2LP4

Solution structure of P1-CheY/P2 complex in bacterial chemotaxis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000160	biological_process	phosphorelay signal transduction system
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

Functional Information from PROSITE/UniProt

site_id	PS00039
Number of Residues	9
Details	DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. FFDEADElL

Chain	Residue	Details
A	PHE12-LEU20

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9

Chain	Residue	Details
Y	ASP12

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:8176739, ECO:0007744|PDB:1CHN

Chain	Residue	Details
Y	ASP13
Y	ASP57
Y	ASN59

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446

Chain	Residue	Details
Y	ASP57

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:9560203

Chain	Residue	Details
Y	LYS92

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:9560203

Chain	Residue	Details
Y	LYS109

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