The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins

FEMS Microbiology Letters

Volumn 176, Issue 1, 1999, Pages 111-116

  Aravind, L ^a   Ponting, Chris P ^a,b  

^a TEXAS A AND M UNIVERSITY   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Adenylyl cyclase; Chemotaxis; Histidine kinase; PAS domain; PP2C like phosphatase; Regulator of receptor function; Sequence analysis

Indexed keywords

ADENYLATE CYCLASE; CYTOPLASM PROTEIN; HISTIDINE; PHOSPHOTRANSFERASE; RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; CHEMORECEPTOR; LIGAND BINDING; METHYLATION; PHOSPHORYLATION; PRIORITY JOURNAL; PROKARYOTE; PROTEIN DOMAIN; SIGNAL TRANSDUCTION;

ADENYLATE CYCLASE; AMINO ACID SEQUENCE; BACTERIA; GENES, BACTERIAL; MOLECULAR SEQUENCE DATA; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN KINASES; PROTEINS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, PEPTIDE; SEQUENCE ALIGNMENT;

EID: 0032766134     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00197-4     Document Type: Article

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