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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 501 |
| Chain | Residue |
| A | ASP235 |
| A | ASN374 |
| A | ASP378 |
| A | VAL390 |
| A | THR394 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 502 |
| Chain | Residue |
| A | TYR175 |
| A | SER179 |
| A | ILE182 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 503 |
| Chain | Residue |
| A | PHE315 |
| A | HIS319 |
| A | GLU440 |
| A | PHE23 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 504 |
| Chain | Residue |
| A | ILE369 |
| A | TYR404 |
| A | ASN439 |
| A | PHE441 |
| A | LEU444 |
| A | OLC505 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 505 |
| Chain | Residue |
| A | PHE407 |
| A | LYS410 |
| A | PHE441 |
| A | OLC504 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 506 |
| Chain | Residue |
| A | ASN85 |
| A | LEU89 |
| A | PHE206 |
| A | THR207 |
| A | ILE208 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue OLC A 507 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE A 508 |
| Chain | Residue |
| A | LEU27 |
| A | LYS30 |
| A | TYR31 |
| A | HIS319 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE A 509 |
| Chain | Residue |
| A | PHE283 |
| A | ASN284 |
| A | SER408 |
| A | VAL409 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE A 510 |
| Chain | Residue |
| A | TYR285 |
| A | ASN288 |
| A | ASP289 |
| A | LYS292 |
| A | ASP416 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 285 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 74 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 73 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
