A0A520W2J9 · A0A520W2J9_9ACTN
- ProteinProtein translocase subunit SecA
- GenesecA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids840 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic activity
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell envelope Sec protein transport complex | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Biological Process | intracellular protein transmembrane transport | |
Biological Process | protein import | |
Biological Process | protein targeting | |
Biological Process | protein transport by the Sec complex |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein translocase subunit SecA
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Candidatus Actinomarinidae > Candidatus Actinomarinales
Accessions
- Primary accessionA0A520W2J9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Note: Distribution is 50-50.
Keywords
- Cellular component
Interaction
Subunit
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-594 | SecA family profile | ||||
Sequence: MVFDKLLTVGSGKLSKELNSIVDLINKLEEEFEGYSDEAIKDGFQSLKEKVEENILLAEVEGFAYVREAAKRKLDQRHFDVQLFGGLVLLRNKIAEMKTGEGKTLVSTLPVSLMALAGRGVHVVTVNDYLAKRDAEWMGPVYEFLGLSVGLIQAGQVLEEKQNAYKADITYGTNNEFGFDYLRDNMTQNVEQLVQRELTFALIDEVDSILVDESRTPLVLSGRVEESTKWYIQFSKIVKGMKKDVHYEIEESKRQIHPTEIGIEYIEKQLGVENLYEETAVNYLHYLTASLRAKELYSRDVEYIVSNGQLNIVDEFTGRVLEGRRYSEGLHQALEAKEGLKVQDENQTLATITFQNFFRLYGRLAGMTGTAKTEEEELIQIYNLEVIEIPTNMEIARIDNEDVIYKTKESKLNAVVDDIKSRVERGQPVLVGTVSVESSEQISSLLTSQGIIHSVLNAKNHEKEALIIAQAGRSGAVTVATNMAGRGVDIKLGGNPDFVGIEEGKDKVQDLDQVTAEKENKKVLDSGGLYVLGTERHESRRIDNQLRGRSGRQGDPGESRFYISLEDELMRRFQGERIQSIMDKLNLPDDERIE | ||||||
Coiled coil | 11-38 | |||||
Sequence: SGKLSKELNSIVDLINKLEEEFEGYSDE | ||||||
Domain | 84-222 | Helicase ATP-binding | ||||
Sequence: FGGLVLLRNKIAEMKTGEGKTLVSTLPVSLMALAGRGVHVVTVNDYLAKRDAEWMGPVYEFLGLSVGLIQAGQVLEEKQNAYKADITYGTNNEFGFDYLRDNMTQNVEQLVQRELTFALIDEVDSILVDESRTPLVLSG | ||||||
Domain | 411-593 | Helicase C-terminal | ||||
Sequence: KLNAVVDDIKSRVERGQPVLVGTVSVESSEQISSLLTSQGIIHSVLNAKNHEKEALIIAQAGRSGAVTVATNMAGRGVDIKLGGNPDFVGIEEGKDKVQDLDQVTAEKENKKVLDSGGLYVLGTERHESRRIDNQLRGRSGRQGDPGESRFYISLEDELMRRFQGERIQSIMDKLNLPDDERI | ||||||
Region | 812-840 | Disordered | ||||
Sequence: KEESINKGPVGRNEPCPCGSGKKYKRCHG |
Sequence similarities
Belongs to the SecA family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length840
- Mass (Da)95,871
- Last updated2019-10-16 v1
- Checksum0B1964D07DD96E27