Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0000166 | molecular_function | nucleotide binding | 
| A | 0005524 | molecular_function | ATP binding | 
| A | 0016887 | molecular_function | ATP hydrolysis activity | 
| A | 0046872 | molecular_function | metal ion binding | 
| B | 0000166 | molecular_function | nucleotide binding | 
| B | 0005524 | molecular_function | ATP binding | 
| B | 0016887 | molecular_function | ATP hydrolysis activity | 
| B | 0046872 | molecular_function | metal ion binding | 
| C | 0000166 | molecular_function | nucleotide binding | 
| C | 0005524 | molecular_function | ATP binding | 
| C | 0016887 | molecular_function | ATP hydrolysis activity | 
| C | 0046872 | molecular_function | metal ion binding | 
| D | 0000166 | molecular_function | nucleotide binding | 
| D | 0005524 | molecular_function | ATP binding | 
| D | 0016887 | molecular_function | ATP hydrolysis activity | 
| D | 0046872 | molecular_function | metal ion binding | 
| E | 0000166 | molecular_function | nucleotide binding | 
| E | 0005524 | molecular_function | ATP binding | 
| E | 0016887 | molecular_function | ATP hydrolysis activity | 
| E | 0046872 | molecular_function | metal ion binding | 
| F | 0000166 | molecular_function | nucleotide 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 | 14 | 
| Details | binding site for residue ADP A 401 | 
| Chain | Residue | 
| A | LEU110 | 
| A | GLU164 | 
| A | LEU269 | 
| A | ARG278 | 
| A | LEU280 | 
| A | HOH501 | 
| A | PRO132 | 
| A | THR133 | 
| A | GLY134 | 
| A | SER135 | 
| A | GLY136 | 
| A | LYS137 | 
| A | SER138 | 
| A | THR139 | 
| site_id | AC2 | 
| Number of Residues | 12 | 
| Details | binding site for residue ADP B 401 | 
| Chain | Residue | 
| B | LEU110 | 
| B | PRO132 | 
| B | THR133 | 
| B | GLY134 | 
| B | SER135 | 
| B | GLY136 | 
| B | LYS137 | 
| B | SER138 | 
| B | THR139 | 
| B | LEU269 | 
| B | ARG278 | 
| B | LEU280 | 
| site_id | AC3 | 
| Number of Residues | 14 | 
| Details | binding site for residue ADP C 401 | 
| Chain | Residue | 
| C | LEU110 | 
| C | PRO132 | 
| C | THR133 | 
| C | GLY134 | 
| C | SER135 | 
| C | GLY136 | 
| C | LYS137 | 
| C | SER138 | 
| C | THR139 | 
| C | GLU164 | 
| C | LEU269 | 
| C | ARG278 | 
| C | LEU280 | 
| C | HOH501 | 
| site_id | AC4 | 
| Number of Residues | 13 | 
| Details | binding site for residue ADP E 401 | 
| Chain | Residue | 
| E | LEU110 | 
| E | PRO132 | 
| E | THR133 | 
| E | GLY134 | 
| E | SER135 | 
| E | GLY136 | 
| E | LYS137 | 
| E | SER138 | 
| E | THR139 | 
| E | GLU164 | 
| E | LEU269 | 
| E | ARG278 | 
| E | LEU280 | 
| site_id | AC5 | 
| Number of Residues | 13 | 
| Details | binding site for Di-peptide ADP D 401 and GLY D 134 | 
| Chain | Residue | 
| D | LEU110 | 
| D | PRO132 | 
| D | THR133 | 
| D | SER135 | 
| D | GLY136 | 
| D | LYS137 | 
| D | SER138 | 
| D | THR139 | 
| D | GLU164 | 
| D | LEU269 | 
| D | ARG278 | 
| D | LEU280 | 
| D | HOH501 | 
| site_id | AC6 | 
| Number of Residues | 16 | 
| Details | binding site for Di-peptide ADP F 401 and LYS F 137 | 
| Chain | Residue | 
| F | ARG98 | 
| F | LEU110 | 
| F | VAL129 | 
| F | THR130 | 
| F | GLY131 | 
| F | PRO132 | 
| F | THR133 | 
| F | GLY134 | 
| F | SER135 | 
| F | GLY136 | 
| F | SER138 | 
| F | THR139 | 
| F | THR140 | 
| F | LEU141 | 
| F | LEU269 | 
| F | LEU280 | 
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 |  |