3.4.23.43: prepilin peptidase
This is an abbreviated version!
For detailed information about prepilin peptidase, go to the full flat file.
Reaction
typically cleaves a -Gly-/-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine
=
Synonyms
ComC, HofD, More, PibD, PilD, PilD-like protein, Pilin leader peptidase, PilU, pre-pseudopilin peptidase, preflagellin peptidase, Prepilin peptidase, prepilin peptidase PilD/XcpA, proepilin peptidase PulO, proteinase, pilin precursor, PulO, PulO prepilin peptidase, TadV protein, TcpJ, TFPP, type 4 prepilin peptidase, type 4 prepilin-like proteins leader peptide-processing enzyme, type IV prepilin peptidase, type IV prepilin-like peptidase, VcpD, XcpA, XpsO
ECTree
General Information
General Information on EC 3.4.23.43 - prepilin peptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
the deletion strain DpibD does not exhibit any type IV pilus-like structures. Attachment to surfaces is strongly reduced in the pibD deletion strain and no growth defect is observed
malfunction
-
the deletion strain DpibD does not exhibit any type IV pilus-like structures. Attachment to surfaces is strongly reduced in the pibD deletion strain and no growth defect is observed
-
metabolism
-
prepilin peptidase cleaves the positively charged peptide anchor on the cytoplasmic face of the transmembrane segment
metabolism
-
the enzyme is needed for maturation of preflagellins and other type IV pilin-like proteins
metabolism
-
the enzyme is needed for maturation of preflagellins and other type IV pilin-like proteins
physiological function
-
pilD mutant is unable to produce pili. PilD deficiency also leads to a nonfunctional type II secretion system. Loss of metal reduction in a PilD mutant is due to a type II secretion deficiency, and therefore the absence of c-cytochromes from the outer surface of MR-1 cells, and not the loss of pili or flagella
physiological function
a prepilin peptidase pilD null mutant accumulates an unprocessed form of the major pilin PilA1 and its non-glycosylated derivative. The mutant strain has aberrant membrane ultrastructure and does not grow photoautotrophically because the synthesis of Photosystem II subunits is abolished. Other membrane components such as Photosystem I and ATP synthase are synthesized at levels comparable to the control strain. Proliferation of the pilD mutant strain is rescued by elimination of the pilA1 gene. PilA1 co-immunoprecipitates with the SecY translocase and the YidC insertase, and both of these essential translocon components are degraded in the mutant
physiological function
-
pilD mutant is unable to produce pili. PilD deficiency also leads to a nonfunctional type II secretion system. Loss of metal reduction in a PilD mutant is due to a type II secretion deficiency, and therefore the absence of c-cytochromes from the outer surface of MR-1 cells, and not the loss of pili or flagella
-