Cloning and sequencing of pepC, a cysteine aminopeptidase gene from Lactococcus lactis subsp. cremoris AM2.
A gene coding for an aminopeptidase (PepC) from Lactococcus lactis subsp. cremoris AM2 was cloned by complementation of an Escherichia coli mutant lacking aminopeptidase activity. The nucleotide sequence was determined. A portion of the predicted amino acid sequence of PepC (436 amino acids) showed strong homology to the active site of cysteine proteases. No signal sequence was found, indicating an intracellular location of the enzyme.
Chapot-Chartier
M P
MP
Station de Recherches Laitières, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
Nardi
M
M
Chopin
M C
MC
Chopin
A
A
Gripon
J C
JC
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000235:genetics* / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D017124:Conserved Sequence; D005798:Genes, Bacterial; D013294:Lactococcus lactis / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D000626:Aminopeptidases; C086319:PepC thiol aminopeptidase