3DOS

Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Thr7Phe and Ala9Val mutations in the Gd donor strand

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0043711	biological_process	pilus organization
A	0061077	biological_process	chaperone-mediated protein folding
A	0071555	biological_process	cell wall organization
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0007155	biological_process	cell adhesion
B	0009289	cellular_component	pilus
B	0042603	cellular_component	capsule
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0007155	biological_process	cell adhesion
C	0009289	cellular_component	pilus
C	0042603	cellular_component	capsule
D	0005515	molecular_function	protein binding
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0043711	biological_process	pilus organization
D	0061077	biological_process	chaperone-mediated protein folding
D	0071555	biological_process	cell wall organization
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0007155	biological_process	cell adhesion
E	0009289	cellular_component	pilus
E	0042603	cellular_component	capsule
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0007155	biological_process	cell adhesion
F	0009289	cellular_component	pilus
F	0042603	cellular_component	capsule

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

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