7ABR

Cryo-EM structure of B. subtilis ClpC (DWB mutant) hexamer bound to a substrate polypeptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0030420	biological_process	establishment of competence for transformation
A	0044183	molecular_function	protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0030420	biological_process	establishment of competence for transformation
B	0044183	molecular_function	protein folding chaperone
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0030420	biological_process	establishment of competence for transformation
C	0044183	molecular_function	protein folding chaperone
D	0000166	molecular_function	nucleotide binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0030420	biological_process	establishment of competence for transformation
D	0044183	molecular_function	protein folding chaperone
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0030420	biological_process	establishment of competence for transformation
E	0044183	molecular_function	protein folding chaperone
F	0000166	molecular_function	nucleotide binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0030420	biological_process	establishment of competence for transformation
F	0044183	molecular_function	protein folding chaperone

Functional Information from PROSITE/UniProt

site_id	PS00870
Number of Residues	13
Details	CLPAB_1 Chaperonins clpA/B signature 1. DASNILKPsLarG

Chain	Residue	Details
A	ASP295-GLY307

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site_id	PS00871
Number of Residues	19
Details	CLPAB_2 Chaperonins clpA/B signature 2. RIDmSEYmEKhStSRLvGS

Chain	Residue	Details
A	ARG571-SER589

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	764
Details	Region: {"description":"II"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	84
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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