Literature summary for 2.7.11.1 extracted from

Li, P.; Xu, D.; Ma, T.; Wang, D.; Li, W.; He, J.; Ran, T.; Wang, W.
Crystal structures of the kinase domain of PpkA, a key regulatory component of T6SS, reveal a general inhibitory mechanism (2018), Biochem. J., 475, 2209-2224 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapour-diffusion method at 16°C. The structure of PpkA-294 is determined in its apo form to a 1.6 A resolution as well as in complex with ATP to a 1.41 A resolution and with an ATP analogue AMP-PCP to a 1.45 A resolution. The residues in the activation loop of PpkA-294 are fully determined, and the N-terminus of the loop is folded into an unprecedented inhibitory helix, revealing that the PpkA kinase domain is in an autoinhibitory state	Serratia marcescens

Crystallization (Comment)

Organism

sitting-drop vapour-diffusion method at 16°C. The structure of PpkA-294 is determined in its apo form to a 1.6 A resolution as well as in complex with ATP to a 1.41 A resolution and with an ATP analogue AMP-PCP to a 1.45 A resolution. The residues in the activation loop of PpkA-294 are fully determined, and the N-terminus of the loop is folded into an unprecedented inhibitory helix, revealing that the PpkA kinase domain is in an autoinhibitory state

Serratia marcescens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	membrane-spanning protein	Serratia marcescens	16020	-

Organism

Organism	UniProt	Comment	Textmining
Serratia marcescens	A0A1S4NYE5	-	-
Serratia marcescens FS14	A0A1S4NYE5	-	-

Synonyms

Synonyms	Comment	Organism
PpkA	-	Serratia marcescens

General Information

General Information	Comment	Organism
physiological function	the enzyme (PpkA) is essential for T6SS secretion in Serratia marcescens since its deletion eliminated the secretion of haemolysin co-regulated protein, while the periplasmic and transmembrane portion of PpkA is disposable for T6SS secretion	Serratia marcescens

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Release 2023.1 (January 2023)