4AY0
High resolution crystal structure of the monomeric subunit-free Caf1M chaperone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006457 | biological_process | protein folding |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043711 | biological_process | pilus organization |
| A | 0044183 | molecular_function | protein folding chaperone |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005515 | molecular_function | protein binding |
| B | 0006457 | biological_process | protein folding |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0043711 | biological_process | pilus organization |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
| site_id | PS00635 |
| Number of Residues | 18 |
| Details | PILI_CHAPERONE Gram-negative pili assembly chaperone signature. FPrDKESLkWlCVkgIPP |
| Chain | Residue | Details |
| A | PHE87-PRO104 |






