lepB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

LepB

Synonyms

leader peptidase (signal peptidase I)[1], B2568[2][1], Lep[2][1], LepB[2][1], LP1[2][1] , ECK2566, JW2552, lep, b2568

Product description

leader peptidase (signal peptidase I)[2][3]

Signal peptidase I; SPI; responsible for type I signal cleavages of periplasmic, OM, some IM, and extracellular proteins[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005886

plasma membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0997

C

Seeded from EcoCyc (v14.0)

complete

GO:0005886

plasma membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-1003

C

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000223

P

Seeded from EcoCyc (v14.0)

complete

GO:0008233

peptidase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0645

F

Seeded from EcoCyc (v14.0)

complete

GO:0008236

serine-type peptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000223

F

Seeded from EcoCyc (v14.0)

complete

GO:0008236

serine-type peptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR019756

F

Seeded from EcoCyc (v14.0)

complete

GO:0008236

serine-type peptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR019757

F

Seeded from EcoCyc (v14.0)

complete

GO:0016485

protein processing

PMID:11511369[5]

IMP: Inferred from Mutant Phenotype

UniProtKB:P17998

P

LepB is required for cleavage and subsequent activation of Colicin D.

complete

GO:0008236

serine-type peptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR019758

F

Seeded from EcoCyc (v14.0)

complete

GO:0015643

toxin binding

PMID:11511369[5]

IMP: Inferred from Mutant Phenotype

UniProtKB:P17998

F

LepB binds and cleaves Colicin D, which activates the colicin.

complete

GO:0015643

toxin binding

PMID:11511369[5]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc (v14.0)

complete

GO:0008233

peptidase activity

PMID:15195997[6]

IDA: Inferred from Direct Assay

F

complete

GO:0015643

toxin binding

PMID:11511369[5]

IMP: Inferred from Mutant Phenotype

UniProtKB:P17998

F

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

PMID:15195997[6]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0016021

integral to membrane

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR019756

C

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

PMID:10891078[7]

IDA: Inferred from Direct Assay

P

complete

GO:0016021

integral to membrane

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR019757

C

Seeded from EcoCyc (v14.0)

complete

GO:0016485

protein processing

PMID:15598653[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0016021

integral to membrane

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR019758

C

Seeded from EcoCyc (v14.0)

complete

GO:0016021

integral to membrane

PMID:10891078[7]

IDA: Inferred from Direct Assay

C

complete

GO:0016021

integral to membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0812

C

Seeded from EcoCyc (v14.0)

complete

GO:0005886

plasma membrane

PMID:10891078[7]

IDA: Inferred from Direct Assay

C

complete

GO:0016021

integral to membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-9909

C

Seeded from EcoCyc (v14.0)

complete

GO:0008233

peptidase activity

PMID:15598653[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0016485

protein processing

PMID:11511369[5]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0016485

protein processing

PMID:11511369[5]

IMP: Inferred from Mutant Phenotype

UniProtKB:P17998

P

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

plasma membrane

C-terminus localized to the periplasm with 2 predicted transmembrane domains

Daley et al. (2005) [9]

plasma membrane


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT LKKVAPKPGW
LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPIYQKTL
IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKVTYDP VSKELTIQPG CSSGQACENA
LPVTYSNVEP SDFVQTFSRR NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT
VPIAQDQVGM YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI
WMSFDKQEGE WPTGLRLSRI GGIH
Length

324

Mol. Wt

35.96 kDa

pI

7.4 (calculated)

Extinction coefficient

49,390 - 49,765 (calc based on 11 Y, 6 W, and 3 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

86..170

PF00717 Peptidase S24-like

PMID:19920124[10]

Domain

233..302

PF10502 Peptidase S26

PMID:19920124[10]

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<motif_map/>

tmhmm.php?gene=lepB&show=pic&.jpg
Click the image to view raw output from TMHMM.

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=lepB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130493

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947040

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0008450

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P00803

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10530

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10530

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947040

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000523

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0525

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 de Zamaroczy, M et al. (2001) Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB. Mol. Cell 8 159-68 PubMed
  6. ↑ 6.0 6.1 Kim, YT et al. (2004) Identification of arginine residues important for the activity of Escherichia coli signal peptidase I. Biol. Chem. 385 381-8 PubMed
  7. ↑ 7.0 7.1 7.2 Stein, RL et al. (2000) Kinetic and mechanistic studies of signal peptidase I from Escherichia coli. Biochemistry 39 7973-83 PubMed
  8. ↑ 8.0 8.1 Karla, A et al. (2005) The identification of residues that control signal peptidase cleavage fidelity and substrate specificity. J. Biol. Chem. 280 6731-41 PubMed
  9. ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed
  10. ↑ 10.0 10.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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