secB: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

SecB

Synonyms

protein export chaperone[1], B3609[2][1], SecB[2][1] , ECK3599, JW3584, b3609

Product description

SecB[2][3];

Component of Sec Protein Secretion Complex[2][3]

Protein export chaperone; SecB helps SecA deliver proteins to the SecYE core translocon; general protein chaperone[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:0005515

protein binding

PMID:2649892[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00821

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0006457

protein folding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00821

P

Seeded from EcoCyc (v14.0)

complete

GO:0051082

unfolded protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003708

F

Seeded from EcoCyc (v14.0)

complete

GO:0051262

protein tetramerization

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003708

P

Seeded from EcoCyc (v14.0)

complete

GO:0006605

protein targeting

PMID:6403503[6]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0015031

protein transport

PMID:6403503[6]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0043952

protein transport by the Sec complex

PMID:6403503[6]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005515

protein binding

PMID:2649892[5]

IDA: Inferred from Direct Assay

F

E. coli SecB is a homotetramer.

complete

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

Protein

Subunits of Sec Protein Secretion Complex

could be indirect

Protein

yaiX

PMID:15690043[7]

Experiment(s):EBI-886253

Protein

ybgK

PMID:16606699[8]

Experiment(s):EBI-1146244

Protein

rpsC

PMID:16606699[8]

Experiment(s):EBI-1146244

Protein

nrdI

PMID:16606699[8]

Experiment(s):EBI-1146244

Protein

motB

PMID:16606699[8]

Experiment(s):EBI-1146244

Protein

lon

PMID:15690043[7]

Experiment(s):EBI-880504, EBI-886253

Protein

cpxR

PMID:15690043[7]

Experiment(s):EBI-886253

Protein

lon

PMID:19402753[9]

LCMS(ID Probability):99.6 MALDI(Z-score):28.283587

Protein

cpxR

PMID:19402753[9]

LCMS(ID Probability):99.2

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Notes

SecB substrates have been examined in a comparative proteomics experiment[10]. Intracellular aggregates of proteins that depend on SecB for secretion were formed in a secB mutant.

Localization

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

Compartment Description Evidence Reference/Source Notes

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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

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL
RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR
GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA
Length

155

Mol. Wt

17.276 kDa

pI

4.1 (calculated)

Extinction coefficient

12,950 - 13,450 (calc based on 5 Y, 1 W, and 4 C residues)


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

Modification Site

22

phosphorylation site at S22

probability greater than 75%

PMID:17938405[11]

Domain

1..146

PF02556 Preprotein translocase subunit SecB

PMID:19920124[12]

<motif_map/>

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

Structures

<beststructure> gene=secB 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:16131480

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948123

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0011798

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AG86

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10937

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10937

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948123

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000926

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0930

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 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 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 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 Watanabe, M & Blobel, G (1989) Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB. Proc. Natl. Acad. Sci. U.S.A. 86 2728-32 PubMed
  6. 6.0 6.1 6.2 Kumamoto, CA & Beckwith, J (1983) Mutations in a new gene, secB, cause defective protein localization in Escherichia coli. J. Bacteriol. 154 253-60 PubMed
  7. 7.0 7.1 7.2 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  8. 8.0 8.1 8.2 8.3 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  9. 9.0 9.1 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  10. Baars, L et al. (2006) Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. J. Biol. Chem. 281 10024-34 PubMed
  11. Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  12. Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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