V1H3V0 · V1H3V0_SALER

Function

function

Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.

Caution

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

Catalytic activity

  • ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
    EC:7.4.2.8 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for binding site.

1901100200300400500600700800900
TypeIDPosition(s)Description
Binding site87ATP (UniProtKB | ChEBI)
Binding site105-109ATP (UniProtKB | ChEBI)
Binding site512ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Biological Processintracellular protein transmembrane transport
Biological Processprotein import
Biological Processprotein targeting

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein translocase subunit SecA
  • EC number

Gene names

    • Name
      secA
    • ORF names
      SEI61121_12751

Organism names

Accessions

  • Primary accession
    V1H3V0

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein
Cytoplasm
Note: Distribution is 50-50.

Keywords

Expression

Induction

Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM.

Interaction

Subunit

Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-619SecA family profile
Domain89-247Helicase ATP-binding

Sequence similarities

Belongs to the SecA family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    901
  • Mass (Da)
    101,826
  • Last updated
    2014-01-22 v1
  • Checksum
    2B7A2062EB922466
MLIKLLTKVFGSRNDRTLRRMRKAVSLINAMEPEMEKLSDDELKAKTNEFRARIEKGESVESLIPEAFAVVREASKRVFGMRHFDVQLLGGMVLNDRCIAEMRTGEGKTLTATLPAYLNALSGKGVHVVTVNDYLAQRDAENNRPLFEFLGMSVGINLPGMPAPAKREAYAADITYGTNNEYGFDYLRDNMAFSPEERVQRKLHYALVDEVDSILIDEARTPLIISGPAEDSSEMYKKVNKIIPHLIRQEKEDSDTFQGEGHFSVDEKARQVNLTERGLVLIEELLVQEGIMDEGESLYSPGNIMLMHHVTAALRAHALFTRDVDYIVKDGEVIIVDEHTGRTMQGRRWSDGLHQAVEAKEGVEIQNENQTLASITFQNYFRLYEKLAGMTGTADTEAFEFSSIYKLDTVVVPTNRPMIRKDLPDLVYMTEAEKIQAIIEDIKERTANGQPVLVGTISIEKSEVVSRELTKAGIKHNVLNAKFHANEAGIVAQAGYPAAVTIATNMAGRGTDIMLGGSWQAEVAALEAPTEEQIAQIKADWQVRHDAVLAAGGLHIIGTERHESRRIDNQLRGRSGRQGDPGSSRFYLSMEDALMRIFASDRVSGMMRKLGMKPGEAIEHPWVTKAIANAQRKVESRNFDIRKQLLEYDDVANDQRRAIYTQRNELLDVSDVSDTINSIREDVFKATIDAYIPPQSLEEMWDIPGLQERLKNDFDLEMPIAEWLDKEPELHEETLRERILAQSIEVYQRKEEVVGAEMMRHFEKGVMLQTLDSLWKEHLAAMDYLRQGIHLRGYAQKDPKQEYKRESFAMFAAMLESLKYEVISTLSKVQVRMPEEVEAMEMQRREEAERLAQMQQLSHQDDDAAVAADLAAQTGERKIGRNDPCPCGSGKKYKQCHGRLS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOXI01000024
EMBL· GenBank· DDBJ
ESE84545.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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