Analysis of chimeric chemoreceptors in Bacillus subtilis reveals a role for CheD in the function of the McpC HAMP domain

Journal of Bacteriology

Volumn 186, Issue 17, 2004, Pages 5950-5955

  Kristich, Christopher J ^b   Ordal, George W ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; PHOSPHOTRANSFERASE; PROLINE; PROTEIN CHED; PROTEIN MCPC; RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CHEMORECEPTOR; CHEMOTAXIS; MOLECULAR INTERACTION; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROKARYOTE; PROTEIN DOMAIN; PROTEIN MODIFICATION; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ASPARAGINE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CHEMORECEPTORS; CHEMOTACTIC FACTORS; CHEMOTAXIS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MOVEMENT; PROLINE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT;

BACILLUS SUBTILIS; POSIBACTERIA; PROKARYOTA;

EID: 4344663857     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.17.5950-5955.2004     Document Type: Article

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