8P4P

Structure average of GroEL14 complexes found in the cytosol of Escherichia coli overexpressing GroEL obtained by cryo electron tomography

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0042026	biological_process	protein refolding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0042026	biological_process	protein refolding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0042026	biological_process	protein refolding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0042026	biological_process	protein refolding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0042026	biological_process	protein refolding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0005524	molecular_function	ATP binding
F	0006457	biological_process	protein folding
F	0042026	biological_process	protein refolding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005524	molecular_function	ATP binding
G	0006457	biological_process	protein folding
G	0042026	biological_process	protein refolding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0005524	molecular_function	ATP binding
H	0006457	biological_process	protein folding
H	0042026	biological_process	protein refolding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
I	0005524	molecular_function	ATP binding
I	0006457	biological_process	protein folding
I	0042026	biological_process	protein refolding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
J	0005524	molecular_function	ATP binding
J	0006457	biological_process	protein folding
J	0042026	biological_process	protein refolding
J	0140662	molecular_function	ATP-dependent protein folding chaperone
K	0005524	molecular_function	ATP binding
K	0006457	biological_process	protein folding
K	0042026	biological_process	protein refolding
K	0140662	molecular_function	ATP-dependent protein folding chaperone
L	0005524	molecular_function	ATP binding
L	0006457	biological_process	protein folding
L	0042026	biological_process	protein refolding
L	0140662	molecular_function	ATP-dependent protein folding chaperone
M	0005524	molecular_function	ATP binding
M	0006457	biological_process	protein folding
M	0042026	biological_process	protein refolding
M	0140662	molecular_function	ATP-dependent protein folding chaperone
N	0005524	molecular_function	ATP binding
N	0006457	biological_process	protein folding
N	0042026	biological_process	protein refolding
N	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PROSITE/UniProt

site_id	PS00296
Number of Residues	12
Details	CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGVVaGGG

Chain	Residue	Details
A	ALA405-GLY416

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