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 | 0015648 | molecular_function | lipid-linked peptidoglycan transporter activity |
| A | 0015836 | biological_process | lipid-linked peptidoglycan transport |
| A | 0034204 | biological_process | lipid translocation |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0015648 | molecular_function | lipid-linked peptidoglycan transporter activity |
| B | 0015836 | biological_process | lipid-linked peptidoglycan transport |
| B | 0034204 | biological_process | lipid translocation |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue OLC A 501 |
| Chain | Residue |
| A | ASN85 |
| B | TYR175 |
| B | OLC502 |
| A | SER88 |
| A | LEU92 |
| A | TYR133 |
| A | PHE206 |
| A | THR207 |
| A | ILE208 |
| A | OLC503 |
| B | LYS174 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 502 |
| Chain | Residue |
| A | VAL227 |
| A | PHE364 |
| A | ALA367 |
| A | THR368 |
| A | SER371 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 503 |
| Chain | Residue |
| A | LEU89 |
| A | OLC501 |
| B | OLC502 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | TYR68 |
| A | LYS76 |
| A | ILE144 |
| A | ASN146 |
| B | ARG280 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue OLC B 501 |
| Chain | Residue |
| B | LEU171 |
| B | TYR175 |
| B | OLC502 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue OLC B 502 |
| Chain | Residue |
| A | PHE206 |
| A | OLC501 |
| A | OLC503 |
| B | OLC501 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue OLC B 503 |
| Chain | Residue |
| A | TYR204 |
| A | PHE206 |
| B | LEU171 |
| B | THR173 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC B 504 |
| Chain | Residue |
| B | ILE182 |
| B | LEU185 |
| B | ILE186 |
| B | ILE189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 550 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 148 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 146 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |