Nucleotide sequence of the gelatinase gene (gelE) from Enterococcus faecalis subsp. liquefaciens.
The gene coding for gelatinase (also called metalloendopeptidase II; microbial proteinase, EC 3.4.24.4) of Enterococcus faecalis subsp. liquefaciens strain OG1-10 was cloned in an Escherichia coli-Enterococcus shuttle vector, and its nucleotide sequence was determined. The DNA sequence encodes one large open reading frame (ORF) with 509 amino acid residues. The ORF contains a signal sequence in its N-terminal region, whereas the N-terminal amino acid sequence determined from the purified extracellular proteinase starts at residue 192 deduced from the ORF. This implies that the gelatinase is synthesized as a prepropolypeptide or prezymogen. The mature gelatinase contains 318 amino acid residues (molecular weight, 34,582) and has significant homology with neutral proteinases from Bacillus species and elastase from Pseudomonas aeruginosa.
Su
Y A
YA
Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor 48109.
Sulavik
M C
MC
He
P
P
Makinen
K K
KK
Makinen
P L
PL
Fiedler
S
S
Wirth
R
R
Clewell
D B
DB
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology; D001483:Base Sequence; D003001:Cloning, Molecular; D013293:Enterococcus faecalis / Q000201:enzymology / Q000235:genetics*; D018093:Gelatinases; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000032:analysis; D010434:Pepsin A / Q000032:analysis / Q000235:genetics*; D011549:Pseudomonas / Q000201:enzymology
D010196:Pancreatic Elastase; D010434:Pepsin A; D018093:Gelatinases