Reviewed, UniProtKB/Swiss-Prot P00803 (LEP_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Molecular function	Hydrolase Protease
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type peptidase activity Inferred from electronic annotation. Source: InterPro
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

Probable

Topological domain

23 – 58

36

Cytoplasmic Probable

Transmembrane

59 – 77

19

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

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

Helix

317 – 319

3

Sequences

	Sequence		Length	Mass (Da)
	P00803-1 [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: 6311837] [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: 9278503] [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: 16738553] [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: 16453726] [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: 2202591] [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: 1618816] [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: 1546969] [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: 8394311] [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: 2551889] [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: 15919996] [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: 9823901] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 77-324.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_003154.1.
NP_417063.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00803. 1 interaction.

Protein family/group databases

MEROPS

S26.001.

Genome annotation databases

GeneID

947040.

GenomeReviews

Gene locus JW2552 in contig AP009048_GR.
Gene locus b2568 in contig U00096_GR.

KEGG

ecj:JW2552.
eco:b2568.

Organism-specific databases

EchoBASE

EB0525.

EcoGene

EG10530. lepB.

CMR

Search...

Phylogenomic databases

HOGENOM

P00803.

OMA

P00803. VAVFKYP.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10530-MON.

BRENDA

3.4.21.89. 246.

Family and domain databases

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_cons-reg.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR019533. Peptidase_S26_cons-reg.
[Graphical view]

Gene3D

G3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit.

Pfam

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

PRINTS

PR00727. LEADERPTASE.

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...

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:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)