B4SU57 · SECA_SALNS

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.

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 )

Note: May bind 1 zinc ion per subunit.

Features

Showing features for binding site.

1901100200300400500600700800900
TypeIDPosition(s)Description
Binding site87ATP (UniProtKB | ChEBI)
Binding site105-109ATP (UniProtKB | ChEBI)
Binding site512ATP (UniProtKB | ChEBI)
Binding site885Zn2+ (UniProtKB | ChEBI)
Binding site887Zn2+ (UniProtKB | ChEBI)
Binding site896Zn2+ (UniProtKB | ChEBI)
Binding site897Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein-exporting ATPase activity
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
    • Ordered locus names
      SNSL254_A0148

Organism names

Accessions

  • Primary accession
    B4SU57

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001450581-901Protein translocase subunit SecA

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.

Structure

Family & Domains

Sequence similarities

Belongs to the SecA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    901
  • Mass (Da)
    101,826
  • Last updated
    2008-09-23 v1
  • Checksum
    2B7A2062EB922466
MLIKLLTKVFGSRNDRTLRRMRKAVSLINAMEPEMEKLSDDELKAKTNEFRARIEKGESVESLIPEAFAVVREASKRVFGMRHFDVQLLGGMVLNDRCIAEMRTGEGKTLTATLPAYLNALSGKGVHVVTVNDYLAQRDAENNRPLFEFLGMSVGINLPGMPAPAKREAYAADITYGTNNEYGFDYLRDNMAFSPEERVQRKLHYALVDEVDSILIDEARTPLIISGPAEDSSEMYKKVNKIIPHLIRQEKEDSDTFQGEGHFSVDEKARQVNLTERGLVLIEELLVQEGIMDEGESLYSPGNIMLMHHVTAALRAHALFTRDVDYIVKDGEVIIVDEHTGRTMQGRRWSDGLHQAVEAKEGVEIQNENQTLASITFQNYFRLYEKLAGMTGTADTEAFEFSSIYKLDTVVVPTNRPMIRKDLPDLVYMTEAEKIQAIIEDIKERTANGQPVLVGTISIEKSEVVSRELTKAGIKHNVLNAKFHANEAGIVAQAGYPAAVTIATNMAGRGTDIMLGGSWQAEVAALEAPTEEQIAQIKADWQVRHDAVLAAGGLHIIGTERHESRRIDNQLRGRSGRQGDPGSSRFYLSMEDALMRIFASDRVSGMMRKLGMKPGEAIEHPWVTKAIANAQRKVESRNFDIRKQLLEYDDVANDQRRAIYTQRNELLDVSDVSDTINSIREDVFKATIDAYIPPQSLEEMWDIPGLQERLKNDFDLEMPIAEWLDKEPELHEETLRERILAQSIEVYQRKEEVVGAEMMRHFEKGVMLQTLDSLWKEHLAAMDYLRQGIHLRGYAQKDPKQEYKRESFAMFAAMLESLKYEVISTLSKVQVRMPEEVEAMEMQRREEAERLAQMQQLSHQDDDAAVAADLAAQTGERKIGRNDPCPCGSGKKYKQCHGRLS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001113
EMBL· GenBank· DDBJ
ACF61968.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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