1UDR

CHEY MUTANT WITH LYS 91 REPLACED BY ASP, LYS 92 REPLACED BY ALA, ILE 96 REPLACED BY LYS AND ALA 98 REPLACED BY LEU (STABILIZING MUTATIONS IN HELIX 4)

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	468
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	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
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	4
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	4
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	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"1390767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9560203","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---