P00803 (LEP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal peptidase I
Short name=SPase I
EC=3.4.21.89

Alternative name(s):
Leader peptidase I

Gene names

Name:	lepB
Ordered Locus Names:	b2568, JW2552

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the peptidase S26 family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein processing Inferred from mutant phenotype PubMed 11511369PubMed 15598653. Source: EcoliWiki proteolysis Inferred from direct assay PubMed 10891078. Source: EcoliWiki
Cellular_component	integral to membrane Inferred from direct assay PubMed 10891078. Source: EcoliWiki plasma membrane Inferred from direct assay PubMed 10891078. Source: EcoliWiki
Molecular_function	peptidase activity Inferred from direct assay PubMed 15195997. Source: EcoliWiki serine-type peptidase activity Inferred from electronic annotation. Source: InterPro toxin binding Inferred from mutant phenotype PubMed 11511369. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 324

324

Signal peptidase I

PRO_0000109506

Regions

Topological domain

1 – 3

3

Periplasmic Probable

Transmembrane

4 – 22

19

Helical; Probable

Topological domain

23 – 58

36

Cytoplasmic Probable

Transmembrane

59 – 77

19

Helical; Probable

Topological domain

78 – 324

247

Periplasmic Probable

Sites

Active site

91

1

Ref.7 Ref.9

Active site

146

1

Ref.7 Ref.9

Amino acid modifications

Modified residue

1

1

Blocked amino end (Met) Ref.1

Disulfide bond

171 ↔ 177

Experimental info

Mutagenesis

62

1

E → V: Indifferent.

Mutagenesis

78

1

R → E, N or L: Indifferent.

Mutagenesis

91

1

S → A: Loss of activity.

Mutagenesis

125

1

H → N: Indifferent.

Mutagenesis

128

1

R → Q: Small effect.

Mutagenesis

130

1

D → A: Indifferent.

Mutagenesis

144

1

Y → F: Indifferent.

Mutagenesis

146

1

K → M, D, G or S: Loss of activity.

Mutagenesis

147

1

R → Q: Small effect.

Mutagenesis

154

1

D → A: Loss of activity.

Mutagenesis

154

1

D → N: Indifferent.

Mutagenesis

159

1

D → N: Small effect.

Mutagenesis

171

1

C → A: Indifferent.

Mutagenesis

177

1

C → A: Indifferent.

Mutagenesis

236

1

H → N: Indifferent.

Mutagenesis

269

1

Y → F: Indifferent.

Mutagenesis

274

1

D → A: Indifferent.

Mutagenesis

276

1

R → Q: Small effect.

Mutagenesis

281

1

D → A: Indifferent.

Mutagenesis

283

1

R → Q: Small effect.

Sequence conflict

42 – 43

2

AG → R Ref.1

Sequence conflict

42 – 43

2

AG → R Ref.2

Sequence conflict

123

1

T → N Ref.1

Sequence conflict

123

1

T → N Ref.2

Sequence conflict

183

1

V → A Ref.1

Sequence conflict

183

1

V → A Ref.2

Secondary structure

1

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324

Helix Strand Turn

Details...

Beta strand

82 – 86

5

Turn

91 – 95

5

Beta strand

100 – 112

13

Helix

114 – 116

3

Beta strand

119 – 123

5

Beta strand

131 – 135

5

Beta strand

142 – 150

9

Beta strand

155 – 159

5

Turn

160 – 163

4

Beta strand

164 – 168

5

Beta strand

183 – 185

3

Beta strand

189 – 198

10

Helix

200 – 202

3

Beta strand

205 – 211

7

Beta strand

214 – 216

3

Beta strand

221 – 231

11

Beta strand

234 – 240

7

Helix

248 – 250

3

Beta strand

261 – 263

3

Beta strand

268 – 272

5

Helix

282 – 285

4

Helix

290 – 292

3

Beta strand

293 – 304

12

Beta strand

308 – 310

3

Beta strand

313 – 315

3

Helix

317 – 319

3

Sequences

	Sequence		Length	Mass (Da)
	P00803 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 9419710D7212E660	FASTA	324	35,960
	10 20 30 40 50 60 MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT LKKVAPKPGW 70 80 90 100 110 120 LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPIYQKTL 130 140 150 160 170 180 IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKVTYDP VSKELTIQPG CSSGQACENA 190 200 210 220 230 240 LPVTYSNVEP SDFVQTFSRR NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT 250 260 270 280 290 300 VPIAQDQVGM YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI 310 320 WMSFDKQEGE WPTGLRLSRI GGIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope." Wolfe P.B., Wickner W., Goodman J.M. J. Biol. Chem. 258:12073-12080(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Nashimoto H., Saito N. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology." von Heijne G. EMBO J. 5:3021-3027(1986) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[6]	"Mapping of catalytically important domains in Escherichia coli leader peptidase." Bilgin N., Lee J.I., Zhu H.Y., Dalbey R., von Heijne G. EMBO J. 9:2717-2722(1990) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[7]	"Identification of potential active-site residues in the Escherichia coli leader peptidase." Sung M., Dalbey R.E. J. Biol. Chem. 267:13154-13159(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS, ACTIVE SITES.
[8]	"On the catalytic mechanism of prokaryotic leader peptidase 1." Black M.T., Munn J.G.R., Allsop A.E. Biochem. J. 282:539-543(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS. Strain: HJM114 and IT41.
[9]	"Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad." Black M.T. J. Bacteriol. 175:4957-4961(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS, ACTIVE SITES.
[10]	"Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase." San Millan J.L., Boyd D., Dalbey R., Wickner W., Beckwith J. J. Bacteriol. 171:5536-5541(1989) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[11]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
[12]	"Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor." Paetzel M., Dalbey R.E., Strynadka N.C. Nature 396:186-190(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 77-324.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K00426 Genomic DNA. Translation: AAA24064.1.
D64044 Genomic DNA. Translation: BAA10915.1.
U00096 Genomic DNA. Translation: AAC75621.1.
AP009048 Genomic DNA. Translation: BAE76744.1.

PIR

ZPECS. G65034.

RefSeq

NP_417063.1. NC_000913.2.
YP_490796.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B12	X-ray	1.95	A/B/C/D	77-324	[»]
1KN9	X-ray	2.40	A/B/C/D	77-324	[»]
1T7D	X-ray	2.47	A/B	76-324	[»]
3IIQ	X-ray	2.00	A/B	77-324	[»]
3S04	X-ray	2.44	A/B	76-324	[»]

ProteinModelPortal

P00803.

SMR

P00803. Positions 78-324.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b2568.

Protein family/group databases

MEROPS

S26.001.

Proteomic databases

PRIDE

P00803.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75621; AAC75621; b2568.
BAE76744; BAE76744; BAE76744.

GeneID

12930473.
947040.

KEGG

ecj:Y75_p2521.
eco:b2568.

PATRIC

32120535. VBIEscCol129921_2670.

Organism-specific databases

EchoBASE

EB0525.

EcoGene

EG10530. lepB.

Phylogenomic databases

eggNOG

COG0681.

HOGENOM

HOG000003674.

KO

K03100.

OMA

ESSHFGD.

ProtClustDB

PRK10861.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10530-MONOMER.
ECOL316407:JW2552-MONOMER.
MetaCyc:EG10530-MONOMER.

BRENDA

3.4.21.89. 2026.

SABIO-RK

P00803.

Gene expression databases

Genevestigator

P00803.

Family and domain databases

Gene3D

2.10.109.10. 2 hits.
2.170.230.10. 1 hit.

InterPro

IPR000223. Pept_S26A_signal_pept_1.
IPR019758. Pept_S26A_signal_pept_1_CS.
IPR019757. Pept_S26A_signal_pept_1_Lys-AS.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR019533. Peptidase_S26.
IPR019766. Peptidase_S26A_all-beta_subdom.
[Graphical view]

PANTHER

PTHR12383. PTHR12383. 1 hit.

Pfam

PF00717. Peptidase_S24. 1 hit.
PF10502. Peptidase_S26. 1 hit.
[Graphical view]

PRINTS

PR00727. LEADERPTASE.

SUPFAM

SSF51306. Pept_S24_S26_C. 1 hit.

TIGRFAMs

TIGR02227. sigpep_I_bact. 1 hit.

PROSITE

PS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4470.

EvolutionaryTrace

P00803.

Entry information

Entry name

LEP_ECOLI

Accession

Primary (citable) accession number: P00803
Secondary accession number(s): P78098, Q2MAG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program