RegulonDB

RegulonDB RegulonDB 10.8: Gene Form

lspA gene in Escherichia coli K-12 genome

Gene local context to scale (view description)

Gene
Name:	lspA
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
OU-MICROARRAY:	b0027
PortEco:	lspA
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:

ECOCYC:

ECOLIWIKI:

INTERPRO:

PANTHER:

PFAM:

PRIDE:

PRINTS:

PRODB:

PROSITE:

REFSEQ:

SMR:

UNIPROT:

Operon

Name:

ribF-ileS-lspA-fkpB-ispH

Operon arrangement:

Transcription unit	Promoter
ribF-ileS-lspA-fkpB-ispH	ribFp
ileS-lspA-fkpB-ispH	ileSp1
ileS-lspA-fkpB-ispH	ileSp2
ileS-lspA-fkpB-ispH	ileSp3
lsp-fkpB-ispH	lspAp

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

Type	Name	Post Left	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
promoter	TSS_58 (cluster)	21834	forward	For this promoter, there is a cluster of 2 transcription start sites,in the interval 21834 to 21835, where the highest frequency is at position 21835. The most upstream position of this cluster is assigned as TSS position in the promoter. Read more >	[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	For this promoter, there is a cluster of 2 transcription start sites,in the interval 22306 to 22307, where the highest frequency is at position 22306. The most upstream position of this cluster is assigned as TSS position in the promoter. Read more >	[RS-EPT-CBR]	[14]
promoter	TSS_66 (cluster)	22371	forward	For this promoter, there is a cluster of 2 transcription start sites,in the interval 22371 to 22372, where the highest frequency is at position 22371. The most upstream position of this cluster is assigned as TSS position in the promoter. Read more >	[RS-EPT-CBR]	[14]
promoter	TSS_67 (cluster)	23007	forward	For this promoter, there is a cluster of 2 transcription start sites,in the interval 23007 to 23008, where the highest frequency is at position 23007. The most upstream position of this cluster is assigned as TSS position in the promoter. Read more >	[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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