9GOQ

Structure of the S.aureus MecA protein, in complex with ClpC

Functional Information from GO Data

Chain	GOid	namespace	contents
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
a	1990169	biological_process	stress response to copper ion
a	1990170	biological_process	stress response to cadmium ion
A	0030674	molecular_function	protein-macromolecule adaptor activity
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
b	1990169	biological_process	stress response to copper ion
b	1990170	biological_process	stress response to cadmium ion
B	0030674	molecular_function	protein-macromolecule adaptor activity
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
c	1990169	biological_process	stress response to copper ion
c	1990170	biological_process	stress response to cadmium ion
C	0030674	molecular_function	protein-macromolecule adaptor activity
d	0005524	molecular_function	ATP binding
d	0006457	biological_process	protein folding
d	0016887	molecular_function	ATP hydrolysis activity
d	0044183	molecular_function	protein folding chaperone
d	1990169	biological_process	stress response to copper ion
d	1990170	biological_process	stress response to cadmium ion
D	0030674	molecular_function	protein-macromolecule adaptor activity
e	0005524	molecular_function	ATP binding
e	0006457	biological_process	protein folding
e	0016887	molecular_function	ATP hydrolysis activity
e	0044183	molecular_function	protein folding chaperone
e	1990169	biological_process	stress response to copper ion
e	1990170	biological_process	stress response to cadmium ion
E	0030674	molecular_function	protein-macromolecule adaptor activity
f	0005524	molecular_function	ATP binding
f	0006457	biological_process	protein folding
f	0016887	molecular_function	ATP hydrolysis activity
f	0044183	molecular_function	protein folding chaperone
f	1990169	biological_process	stress response to copper ion
f	1990170	biological_process	stress response to cadmium ion
F	0030674	molecular_function	protein-macromolecule adaptor activity
g	0005524	molecular_function	ATP binding
g	0006457	biological_process	protein folding
g	0016887	molecular_function	ATP hydrolysis activity
g	0044183	molecular_function	protein folding chaperone
g	1990169	biological_process	stress response to copper ion
g	1990170	biological_process	stress response to cadmium ion
h	0005524	molecular_function	ATP binding
h	0006457	biological_process	protein folding
h	0016887	molecular_function	ATP hydrolysis activity
h	0044183	molecular_function	protein folding chaperone
h	1990169	biological_process	stress response to copper ion
h	1990170	biological_process	stress response to cadmium ion
i	0005524	molecular_function	ATP binding
i	0006457	biological_process	protein folding
i	0016887	molecular_function	ATP hydrolysis activity
i	0044183	molecular_function	protein folding chaperone
i	1990169	biological_process	stress response to copper ion
i	1990170	biological_process	stress response to cadmium ion
l	0005524	molecular_function	ATP binding
l	0006457	biological_process	protein folding
l	0016887	molecular_function	ATP hydrolysis activity
l	0044183	molecular_function	protein folding chaperone
l	1990169	biological_process	stress response to copper ion
l	1990170	biological_process	stress response to cadmium ion
m	0005524	molecular_function	ATP binding
m	0006457	biological_process	protein folding
m	0016887	molecular_function	ATP hydrolysis activity
m	0044183	molecular_function	protein folding chaperone
m	1990169	biological_process	stress response to copper ion
m	1990170	biological_process	stress response to cadmium ion
n	0005524	molecular_function	ATP binding
n	0006457	biological_process	protein folding
n	0016887	molecular_function	ATP hydrolysis activity
n	0044183	molecular_function	protein folding chaperone
n	1990169	biological_process	stress response to copper ion
n	1990170	biological_process	stress response to cadmium ion

Functional Information from PROSITE/UniProt

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

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. RVDmSEFmEKhAvSRLvGA

Chain	Residue	Details
a	ARG571-ALA589

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	384
Details	Region: {"description":"Repeat 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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