1FFG

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY AT 2.1 A RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000156	molecular_function	phosphorelay response regulator activity
A	0000160	biological_process	phosphorelay signal transduction system
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006935	biological_process	chemotaxis
A	0007165	biological_process	signal transduction
A	0009288	cellular_component	bacterial-type flagellum
A	0009433	cellular_component	bacterial-type flagellum basal body, C ring
A	0009454	biological_process	aerotaxis
A	0016407	molecular_function	acetyltransferase activity
A	0018393	biological_process	internal peptidyl-lysine acetylation
A	0043052	biological_process	thermotaxis
A	0046872	molecular_function	metal ion binding
A	0050920	biological_process	regulation of chemotaxis
A	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
A	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
A	0120107	cellular_component	bacterial-type flagellum rotor complex
A	1902021	biological_process	regulation of bacterial-type flagellum-dependent cell motility
C	0000156	molecular_function	phosphorelay response regulator activity
C	0000160	biological_process	phosphorelay signal transduction system
C	0000287	molecular_function	magnesium ion binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006935	biological_process	chemotaxis
C	0007165	biological_process	signal transduction
C	0009288	cellular_component	bacterial-type flagellum
C	0009433	cellular_component	bacterial-type flagellum basal body, C ring
C	0009454	biological_process	aerotaxis
C	0016407	molecular_function	acetyltransferase activity
C	0018393	biological_process	internal peptidyl-lysine acetylation
C	0043052	biological_process	thermotaxis
C	0046872	molecular_function	metal ion binding
C	0050920	biological_process	regulation of chemotaxis
C	0071977	biological_process	bacterial-type flagellum-dependent swimming motility
C	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility
C	0120107	cellular_component	bacterial-type flagellum rotor complex
C	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 MN A 1

Chain	Residue
A	ASP12
A	ASP13
A	ASP57
A	ASN59
A	HOH218

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 130

Chain	Residue
C	HOH191
C	ASP12
C	ASP13
C	ASP57
C	ASN59

---

Functional Information from PROSITE/UniProt

site_id	PS00430
Number of Residues	108
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. rqlaleakgetpsavtrlsvvaksepqdeqsrsqsprriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfvieadqitf...............ETVEVSPK

Chain	Residue	Details
B	ARG124-LYS231

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	234
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	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
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	2
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	2
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	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---