Q4WYP6 · SPFA_ASPFU

Function

function

Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum (By similarity).
Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (By similarity).
Works in concert with the ER Ca2+ pump srcA to support ER homeostasis (PubMed:34663092).
With srcA, supports also redox homeostasis and virulence (PubMed:34663092).

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

The ATPase activity is stimulated by phosphatidylinositol 4-phosphate (PI4P).

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site5054-aspartylphosphate intermediate
Binding site505Mg2+ (UniProtKB | ChEBI)
Binding site505-507ATP (UniProtKB | ChEBI)
Binding site507Mg2+ (UniProtKB | ChEBI)
Binding site616ATP (UniProtKB | ChEBI)
Binding site678ATP (UniProtKB | ChEBI)
Binding site746ATP (UniProtKB | ChEBI)
Binding site862Mg2+ (UniProtKB | ChEBI)
Binding site862-866ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcis-Golgi network
Cellular Componentendoplasmic reticulum membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATPase-coupled monoatomic cation transmembrane transporter activity
Molecular Functionmembrane protein dislocase activity
Molecular Functionmetal ion binding
Molecular FunctionP-type ion transporter activity
Molecular Functionphosphatidylinositol-4-phosphate binding
Biological Processextraction of mislocalized protein from ER membrane
Biological Processintracellular calcium ion homeostasis
Biological Processintracellular manganese ion homeostasis
Biological Processprotein hexamerization
Biological Processprotein unfolding
Biological Processresponse to unfolded protein
Biological Processsterol homeostasis
Biological Processtransmembrane transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endoplasmic reticulum transmembrane helix translocase spfA
  • EC number

Gene names

    • Name
      spfA
    • ORF names
      AFUA_3G13790

Organism names

Accessions

  • Primary accession
    Q4WYP6

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane25-45Helical
Transmembrane57-77Helical
Transmembrane201-221Helical
Transmembrane223-243Helical
Transmembrane415-435Helical
Transmembrane1060-1080Helical
Transmembrane1082-1102Helical
Transmembrane1122-1142Helical
Transmembrane1201-1221Helical
Transmembrane1239-1259Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Induces acute ER stress.

Miscellaneous

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004568861-1303Endoplasmic reticulum transmembrane helix translocase spfA
Glycosylation287N-linked (GlcNAc...) asparagine
Glycosylation474N-linked (GlcNAc...) asparagine
Glycosylation589N-linked (GlcNAc...) asparagine
Glycosylation734N-linked (GlcNAc...) asparagine
Glycosylation958N-linked (GlcNAc...) asparagine

Keywords

Expression

Induction

Expression is induced by ER stress in a UPR-dependent manner (PubMed:34663092).
Leads to the down-regulation of genes largely associated with the metabolism of carbohydrates, amino acids, nitrogen, and sulfur; as well as genes that encode abundantly secreted proteins (PubMed:34663092).

Interaction

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region158-191A-domain; part 1
Region256-408A-domain; part 2
Region484-513P-domain; part 1
Region515-721N-domain
Region724-883P-domain; part 2
Region884-1019Arm-like
Region1020-1035P-domain; part 3
Region1277-1303Disordered

Domain

Contains a large substrate-binding pocket that recognizes alpha-helical transmembranes, which alternately faces the endoplasmic reticulum lumen and cytosol, while remaining accessible to the lipid bilayer through a lateral opening (By similarity).
The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states (By similarity).
Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (By similarity).
A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation (By similarity).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,303
  • Mass (Da)
    145,555
  • Last updated
    2005-07-05 v1
  • Checksum
    6B8B5E48DFDE9268
MLRAKLVDDPQIKYASLHNPLPTQLHAYVWPFLIIWPAFFAVYLSPERYDTYIQGQEWTFVWSGSIITAQSLLWLMTKWNINIQTLFTATKARSLDSAQLIKVIPVANAGSAEICPLHCDTMGGKKTFSFLFQKRRFLYYPERQCFAPLSYVLDAEPKPPVKVFQQAQGLTSKEEIDRIQHHYGDNTFDIPVPTFMELFKEHAVAPFFVFQVFCVGLWMLDEYWYYSLFTLFMLVVFESTVVWQRQRTLNEFRGMNIKPYDVWVYRQKKWQELTSDKLLPGDLMSVNRTKEDSGVACDILLIEGSAIVNEAMLSGESTPLLKESIQLRPGDDLIDPDGLDKNAFVHGGTKVLQITHHNSNGEDGSEKARKLSSGVPLPPDNGAVGVVVKTGFETSQGSLVRTMIYSTERVSANNVEALLFILFLLIFAIAAAWYVWQEGVAKDRKRSKLLLDCVLIVTSVVPPELPMELSLAVNTSLAALSKFAIFCTEPFRIPFAGRVDVACFDKTGTLTGEDLVVDGIAGLTLGHEGADVGKDGAHTELAKSANVPLDTTLVLASAHALVKLDEGEVVGDPMEKATLQWLGWTLGRNDTLMSKAAALAGPRTVESVQIKRRFQFSSALKRQSTIATVVTADRKTSKKTKATFVGVKGAPETIRTMLVNTPPHYEETFKYFTRNGARVLALAYKYLSEESELSQGRINGYIREEIEADLIFAGFLVLQCPLKEDAIKAVRMLNESSHRVVMITGDNPLTAVHVARKVEIVDRDVLILDAPEDDMSGTRLVWRSIDDKFNRDVDPTQDLDPEIIETKDICITGYALAKFKGQKAFSTLLRHTWVYARVSPKQKEDILVGLKDAGYTTLMCGDGTNDVGALKQAHVGVALLNGSPEDLAKIAEHYRTTKMKEIYEKQVSMMQRFNQPPPPVPVQIAHLYPPGPRNPHYQKAMEREAQRKGAATLATAGNQTEHIPTITSPGAQALQQSNANLTPQQQRQQQASIAAAGFADKLTSSMLEQELDDSEPPTIKLGDASVAAPFTSKLANVIAIPNILRQGRCTLVATIQMYKILALNCLISAYSLSVIYLDGIKFGDGQVTISGMLMSVCFLSISRAKSVEGLSKERPQPNIFNVYIIGSVLGQFAIHIATLIYLSNYVYSIEPRKSDIDLEGEFEPSLLNSAIYLLQLIQQISTFSINYQGRPFRESIRENKAMYWGLVAASGVAFSCATEFIPELNEKMRLVPFSTEFKVTLTVLMIIDYAGCWIIENVLKNLFSDFRPKDIAVRRPDQLQREMERKKQEELETQAEKERQRKV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHF01000002
EMBL· GenBank· DDBJ
EAL92207.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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