3PXI

Structure of MecA108:ClpC

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0044183	molecular_function	protein folding chaperone
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	0044183	molecular_function	protein folding chaperone
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	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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	423
Details	Domain: {"description":"Clp R","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	105
Details	Domain: {"description":"UVR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00217","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	195
Details	Region: {"description":"Repeat 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	192
Details	Region: {"description":"Repeat 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	42
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---