Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016462 | molecular_function | pyrophosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0050380 | molecular_function | undecaprenyl-diphosphatase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue HG A 301 |
| Chain | Residue |
| A | CYS162 |
| A | CYS165 |
| A | OLC305 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue HG A 302 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue TRS A 303 |
| Chain | Residue |
| A | MET185 |
| A | ARG145 |
| A | ARG145 |
| A | ARG155 |
| A | ARG155 |
| A | MET185 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue OLC A 304 |
| Chain | Residue |
| A | HIS30 |
| A | ILE74 |
| A | HIS75 |
| A | PHE76 |
| A | LEU248 |
| A | ARG251 |
| A | ILE252 |
| A | TYR260 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue OLC A 305 |
| Chain | Residue |
| A | LEU105 |
| A | VAL128 |
| A | ALA135 |
| A | CYS138 |
| A | LEU139 |
| A | TYR154 |
| A | PHE158 |
| A | LEU166 |
| A | HG301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 140 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | SER6-SER26 | |
| A | ALA45-TRP65 | |
| A | LEU90-HIS110 | |
| A | LEU116-ALA136 | |
| A | TYR190-LEU210 | |
| A | GLY222-ILE242 | |
| A | ILE252-PHE272 | |
