V6V146 · V6V146_CORUL

Function

function

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

166850100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site203-210ATP (UniProtKB | ChEBI)
Binding site424Zn2+ (UniProtKB | ChEBI); catalytic
Active site425
Binding site428Zn2+ (UniProtKB | ChEBI); catalytic
Binding site500Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcell division
Biological Processprotein catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent zinc metalloprotease FtsH
  • EC number

Gene names

    • Name
      ftsH
    • ORF names
      D881_11070

Organism names

Accessions

  • Primary accession
    V6V146

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane6-25Helical
Transmembrane112-134Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain195-334AAA+ ATPase
Region618-668Disordered
Compositional bias652-668Basic and acidic residues

Sequence similarities

Belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    668
  • Mass (Da)
    74,002
  • Last updated
    2014-02-19 v1
  • Checksum
    780A7D7D75877DE6
MNKKILQYSVIAAIVLMAIYVFTLLGNDARGYKQVDTSVAIAQLDKKNVKEVQIDDREQRIRIKLKNAIDHEGREVSEILARYPARTSPEIFSKVEKSEAEKYSTNVNKENFLVSMLGYILPMLIVFGLIMWMFSRMQGNSMFGFGGSRAKELNKDMPTNTFADVAGAEEAVDELHEIKDFLEDPSRYEQLGAKIPRGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFKQARENSPCIIFIDEIDAVGRQRGSGMGGGHDEREQTLNQMLVEMDGFGDREGVIIMAATNRPDILDPALLRPGRFDRQIPVSNPDLKGREQILRVHAKGKPFAPDADIESLARRTAGMSGADLANVLNEAALLTARIGKTVITADALEEATDRVVGGPRRSKVISEKEKKVTAYHEGGHTLAAWALKNIERVYKVTILARGRTGGHAMTAQEDDKGMYNRDELYARLVFAMGGRAAEELVFGEPTTGASADIEQATKIAKAMITEYGMSPTLGMVKYGEEQGDPFARGGSGGVLEYSPEVAAQIDREMQYLLDRAHTEAYMILAEYRDYLDRLAEKLLEKETLRRPDLEELFQGIVPREVGDVFPDEDARFPRQAGREPVKTPTELAIERGEEPPKPFTLLDASKAERARRQSERADRV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias652-668Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AYUJ01000010
EMBL· GenBank· DDBJ
ESU57233.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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