Sequence of LEP4_VIBVU
EC Number:3.4.23.43
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
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
Other sequences found for EC No. 3.4.23.43
General information:
Sequence
0 MDALQYYPWL YIGLASLFGL LVGSFLNVVI YRLPKIMELE WRQECAESFP EYNITPPTET
60 LTLSTPRSSC PSCHTPIRVR DNIPVFSWLA LRGKCHHCQT KISARYPFVE ALSAFLCGLV
120 AWKFGYAPIT VALIGFTLVL IAATFIDLDT MLLPDQLTLP LTWTGIALAL LEISPVSLQD
180 SVFGAMAGYL CLWSVYHLFR LLTGKEGMGY GDFKLLAALG AWLGWQYLPM IILLSSVVGL
240 IFGLIQLRLQ KQGIEMAFPF GPYLAIAGWV ALMWGDSLMS WYLNYLIGA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
53281
Paranjpye R.N.,Lara J.C.,Pepe J.C.,Pepe C.M.,Strom M.S.
The type IV leader peptidase/N-methyltransferase of Vibrio vulnificus controls factors required for adherence to HEp-2 cells and virulence in iron-overloaded mice.
Infect. Immun.
66
5659-5668
1998
53283
Park J.,Ryu S.Y.,Kim C.M.,Shin S.H.
Two forms of Vibrio vulnificus metalloprotease VvpE are secreted via the type II general secretion system.
J. Microbiol.
46
338-343
2008
