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Protein

Signal peptidase I

Gene

lepB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei911
Active sitei1461

GO - Molecular functioni

  • endopeptidase activity Source: EcoCyc
  • peptidase activity Source: EcoliWiki
  • serine-type endopeptidase activity Source: EcoCyc
  • toxic substance binding Source: EcoliWiki

GO - Biological processi

  • protein processing Source: EcoliWiki
  • proteolysis Source: EcoliWiki
  • signal peptide processing Source: EcoCyc

Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

BioCyciEcoCyc:EG10530-MONOMER
MetaCyc:EG10530-MONOMER
BRENDAi3.4.21.89 2026
SABIO-RKiP00803

Protein family/group databases

MEROPSiS26.001

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptidase I (EC:3.4.21.89)
Short name:
SPase I
Alternative name(s):
Leader peptidase I
Gene namesi
Name:lepB
Ordered Locus Names:b2568, JW2552
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10530 lepB

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 3PeriplasmicCurated3
Transmembranei4 – 22HelicalCuratedAdd BLAST19
Topological domaini23 – 58CytoplasmicCuratedAdd BLAST36
Transmembranei59 – 77HelicalCuratedAdd BLAST19
Topological domaini78 – 324PeriplasmicCuratedAdd BLAST247

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoliWiki

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi62E → V: Indifferent. 1
Mutagenesisi78R → E, N or L: Indifferent. 1
Mutagenesisi91S → A: Loss of activity. 1
Mutagenesisi125H → N: Indifferent. 1
Mutagenesisi128R → Q: Small effect. 1
Mutagenesisi130D → A: Indifferent. 1
Mutagenesisi144Y → F: Indifferent. 1
Mutagenesisi146K → M, D, G or S: Loss of activity. 1
Mutagenesisi147R → Q: Small effect. 1
Mutagenesisi154D → A: Loss of activity. 1
Mutagenesisi154D → N: Indifferent. 1
Mutagenesisi159D → N: Small effect. 1
Mutagenesisi171C → A: Indifferent. 1
Mutagenesisi177C → A: Indifferent. 1
Mutagenesisi236H → N: Indifferent. 1
Mutagenesisi269Y → F: Indifferent. 1
Mutagenesisi274D → A: Indifferent. 1
Mutagenesisi276R → Q: Small effect. 1
Mutagenesisi281D → A: Indifferent. 1
Mutagenesisi283R → Q: Small effect. 1

Chemistry databases

ChEMBLiCHEMBL4470

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001095061 – 324Signal peptidase IAdd BLAST324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Blocked amino end (Met)1 Publication1
Disulfide bondi171 ↔ 177

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP00803
PRIDEiP00803

Interactioni

Protein-protein interaction databases

BioGridi4259467112 interactors.
STRINGi316385.ECDH10B_2736

Chemistry databases

BindingDBiP00803

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi82 – 86Combined sources5
Turni91 – 95Combined sources5
Beta strandi100 – 112Combined sources13
Helixi114 – 116Combined sources3
Beta strandi119 – 123Combined sources5
Beta strandi131 – 135Combined sources5
Beta strandi142 – 150Combined sources9
Beta strandi155 – 159Combined sources5
Turni160 – 163Combined sources4
Beta strandi164 – 168Combined sources5
Beta strandi174 – 176Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi189 – 198Combined sources10
Helixi200 – 202Combined sources3
Beta strandi205 – 211Combined sources7
Beta strandi214 – 216Combined sources3
Beta strandi221 – 231Combined sources11
Beta strandi234 – 240Combined sources7
Helixi248 – 250Combined sources3
Beta strandi261 – 263Combined sources3
Beta strandi268 – 272Combined sources5
Helixi282 – 285Combined sources4
Helixi290 – 292Combined sources3
Beta strandi293 – 304Combined sources12
Beta strandi310 – 312Combined sources3
Beta strandi313 – 315Combined sources3
Helixi317 – 319Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B12X-ray1.95A/B/C/D77-324[»]
1KN9X-ray2.40A/B/C/D77-324[»]
1T7DX-ray2.47A/B76-324[»]
3IIQX-ray2.00A/B77-324[»]
3S04X-ray2.44A/B76-324[»]
ProteinModelPortaliP00803
SMRiP00803
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00803

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C3F Bacteria
COG0681 LUCA
HOGENOMiHOG000003674
InParanoidiP00803
KOiK03100
OMAiGDMLFVK
PhylomeDBiP00803

Family and domain databases

InterProiView protein in InterPro
IPR036286 LexA/Signal_pep-like_sf
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
IPR015927 Peptidase_S24_S26A/B/C
IPR019533 Peptidase_S26
PfamiView protein in Pfam
PF00717 Peptidase_S24, 1 hit
PF10502 Peptidase_S26, 1 hit
PRINTSiPR00727 LEADERPTASE
SUPFAMiSSF51306 SSF51306, 1 hit
TIGRFAMsiTIGR02227 sigpep_I_bact, 1 hit
PROSITEiView protein in PROSITE
PS00501 SPASE_I_1, 1 hit
PS00760 SPASE_I_2, 1 hit
PS00761 SPASE_I_3, 1 hit

Sequencei

Sequence statusi: Complete.

P00803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT
60 70 80 90 100
LKKVAPKPGW LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD
110 120 130 140 150
FILVEKFAYG IKDPIYQKTL IETGHPKRGD IVVFKYPEDP KLDYIKRAVG
160 170 180 190 200
LPGDKVTYDP VSKELTIQPG CSSGQACENA LPVTYSNVEP SDFVQTFSRR
210 220 230 240 250
NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT VPIAQDQVGM
260 270 280 290 300
YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI
310 320
WMSFDKQEGE WPTGLRLSRI GGIH
Length:324
Mass (Da):35,960
Last modified:November 1, 1997 - v2
Checksum:i9419710D7212E660
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42 – 43AG → R (PubMed:6311837).Curated2
Sequence conflicti42 – 43AG → R (Ref. 2) Curated2
Sequence conflicti123T → N (PubMed:6311837).Curated1
Sequence conflicti123T → N (Ref. 2) Curated1
Sequence conflicti183V → A (PubMed:6311837).Curated1
Sequence conflicti183V → A (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00426 Genomic DNA Translation: AAA24064.1
D64044 Genomic DNA Translation: BAA10915.1
U00096 Genomic DNA Translation: AAC75621.1
AP009048 Genomic DNA Translation: BAE76744.1
PIRiG65034 ZPECS
RefSeqiNP_417063.1, NC_000913.3
WP_000002541.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75621; AAC75621; b2568
BAE76744; BAE76744; BAE76744
GeneIDi947040
KEGGiecj:JW2552
eco:b2568
PATRICifig|1411691.4.peg.4166

Similar proteinsi

Entry informationi

Entry nameiLEP_ECOLI
AccessioniPrimary (citable) accession number: P00803
Secondary accession number(s): P78098, Q2MAG2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 165 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome