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
Functions
endopeptidase activity / peptidase activity / serine-type endopeptidase activity / toxic substance binding
Processes
protein processing / proteolysis / signal peptide processing
Components
integral 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
ResourceLink
UniProtKB IDP00803
UniProtKB Entry NameLEP_ECOLI
GenBank Protein ID146600
GenBank Gene IDK00426
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01934Arylomycin A2experimentalunknownDetails
DB06904(5S,6S)-6-[(R)ACETOXYETH-2-YL]-PENEM-3-CARBOXYLATEPROPANEexperimentalunknownDetails
DB020801-{2-[2-(2-Methoxyethoxy)Ethoxy]Ethoxy}-4-(1,1,3,3-Tetramethylbutyl)BenzeneexperimentalunknownDetails