degP: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

DegP

Synonyms

serine endoprotease (protease Do), membrane-associated[1], B0161[2][1], Ptd[2][1], protease Do[2][1], HtrA[2][1] , ECK0160, htrA, JW0157, ptd, b0161

Product description

DegP[2][3];

Component of serine protease Do[3]

Periplasmic, membrane-associated serine endoprotease; protease Do, required for high-temperature growth and the degradation of damaged 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:0030288

outer membrane-bounded periplasmic space

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009003

F

Seeded from EcoCyc (v14.0)

complete

GO:0004252

serine-type endopeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001254

F

Seeded from EcoCyc (v14.0)

complete

GO:0004252

serine-type endopeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001940

F

Seeded from EcoCyc (v14.0)

complete

GO:0004252

serine-type endopeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011782

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001478

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:10600391[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001254

P

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001940

P

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011782

P

Seeded from EcoCyc (v14.0)

complete

GO:0006950

response to stress

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0346

P

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:10600391[5]

IDA: Inferred from Direct Assay

F

Forms a dodecameric structure consisting of 2 hexameric rings.

complete

GO:0006979

response to oxidative stress

PMID:10517331[6]

IEP: Inferred from Expression Pattern

P

complete

GO:0030288

outer membrane-bounded periplasmic space

PMID:10517331[6]

IDA: Inferred from Direct Assay

C

complete

GO:0006508

proteolysis

PMID:2180903[7]

IDA: Inferred from Direct Assay

P

complete

GO:0004252

serine-type endopeptidase activity

PMID:2180903[7]

IDA: Inferred from Direct Assay

F

complete

GO:0004252

serine-type endopeptidase activity

PMID:19255437[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0006515

misfolded or incompletely synthesized protein catabolic process

PMID:10319814[9]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0009266

response to temperature stimulus

PMID:10319814[9]

IEP: Inferred from Expression Pattern

P

complete

GO:0006457

protein folding

PMID:10319814[9]

IMP: Inferred from Mutant Phenotype

P

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

Protein

Subunits of serine protease Do

could be indirect

Protein

dnaK

PMID:16606699[10]

Experiment(s):EBI-1135751
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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

periplasm

From EcoCyc[3]

Periplasm

PMID:2180903[7]

EchoLocation:degP


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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 

MKKTTLALSA LALSLGLALS PLSATAAETS SATTAQQMPS LAPMLEKVMP SVVSINVEGS
TTVNTPRMPR NFQQFFGDDS PFCQEGSPFQ SSPFCQGGQG GNGGGQQQKF MALGSGVIID
ADKGYVVTNN HVVDNATVIK VQLSDGRKFD AKMVGKDPRS DIALIQIQNP KNLTAIKMAD
SDALRVGDYT VAIGNPFGLG ETVTSGIVSA LGRSGLNAEN YENFIQTDAA INRGNSGGAL
VNLNGELIGI NTAILAPDGG NIGIGFAIPS NMVKNLTSQM VEYGQVKRGE LGIMGTELNS
ELAKAMKVDA QRGAFVSQVL PNSSAAKAGI KAGDVITSLN GKPISSFAAL RAQVGTMPVG
SKLTLGLLRD GKQVNVNLEL QQSSQNQVDS SSIFNGIEGA EMSNKGKDQG VVVNNVKTGT
PAAQIGLKKG DVIIGANQQA VKNIAELRKV LDSKPSVLAL NIQRGDSTIY LLMQ
Length

474

Mol. Wt

49.354 kDa

pI

8.8 (calculated)

Extinction coefficient

7,450 - 7,700 (calc based on 5 Y, 0 W, and 2 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

motif

1-26

UniProt Manual:Signal Peptides

UniProt:P0C0V0

Domain

87..277

PF00089 Trypsin

PMID:19920124[11]

Domain

279..368

PF00595 PDZ domain (Also known as DHR or GLGF)

PMID:19920124[11]

Domain

385..463

PF00595 PDZ domain (Also known as DHR or GLGF)

PMID:19920124[11]

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

Structures

<beststructure> gene=degP 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:16128154

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947139

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000551

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0C0V0

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10463

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10463

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947139

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000456

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0458

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 1.6 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. ↑ 3.0 3.1 3.2 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 Kim, KI et al. (1999) Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli. J. Mol. Biol. 294 1363-74 PubMed
  6. ↑ 6.0 6.1 Skórko-Glonek, J et al. (1999) The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Mol. Gen. Genet. 262 342-50 PubMed
  7. ↑ 7.0 7.1 7.2 Lipinska, B et al. (1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 172 1791-7 PubMed
  8. ↑ Shen, QT et al. (2009) Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control. Proc. Natl. Acad. Sci. U.S.A. 106 4858-63 PubMed
  9. ↑ 9.0 9.1 9.2 Spiess, C et al. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 339-47 PubMed
  10. ↑ Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  11. ↑ 11.0 11.1 11.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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