| A | LEU194-ASP208 | |
