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7ABR

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
A0030420biological_processestablishment of competence for transformation
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
B0030420biological_processestablishment of competence for transformation
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
C0030420biological_processestablishment of competence for transformation
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
D0030420biological_processestablishment of competence for transformation
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0016887molecular_functionATP hydrolysis activity
E0030420biological_processestablishment of competence for transformation
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0016887molecular_functionATP hydrolysis activity
F0030420biological_processestablishment of competence for transformation
Functional Information from PROSITE/UniProt
site_idPS00870
Number of Residues13
DetailsCLPAB_1 Chaperonins clpA/B signature 1. DASNILKPsLarG
ChainResidueDetails
AASP295-GLY307

site_idPS00871
Number of Residues19
DetailsCLPAB_2 Chaperonins clpA/B signature 2. RIDmSEYmEKhStSRLvGS
ChainResidueDetails
AARG571-SER589

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY208
EGLY545
FGLY208
FGLY545
AGLY545
BGLY208
BGLY545
CGLY208
CGLY545
DGLY208
DGLY545
EGLY208

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PDB entries from 2024-07-24

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