1KMI

CRYSTAL STRUCTURE OF AN E.COLI CHEMOTAXIS PROTEIN, CHEZ

Functional Information from GO Data

Chain	GOid	namespace	contents
Y	0000156	molecular_function	phosphorelay response regulator activity
Y	0000160	biological_process	phosphorelay signal transduction system
Y	0000287	molecular_function	magnesium ion binding
Y	0005515	molecular_function	protein binding
Y	0005737	cellular_component	cytoplasm
Y	0005829	cellular_component	cytosol
Y	0006935	biological_process	chemotaxis
Y	0007165	biological_process	signal transduction
Y	0009288	cellular_component	bacterial-type flagellum
Y	0009433	cellular_component	bacterial-type flagellum basal body, C ring
Y	0009454	biological_process	aerotaxis
Y	0016407	molecular_function	acetyltransferase activity
Y	0018393	biological_process	internal peptidyl-lysine acetylation
Y	0043052	biological_process	thermotaxis
Y	0046872	molecular_function	metal ion binding
Y	0050920	biological_process	regulation of chemotaxis
Y	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
Y	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
Y	0120107	cellular_component	bacterial-type flagellum rotor complex
Y	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility
Z	0003824	molecular_function	catalytic activity
Z	0004721	molecular_function	phosphoprotein phosphatase activity
Z	0005515	molecular_function	protein binding
Z	0005737	cellular_component	cytoplasm
Z	0005829	cellular_component	cytosol
Z	0005886	cellular_component	plasma membrane
Z	0006470	biological_process	protein dephosphorylation
Z	0006935	biological_process	chemotaxis
Z	0009288	cellular_component	bacterial-type flagellum
Z	0016787	molecular_function	hydrolase activity
Z	0042802	molecular_function	identical protein binding
Z	0050920	biological_process	regulation of chemotaxis
Z	0051219	molecular_function	phosphoprotein binding
Z	0071978	biological_process	bacterial-type flagellum-dependent swarming motility
Z	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
Z	0098561	cellular_component	methyl accepting chemotaxis protein complex
Z	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG Y 301

Chain	Residue
Y	ASP13
Y	ASP57
Y	ASN59
Y	BEF201
Z	GLN147

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BEF Y 201

Chain	Residue
Y	ALA88
Y	MG301
Z	GLN147
Y	ASP57
Y	TRP58
Y	ASN59
Y	THR87

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BCN Z 215

Chain	Residue
Z	HIS12
Z	GLN39
Z	PHE98
Z	THR112

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	117
Details	Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8176739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CHN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1869568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2689446","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11359578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Enhances dephosphorylation of CheY-P"}

Chain

Residue

Details

---