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Escherichia coli K-12 substr. MG1655 Enzyme: prolipoprotein signal peptidase II



Gene: lspA Accession Numbers: EG10548 (EcoCyc), b0027, ECK0028

Synonyms: lsp, signal peptidase II, leader peptidase II, SPase II

Regulation Summary Diagram: ?

Summary:
The lspA gene encodes prolipoprotein signal peptidase (signal peptidase II) [Yamagata83, Innis84].

The enzyme activity has been characterized [Tokunaga84, Tokunaga84a, Dev84]. Substrate recognition and specificity of the enzyme has been studied [Pollitt86, Inouye83].

A recessive mutation causing heat-sensitive prolipoprotein signal peptidase activity has been characterized [Yamagata83].

The topology of LspA in the inner membrane has been determined; there are four transmembrane regions and both termini are cytoplasmic [Munoa91]. LspA has four predicted membrane-spanning hydrophobic segments [Innis84]. LspA does not have a predicted signal sequence [Innis84, Yu84].

LspA has similarity to the SPase II of Enterobacter aerogenes [Isaki90], Pseudomonas fluorescens [Isaki90a], Bacillus subtilis [Pragai97]. Staphylococcus aureus Lsp functionally complements inviability of an E. coli lspA mutant [Zhao92].

Regulation has been described [Innis84, Yamada84, Yu84, Tokunaga85, Kamio85, Miller87, Miller87a].

Review: [Hayashi90a, Sankaran95].

Citations: [Regue84, Sakka87, Ghrayeb85, Krishnabhakdi88, Kosic93, Sankaran94, Tokunaga83, Yamagata83a, Yamagata83b, Tokunaga82]

Gene Citations: [Regue84, Brissette91]

Locations: inner membrane

Map Position: [25,207 -> 25,701] (0.54 centisomes)
Length: 495 bp / 164 aa

Molecular Weight of Polypeptide: 18.156 kD (from nucleotide sequence), 18 kD (experimental)

Unification Links: ASAP:ABE-0000096 , CGSC:11326 , DIP:DIP-10129N , EchoBASE:EB0543 , EcoGene:EG10548 , EcoliWiki:b0027 , OU-Microarray:b0027 , PortEco:lspA , PR:PRO_000023127 , RefSeq:NP_414568 , RegulonDB:EG10548 , String:511145.b0027 , UniProt:P00804

Relationship Links: InterPro:IN-FAMILY:IPR001872 , Pfam:IN-FAMILY:PF01252 , Prints:IN-FAMILY:PR00781 , Prosite:IN-FAMILY:PS00855

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006465 - signal peptide processing Inferred from experiment [Yamagata83a]
GO:0006508 - proteolysis Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008233 - peptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, Tokunaga83]
GO:0004190 - aspartic-type endopeptidase activity Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
information transfer protein related export, signal peptide cleavage

Essentiality data for lspA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Enzymatic reaction of: prolipoprotein signal peptidase

Synonyms: signal peptidase, premurein-leader peptidase, leader peptidase, premurein leader proteinase

EC Number: 3.4.23.36

a prolipoprotein + H2O <=> a lipoprotein + a cleaved lipoprotein signal peptide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Inhibitors (Noncompetitive): globomycin [Dev85]

T(opt): 37 °C [BRENDA14, Sankaran95]

pH(opt): 6 [BRENDA14, Sankaran95]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 12 -> 26
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 70 -> 88
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 96 -> 113
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Active-Site 114
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;
Active-Site 141
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;
Transmembrane-Region 142 -> 159
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: probable;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0027 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10548; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Brissette91: Brissette JL, Weiner L, Ripmaster TL, Model P (1991). "Characterization and sequence of the Escherichia coli stress-induced psp operon." J Mol Biol 220(1);35-48. PMID: 1712397

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

Dev84: Dev IK, Ray PH (1984). "Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B." J Biol Chem 259(17);11114-20. PMID: 6381496

Dev85: Dev IK, Harvey RJ, Ray PH (1985). "Inhibition of prolipoprotein signal peptidase by globomycin." J Biol Chem 260(10);5891-4. PMID: 3888977

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Ghrayeb85: Ghrayeb J, Lunn CA, Inouye S, Inouye M (1985). "An alternate pathway for the processing of the prolipoprotein signal peptide in Escherichia coli." J Biol Chem 260(20);10961-5. PMID: 2993296

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hayashi90a: Hayashi S, Wu HC (1990). "Lipoproteins in bacteria." J Bioenerg Biomembr 22(3);451-71. PMID: 2202727

Innis84: Innis MA, Tokunaga M, Williams ME, Loranger JM, Chang SY, Chang S, Wu HC (1984). "Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene." Proc Natl Acad Sci U S A 81(12);3708-12. PMID: 6374664

Inouye83: Inouye S, Franceschini T, Sato M, Itakura K, Inouye M (1983). "Prolipoprotein signal peptidase of Escherichia coli requires a cysteine residue at the cleavage site." EMBO J 2(1);87-91. PMID: 11894915

Isaki90: Isaki L, Kawakami M, Beers R, Hom R, Wu HC (1990). "Cloning and nucleotide sequence of the Enterobacter aerogenes signal peptidase II (lsp) gene." J Bacteriol 172(1);469-72. PMID: 2403548

Isaki90a: Isaki L, Beers R, Wu HC (1990). "Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes." J Bacteriol 172(11);6512-7. PMID: 2121716

Kamio85: Kamio Y, Lin CK, Regue M, Wu HC (1985). "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon." J Biol Chem 260(9);5616-20. PMID: 2985604

Kosic93: Kosic N, Sugai M, Fan CK, Wu HC (1993). "Processing of lipid-modified prolipoprotein requires energy and sec gene products in vivo." J Bacteriol 175(19);6113-7. PMID: 8407783

Krishnabhakdi88: Krishnabhakdi SS, Muller M (1988). "Processing by inverted plasma membrane vesicles of in vitro synthesized major lipoprotein from Escherichia coli." FEBS Lett 231(1);99-101. PMID: 3282924

Miller87: Miller KW, Wu HC (1987). "Cotranscription of the Escherichia coli isoleucyl-tRNA synthetase (ileS) and prolipoprotein signal peptidase (lsp) genes. Fine-structure mapping of the lsp internal promoter." J Biol Chem 262(1);389-93. PMID: 2432063

Miller87a: Miller KW, Bouvier J, Stragier P, Wu HC (1987). "Identification of the genes in the Escherichia coli ileS-lsp operon. Analysis of multiple polycistronic mRNAs made in vivo." J Biol Chem 262(15);7391-7. PMID: 3294831

Munoa91: Munoa FJ, Miller KW, Beers R, Graham M, Wu HC (1991). "Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)." J Biol Chem 266(26);17667-72. PMID: 1894646

Pollitt86: Pollitt S, Inouye S, Inouye M (1986). "Effect of amino acid substitutions at the signal peptide cleavage site of the Escherichia coli major outer membrane lipoprotein." J Biol Chem 261(4);1835-7. PMID: 3511052

Pragai97: Pragai Z, Tjalsma H, Bolhuis A, van Dijl JM, Venema G, Bron S (1997). "The signal peptidase II (Isp) gene of Bacillus subtilis." Microbiology 143 ( Pt 4);1327-33. PMID: 9141696

Regue84: Regue M, Remenick J, Tokunaga M, Mackie GA, Wu HC (1984). "Mapping of the lipoprotein signal peptidase gene (lsp)." J Bacteriol 158(2);632-5. PMID: 6373724

Sakka87: Sakka K, Watanabe T, Beers R, Wu HC (1987). "Isolation and characterization of a new globomycin-resistant dnaE mutant of Escherichia coli." J Bacteriol 169(8);3400-8. PMID: 3112119

Sankaran94: Sankaran K, Wu HC (1994). "Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol." J Biol Chem 269(31);19701-6. PMID: 8051048

Sankaran95: Sankaran K, Wu HC (1995). "Bacterial prolipoprotein signal peptidase." Methods Enzymol 248;169-80. PMID: 7674920

Tokunaga82: Tokunaga M, Loranger JM, Wolfe PB, Wu HC (1982). "Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase." J Biol Chem 257(17);9922-5. PMID: 7050113

Tokunaga83: Tokunaga M, Loranger JM, Wu HC (1983). "Isolation and characterization of an Escherichia coli clone overproducing prolipoprotein signal peptidase." J Biol Chem 258(20);12102-5. PMID: 6313636

Tokunaga84: Tokunaga M, Loranger JM, Wu HC (1984). "A distinct signal peptidase for prolipoprotein in Escherichia coli." J Cell Biochem 24(2);113-20. PMID: 6373799

Tokunaga84a: Tokunaga M, Loranger JM, Wu HC (1984). "Prolipoprotein modification and processing enzymes in Escherichia coli." J Biol Chem 259(6);3825-30. PMID: 6368552

Tokunaga85: Tokunaga M, Loranger JM, Chang SY, Regue M, Chang S, Wu HC (1985). "Identification of prolipoprotein signal peptidase and genomic organization of the lsp gene in Escherichia coli." J Biol Chem 260(9);5610-5. PMID: 2580835

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Yamada84: Yamada H, Kitagawa M, Kawakami M, Mizushima S (1984). "The gene coding for lipoprotein signal peptidase (lspA) and that for isoleucyl-tRNA synthetase (ileS) constitute a cotranscriptional unit in Escherichia coli." FEBS Lett 171(2);245-8. PMID: 6373377

Yamagata83: Yamagata H, Taguchi N, Daishima K, Mizushima S (1983). "Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli." Mol Gen Genet 192(1-2);10-4. PMID: 6227793

Yamagata83a: Yamagata H, Daishima K, Mizushima S (1983). "Cloning and expression of a gene coding for the prolipoprotein signal peptidase of Escherichia coli." FEBS Lett 158(2);301-4. PMID: 6347715

Yamagata83b: Yamagata H (1983). "Temperature-sensitive prolipoprotein signal peptidase in an Escherichia coli mutant: use of the mutant for an efficient and convenient assay system." J Biochem (Tokyo) 93(6);1509-15. PMID: 6350278

Yu84: Yu F, Yamada H, Daishima K, Mizushima S (1984). "Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli." FEBS Lett 173(1);264-8. PMID: 6378662

Zhao92: Zhao XJ, Wu HC (1992). "Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene." FEBS Lett 299(1);80-4. PMID: 1544479

Other References Related to Gene Regulation

Bouvier91: Bouvier J, Stragier P (1991). "Nucleotide sequence of the lsp-dapB interval in Escherichia coli." Nucleic Acids Res 19(1);180. PMID: 2011499

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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