Q9ZJS9 · SECY_HELPJ

Function

function

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

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 Componentcell envelope Sec protein transport complex
Cellular Componentplasma membrane
Molecular Functionprotein transmembrane transporter activity
Molecular Functionsignal sequence binding
Biological Processprotein transport by the Sec complex
Biological ProcessSRP-dependent cotranslational protein targeting to membrane, translocation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein translocase subunit SecY

Gene names

    • Name
      secY
    • Ordered locus names
      jhp_1220

Organism names

Accessions

  • Primary accession
    Q9ZJS9

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane9-29Helical
Transmembrane61-81Helical
Transmembrane104-124Helical
Transmembrane141-161Helical
Transmembrane173-193Helical
Transmembrane203-223Helical
Transmembrane257-277Helical
Transmembrane300-320Helical
Transmembrane355-375Helical
Transmembrane377-397Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001317261-420Protein translocase subunit SecY

Interaction

Subunit

Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.

Family & Domains

Sequence similarities

Belongs to the SecY/SEC61-alpha family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    420
  • Mass (Da)
    45,827
  • Last updated
    1999-05-01 v1
  • Checksum
    89074E032E9AB7FF
MNKAIASKILITLGFLFLYRVLAYIPIPGVDLAAIKAFFDSNSNNALGLFNMFSGNAVSRLSIISLGIMPYITSSIIMELLSATFPNLAKMKKERDGMQKYMQIVRYLTILITLIQAVSVSVGLRSISGGANGAIMIDMQVFMIVSAFSMLTGTMLLMWIGEQITQRGVGNGISLIIFAGIVSGIPSAISGTFNLVNTGVINILMLIGIVLIVLATIFAIIYVELAERRIPISYARKVVMQNQNKRIMNYIPIKLNLSGVIPPIFASALLVFPSTILQQATSNKTLQAIADFLSPQGYAYNILMFLLIIFFAYFYSSIVFNSKDIADNLRRNGGYIPGLRPGEGTSSFLNAVASKLTLWGSLYLALISTVPWILVKAMGVPFYFGGTAVLIVVQVAIDTMKKIEAQIYMSKYKTLSAVGF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE001439
EMBL· GenBank· DDBJ
AAD06804.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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