TY  - JOUR
N1  - Copyright of this article belongs to Elsevier Science.
ID  - open1219
UR  - http://www.sciencedirect.com/science/article/pii/S0014579312007144
IS  - 21
A1  - Srinivasan, Vijaya Bharathi
A1  - Vaidyanathan, Vasanth
A1  - Mondal, Amitabha
A1  - Venkataramaiah, Manjunath
A1  - Rajamohan, Govindan
Y1  - 2012/11/02/
N2  - Klebsiella pneumoniae MGH78578 contains ?500 uncharacterized signaling proteins and in this study, we characterized the biological functions of a novel eukaryotic-like serine/threonine kinase; ESTK (KpnK). Studies demonstrated that KpnK undergoes autophosphorylation within the pH range 7.0-7.5 at 37°C in a time- and concentration- dependent manner, with Mn(2+) as its cofactor. The ?kpnK mutant exhibited higher sensitivity to gastrointestinal and oxidative stresses. Deletion of kpnK resulted in a two to threefold increased susceptibility towards imipenem, cefepime, ceftriaxone and ceftazidime. Our study has provided overall evidence for the involvement of ESTK in regulating bacterial physiology, stress response and drug resistance. This report has unmasked the occurrence of Ser/Thr kinase mediated signaling for the first time in K. pneumoniae. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: KpnKphosphorylatesKpnK by protein kinase assay (View interaction).
PB  - Elsevier Science
JF  - FEBS letters
VL  - 586
KW  -  Nosocomial pathogen; Antimicrobial resistance; Ser/Thr kinase;Klebsiella pneumoniae
SN  - 1873-3468
TI  - Functional characterization of a novel Mn(2+) dependent protein serine/threonine kinase KpnK, produced by Klebsiella pneumoniae strain MGH78578.
SP  - 3778
EP  - 86
ER  -