RegulonDB RegulonDB 10.10: Gene Form
   

lspA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

Gene      
Name: lspA    Texpresso search in the literature
Synonym(s): ECK0028, EG10548, b0027, lsp
Genome position(nucleotides): 25207 --> 25701 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 53.54
External database links:  
ASAP:
 ABE-0000096
CGSC:
 11326
ECHOBASE:
 EB0543
ECOLIHUB:
 lspA
OU-MICROARRAY:
 b0027
STRING:
 511145.b0027
COLOMBOS: lspA


Product      
Name: lipoprotein signal peptidase
Synonym(s): Lsp, LspA, SPase II, diacylglycerol prolipoprotein signal peptidase, leader peptidase II, premurein-leader peptidase, prolipoprotein signal peptidase, signal peptidase II
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 18.156
Isoelectric point: 8.682
Motif(s):
 
Type Positions Sequence
12 -> 26 WLWLVVVVLIIDLGS
16 -> 154 VVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVILAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLE
96 -> 113 LNNIAYALIIGGALGNLF
142 -> 159 TAICVGAALIVLEGFLPS
70 -> 88 WFFAGIAIGISVILAVMMY

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.5 - export, signal peptide cleavage
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
molecular_function GO:0008233 - peptidase activity
GO:0016787 - hydrolase activity
GO:0004175 - endopeptidase activity
GO:0004190 - aspartic-type endopeptidase activity
biological_process GO:0006508 - proteolysis
GO:0097304 - lipoprotein biosynthetic process via signal peptide cleavage
Note(s): Note(s): ...[more].
Reference(s): [1] Ghrayeb J., et al., 1985
[2] Kosic N., et al., 1993
[3] Krishnabhakdi SS., et al., 1988
[4] Sakka K., et al., 1987
[5] Sankaran K., et al., 1994
[6] Stenberg U., et al., 1983
[7] Tokunaga M., et al., 1982
[8] Tokunaga M., et al., 1983
[9] Tokunaga M., et al., 1982
[10] Yamagata H. 1983
[11] Yamagata H., et al., 1983
[12] Yamagata H., et al., 1982
[13] Zhao XJ., et al., 1992
External database links:  
DIP:
 DIP-10129N
ECOCYC:
 EG10548-MONOMER
ECOLIWIKI:
 b0027
INTERPRO:
 IPR001872
PANTHER:
 PTHR33695
PFAM:
 PF01252
PRIDE:
 P00804
PRINTS:
 PR00781
PRODB:
 PRO_000023127
PROSITE:
 PS00855
REFSEQ:
 NP_414568
UNIPROT:
 P00804


Operon      
Name: ribF-ileS-lspA-fkpB-ispH         
Operon arrangement:
Transcription unit        Promoter
ribF-ileS-lspA-fkpB-ispH
ileS-lspA-fkpB-ispH
ileS-lspA-fkpB-ispH
ileS-lspA-fkpB-ispH
lsp-fkpB-ispH


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_58 (cluster) 21834 forward nd [RS-EPT-CBR] [14]
  promoter TSS_59 22220 forward nd [RS-EPT-CBR] [14]
  promoter TSS_60 22222 forward nd [RS-EPT-CBR] [14]
  promoter TSS_62 22244 forward nd [RS-EPT-CBR] [14]
  promoter TSS_63 22262 forward nd [RS-EPT-CBR] [14]
  promoter TSS_64 22279 forward nd [RS-EPT-CBR] [14]
  promoter TSS_65 (cluster) 22306 forward nd [RS-EPT-CBR] [14]
  promoter TSS_66 (cluster) 22371 forward nd [RS-EPT-CBR] [14]
  promoter TSS_67 (cluster) 23007 forward nd [RS-EPT-CBR] [14]
  promoter TSS_68 23888 forward nd [RS-EPT-CBR] [14]
  promoter TSS_69 24198 forward nd [RS-EPT-CBR] [14]
  promoter TSS_70 24243 forward nd [RS-EPT-CBR] [14]
  promoter TSS_71 24709 forward nd [RS-EPT-CBR] [14]
  promoter TSS_72 24918 forward nd [RS-EPT-CBR] [14]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates


Reference(s)    

 [1] 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

 [2] 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

 [3] 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

 [4] 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

 [5] Sankaran K., Wu HC., 1994, Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol., J Biol Chem 269(31):19701-6

 [6] Stenberg U., Alsberg T., Westerholm R., 1983, Applicability of a cryogradient technique for the enrichment of PAH from automobile exhausts: demonstration of methodology and evaluation experiments., Environ Health Perspect 47:43-51

 [7] 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

 [8] 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

 [9] Tokunaga M., Tokunaga H., Wu HC., 1982, Post-translational modification and processing of Escherichia coli prolipoprotein in vitro., Proc Natl Acad Sci U S A 79(7):2255-9

 [10] 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

 [11] 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

 [12] Yamagata H., Ippolito C., Inukai M., Inouye M., 1982, Temperature-sensitive processing of outer membrane lipoprotein in an Escherichia coli mutant., J Bacteriol 152(3):1163-8

 [13] Zhao XJ., Wu HC., 1992, Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene., FEBS Lett 299(1):80-4

 [14] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

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