Signal peptidase I
Details
- Name
- Signal peptidase I
- Synonyms
- 3.4.21.89
- Leader peptidase I
- SPase I
- Gene Name
- lepB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016384|Signal peptidase I MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGW LETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTL IETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENA LPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILT VPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAI WMSFDKQEGEWPTGLRLSRIGGIH
- Number of residues
- 324
- Molecular Weight
- 35960.075
- Theoretical pI
- 7.43
- GO Classification
- Functionsendopeptidase activity / peptidase activity / serine-type endopeptidase activity / toxic substance bindingProcessesprotein processing / proteolysis / signal peptide processingComponentsintegral component of membrane / integral component of plasma membrane / plasma membrane
- General Function
- Toxic substance binding
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- 4-22 59-77
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0016385|Signal peptidase I (lepB) ATGGCGAATATGTTTGCCCTGATTCTGGTGATTGCCACACTGGTGACGGGCATTTTATGG TGCGTGGATAAATTCTTTTTCGCACCTAAACGGCGGGAACGTCAGGCAGCGGCGCAGGCG GCTGCCGGGGACTCACTGGATAAAGCAACGTTGAAAAAGGTTGCGCCGAAGCCTGGCTGG CTGGAAACCGGTGCTTCTGTTTTTCCGGTACTGGCTATCGTATTGATTGTGCGTTCGTTT ATTTATGAACCGTTCCAGATCCCGTCAGGTTCGATGATGCCGACTCTGTTAATTGGTGAT TTTATTCTGGTAGAGAAGTTTGCTTATGGCATTAAAGATCCTATCTACCAGAAAACGCTG ATCGAAACCGGTCATCCGAAACGCGGCGATATCGTGGTCTTTAAATATCCGGAAGATCCA AAGCTTGATTACATCAAGCGCGCGGTGGGTTTACCGGGCGATAAAGTCACTTACGATCCG GTCTCAAAAGAGCTGACGATTCAACCGGGATGCAGTTCCGGCCAGGCGTGTGAAAACGCG CTGCCGGTCACCTACTCAAACGTGGAACCGAGCGATTTCGTTCAGACCTTCTCACGCCGT AATGGTGGGGAAGCGACCAGCGGATTCTTTGAAGTGCCGAAAAACGAAACCAAAGAAAAT GGAATTCGTCTTTCCGAGCGTAAAGAGACACTGGGTGATGTGACGCACCGCATTCTGACA GTGCCGATTGCGCAGGATCAGGTGGGGATGTATTACCAGCAGCCAGGGCAACAACTGGCA ACCTGGATTGTTCCTCCGGGACAATACTTCATGATGGGCGACAACCGCGACAACAGCGCG GACAGCCGTTACTGGGGCTTTGTGCCGGAAGCGAATCTGGTCGGTCGGGCAACGGCTATC TGGATGAGCTTCGATAAGCAAGAAGGCGAATGGCCGACTGGTCTGCGCTTAAGTCGCATT GGCGGCATCCATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00803 UniProtKB Entry Name LEP_ECOLI GenBank Protein ID 146600 GenBank Gene ID K00426 - General References
- Wolfe PB, Wickner W, Goodman JM: Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J Biol Chem. 1983 Oct 10;258(19):12073-80. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Heijne G: The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 1986 Nov;5(11):3021-7. [Article]
- Bilgin N, Lee JI, Zhu HY, Dalbey R, von Heijne G: Mapping of catalytically important domains in Escherichia coli leader peptidase. EMBO J. 1990 Sep;9(9):2717-22. [Article]
- Sung M, Dalbey RE: Identification of potential active-site residues in the Escherichia coli leader peptidase. J Biol Chem. 1992 Jul 5;267(19):13154-9. [Article]
- Black MT, Munn JG, Allsop AE: On the catalytic mechanism of prokaryotic leader peptidase 1. Biochem J. 1992 Mar 1;282 ( Pt 2):539-43. [Article]
- Black MT: Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad. J Bacteriol. 1993 Aug;175(16):4957-61. [Article]
- San Millan JL, 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. 1989 Oct;171(10):5536-41. [Article]
- Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
- Fontaine F, Fuchs RT, Storz G: Membrane localization of small proteins in Escherichia coli. J Biol Chem. 2011 Sep 16;286(37):32464-74. doi: 10.1074/jbc.M111.245696. Epub 2011 Jul 21. [Article]
- Paetzel M, Dalbey RE, Strynadka NC: Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature. 1998 Nov 12;396(6707):186-90. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01934 Arylomycin A2 experimental unknown Details DB06904 (5S,6S)-6-[(R)ACETOXYETH-2-YL]-PENEM-3-CARBOXYLATEPROPANE experimental unknown Details DB02080 1-{2-[2-(2-Methoxyethoxy)Ethoxy]Ethoxy}-4-(1,1,3,3-Tetramethylbutyl)Benzene experimental unknown Details