The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa

Molecular Microbiology

Volumn 93, Issue 1, 2014, Pages 113-128

  Jorgenson, Matthew A ^a   Chen, Yan ^b   Yahashiri, Atsushi ^a   Popham, David L ^b   Weiss, David S ^a  

^a UNIVERSITY OF IOWA   (United States)

^b VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIB PROTEIN; AMIDASE; BACTERIAL PROTEIN; GLYCOSYLTRANSFERASE; MLTB1 PROTEIN; PEPTIDOGLYCAN; RARE LIPOPROTEIN A PROTEIN; SACCULI; SLTB1 PROTEIN; UNCLASSIFIED DRUG; GLYCOSIDASE;

ARTICLE; BACTERIAL CELL; BACTERIAL GROWTH; CELL SEPARATION; CELL SHAPE; CELL STRUCTURE; CONTROLLED STUDY; DAUGHTER CELL; DEGRADATION KINETICS; ENZYME ACTIVITY; NONHUMAN; OSMOLARITY; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PSEUDOMONAS AERUGINOSA; CELL DIVISION; CELL WALL; CYTOLOGY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; MUTATION; PHYSIOLOGY;

BACTERIAL PROTEINS; CELL DIVISION; CELL WALL; GLYCOSIDE HYDROLASES; MUTATION; PEPTIDOGLYCAN; PSEUDOMONAS AERUGINOSA; SUBSTRATE SPECIFICITY;

EID: 84903374199     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12643     Document Type: Article

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