Conserved sequence motif at the C-terminus of the bacterial cell-division protein FtsA.
FtsA is an essential part of the septal ring structure in bacterial cell division. Two peptide-protein interactions are known in this process: FtsA and ZipA bind the C-terminus of FtsZ, the bacterial tubulin homologue, which is the first septal component to appear at the septum. Our recent crystal structure of FtsA revealed a possible peptide binding site on FtsA and a long disordered C-terminal region. Here we show that all FtsA proteins contain a conserved 10-13 residue motif at the C-terminal end that may facilitate targeting of downstream septal components.
MRC Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK. jyl@mrc-lmb.cam.ac.uk
J
J
Löwe
F
F
van den Ent
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D002455:Cell Division; D017124:Conserved Sequence; D016208:Databases, Factual; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D001426:Bacterial Proteins; C065103:FtsA protein, Bacteria