Sequence of LEP_ECOLI
EC Number:3.4.21.89
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Cleavage of hydrophobic, N-terminal signal or leader sequences
Other sequences found for EC No. 3.4.21.89
General information:
Sequence
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>P00803|Signal peptidase I|EC 3.4.21.89|Escherichia coli (strain K12)|Swiss-Prot
MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGW
LETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTL
IETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENA
LPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILT
VPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAI
WMSFDKQEGEWPTGLRLSRIGGIH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
182336
Wolfe P.B.,Wickner W.,Goodman J.M.
Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope.
J. Biol. Chem.
258
12073-12080
1983
182338
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
182339
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
182340
von Heijne G.
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology.
EMBO J.
5
3021-3027
1986
182341
Bilgin N.,Lee J.I.,Zhu H.Y.,Dalbey R.,von Heijne G.
Mapping of catalytically important domains in Escherichia coli leader peptidase.
EMBO J.
9
2717-2722
1990
182342
Sung M.,Dalbey R.E.
Identification of potential active-site residues in the Escherichia coli leader peptidase.
J. Biol. Chem.
267
13154-13159
1992
182343
Black M.T.,Munn J.G.R.,Allsop A.E.
On the catalytic mechanism of prokaryotic leader peptidase 1.
Biochem. J.
282
539-543
1992
182344
Black M.T.
Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad.
J. Bacteriol.
175
4957-4961
1993
182345
San Millan J.L.,Boyd D.,Dalbey R.,Wickner W.,Beckwith J.
Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase.
J. Bacteriol.
171
5536-5541
1989
182346
Daley D.O.,Rapp M.,Granseth E.,Melen K.,Drew D.,von Heijne G.
Global topology analysis of the Escherichia coli inner membrane proteome.
Science
308
1321-1323
2005
182347
Fontaine F.,Fuchs R.T.,Storz G.
Membrane localization of small proteins in Escherichia coli.
J. Biol. Chem.
286
32464-32474
2011
182348
Paetzel M.,Dalbey R.E.,Strynadka N.C.
Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor.
Nature
396
186-190
1998
