Amino acid identity at one position within the α1 helix of both the histidine kinase and the response regulator of the WalRK and PhoPR two-component systems plays a crucial role in the specificity of phosphotransfer

Microbiology

Volumn 156, Issue 6, 2010, Pages 1848-1859

  Jende, Inga ^a   Varughese, Kottayil I ^b   Devine, Kevin M ^a  

^a TRINITY COLLEGE DUBLIN   (Ireland)

^b UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BETA GALACTOSIDASE; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; MUTANT PROTEIN; PROTEIN HISTIDINE KINASE; PROTEIN HISTIDINE KINASE PHOR; PROTEIN HISTIDINE KINASE WALK; SERINE; THREONINE; UNCLASSIFIED DRUG;

ALPHA 1 HELIX; ALPHA HELIX; AMINO ACID COMPOSITION; ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; AUTORADIOGRAPHY; BACILLUS SUBTILIS; BACTERIAL GENE; BACTERIAL PHENOMENA AND FUNCTIONS; BACTERIAL STRAIN; BACTERIAL TWO COMPONENT SYSTEM WALRK PHOPR; BACTERIUM CULTURE; CONTROLLED STUDY; ENZYME ACTIVITY; GENE EXPRESSION; MOLECULAR CLONING; NONHUMAN; PHOR GENE; PHOSPHATE TRANSPORT; PLASMID; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; WALK GENE;

AMINO ACIDS; BACILLUS SUBTILIS; BACTERIAL PROTEINS; MODELS, MOLECULAR; MUTAGENESIS; PHOSPHORYLATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY;

EID: 77953179874     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.037515-0     Document Type: Article

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