9JVP

CryoEM structure of M. tuberculosis ClpC1P1P2 complex bound to bortezomib, conformation 3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity
B	0005524	molecular_function	ATP binding
B	0016887	molecular_function	ATP hydrolysis activity
C	0005524	molecular_function	ATP binding
C	0016887	molecular_function	ATP hydrolysis activity
D	0005524	molecular_function	ATP binding
D	0016887	molecular_function	ATP hydrolysis activity
E	0005524	molecular_function	ATP binding
E	0016887	molecular_function	ATP hydrolysis activity
F	0005524	molecular_function	ATP binding
F	0016887	molecular_function	ATP hydrolysis activity
G	0004176	molecular_function	ATP-dependent peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0006508	biological_process	proteolysis
H	0004176	molecular_function	ATP-dependent peptidase activity
H	0004252	molecular_function	serine-type endopeptidase activity
H	0006508	biological_process	proteolysis
I	0004176	molecular_function	ATP-dependent peptidase activity
I	0004252	molecular_function	serine-type endopeptidase activity
I	0006508	biological_process	proteolysis
J	0004176	molecular_function	ATP-dependent peptidase activity
J	0004252	molecular_function	serine-type endopeptidase activity
J	0006508	biological_process	proteolysis
K	0004176	molecular_function	ATP-dependent peptidase activity
K	0004252	molecular_function	serine-type endopeptidase activity
K	0006508	biological_process	proteolysis
L	0004176	molecular_function	ATP-dependent peptidase activity
L	0004252	molecular_function	serine-type endopeptidase activity
L	0006508	biological_process	proteolysis
M	0004176	molecular_function	ATP-dependent peptidase activity
M	0004252	molecular_function	serine-type endopeptidase activity
M	0006508	biological_process	proteolysis
N	0004176	molecular_function	ATP-dependent peptidase activity
N	0004252	molecular_function	serine-type endopeptidase activity
N	0006508	biological_process	proteolysis
O	0004176	molecular_function	ATP-dependent peptidase activity
O	0004252	molecular_function	serine-type endopeptidase activity
O	0006508	biological_process	proteolysis
P	0004176	molecular_function	ATP-dependent peptidase activity
P	0004252	molecular_function	serine-type endopeptidase activity
P	0006508	biological_process	proteolysis
Q	0004176	molecular_function	ATP-dependent peptidase activity
Q	0004252	molecular_function	serine-type endopeptidase activity
Q	0006508	biological_process	proteolysis
R	0004176	molecular_function	ATP-dependent peptidase activity
R	0004252	molecular_function	serine-type endopeptidase activity
R	0006508	biological_process	proteolysis
S	0004176	molecular_function	ATP-dependent peptidase activity
S	0004252	molecular_function	serine-type endopeptidase activity
S	0006508	biological_process	proteolysis
T	0004176	molecular_function	ATP-dependent peptidase activity
T	0004252	molecular_function	serine-type endopeptidase activity
T	0006508	biological_process	proteolysis

Functional Information from PROSITE/UniProt

site_id	PS00306
Number of Residues	8
Details	CASEIN_ALPHA_BETA Caseins alpha/beta signature. CLVAlALA

Chain	Residue	Details
U	CYS8-ALA15

---

site_id	PS00381
Number of Residues	12
Details	CLP_PROTEASE_SER Endopeptidase Clp serine active site. TvcLGqAASAAA

Chain	Residue	Details
M	THR102-ALA113

---

site_id	PS00382
Number of Residues	14
Details	CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RyalPharILMHQP

Chain	Residue	Details
T	ARG112-PRO125
M	ARG124-PRO137

---

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

Chain	Residue	Details
A	ASP303-GLY315

---

Functional Information from SwissProt/UniProt

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

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	77
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	14
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00444","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00444","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	14
Details	Signal: {"evidences":[{"source":"PubMed","id":"10690361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3278933","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4557764","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---