htpX:Gene Product(s)

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
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

HtpX

Synonyms

predicted endopeptidase[1], B1829[2][1], HtpX[2][1]

Product description

heat shock protein, integral membrane protein[2][3]

Zinc metalloprotease HtpX, membrane-bound; cleaves SecY in vivo and in vitro; self-cleaves; M48 family[4]

EC number (for enzymes)


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Notes

Function

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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(s) Evidence Code with/from Aspect Notes Status
GO:0008270

zinc ion binding

PMID:16076848[5] PMID:1826904[6]

IDA: Inferred from Direct Assay

F

complete

GO:0009266

response to temperature stimulus

PMID:1826904[6]

IEP: Inferred from Expression Pattern

P

complete

GO:0005886

plasma membrane

PMID:16076848[5] PMID:1826904[6]

IDA: Inferred from Direct Assay

C

complete

GO:0004222

metalloendopeptidase activity

PMID:16076848[5]

IDA: Inferred from Direct Assay

F

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

HtpX is ATP-independent and introduces endoproteolytic cuts in abnormal membrane proteins

Localization

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

Compartment Description Evidence Source Notes

plasma membrane

C-terminus localized in the cytoplasm with 4 predicted transmembrane domains

Daley et al. (2005) [7]

plasma membrane


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Notes

Structure and Physical Properties

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

Sequence

at EcoCyc 

MMRIALFLLT NLAVMVVFGL VLSLTGIQSS SVQGLMIMAL LFGFGGSFVS LLMSKWMALR
SVGGEVIEQP RNERERWLVN TVATQARQAG IAMPQVAIYH APDINAFATG ARRDASLVAV
STGLLQNMSP DEAEAVIAHE ISHIANGDMV TMTLIQGVVN TFVIFISRIL AQLAAGFMGG
NRDEGEESNG NPLIYFAVAT VLELVFGILA SIITMWFSRH REFHADAGSA KLVGREKMIA
ALQRLKTSYE PQEATSMMAL CINGKSKSLS ELFMTHPPLD KRIEALRTGE YLK
Length

293

Mol. Wt

31.923 kDa

pI

7.1 (calculated)

Extinction coefficient

22,460 - 22,585 (calc based on 4 Y, 3 W, and 1 C residues)

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Domains/Motifs/Modification Sites

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Type Residues Description Notes References
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<motif_map/>

tmhmm.php?gene=htpX&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=htpX taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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

EcoCyc (EcoliWiki Page)

EcoCyc:EG10462-MONOMER

UniProt (EcoliWiki Page)

UniProt:P23894

PFAM (EcoliWiki Page)

PFAM:PF06509

RefSeq (EcoliWiki Page)

RefSeq:NP_416343


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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 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 Sakoh, M et al. (2005) Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli. J. Biol. Chem. 280 33305-10 PubMed
  6. ↑ 6.0 6.1 6.2 Kornitzer, D et al. (1991) Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX. J. Bacteriol. 173 2944-53 PubMed
  7. ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed

Categories

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