A0A365PCS2 · A0A365PCS2_9ACTN
- ProteinProtein translocase subunit SecA
- GenesecA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids925 (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
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 | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Dietziaceae > Dietzia
Accessions
- Primary accessionA0A365PCS2
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, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-614 | SecA family profile | ||||
Sequence: MSILSKLLRAGEGRKLKKYTALADYVDTLADETEKLSDDELRAKTDEFRRRVADGETLDELLPEAFAVAREAAHRVLGQKPYKVQIIGAIVLHTGSVAEMKTGEGKTLTCVLPAYLNALAGNGVHVVTVNDYLAKRDAEWMGRVHRFLGLSVGAILGGMTPAQRREAYHADITYGTNNEFGFDYLRDNMAHDTADLVQRGHNYAIVDEVDSILIDEARTPLIISGPADGSSKWYGEFARIAPLLEEGTHYEVDRKKRTIGVTEQGVEFVEDQLGIDNLYEAANSPLVSYLNNSIKAKELFTKDKDYIVRDGDVIIVDEFTGRVLDGRRYNEGMHQAIEAKERVEIKAENQTLATITLQNYFRLYDKLAGMTGTAETEAAELYSIYKLEVMPIPTNRPMAREDQADLIYKTEEAKFAAVVEDIAERVEKKQPVLVGTASVERSEHLSKLLTRKGIKHHVLNAKFHASEAQIIAQAGRPGAVTVATNMAGRGTDIVLGGNADIIADLNLRERGLDPVTTPEEYEQAWDTEIERMRTLTKEEAERVRQAGGLYVLGTERHDSRRIDNQLRGRSGRQGDPGESRFYLSLGDELMRRFNGAAVEAIMNRLSLPDDVPIE | ||||||
Domain | 87-245 | Helicase ATP-binding | ||||
Sequence: IGAIVLHTGSVAEMKTGEGKTLTCVLPAYLNALAGNGVHVVTVNDYLAKRDAEWMGRVHRFLGLSVGAILGGMTPAQRREAYHADITYGTNNEFGFDYLRDNMAHDTADLVQRGHNYAIVDEVDSILIDEARTPLIISGPADGSSKWYGEFARIAPLLE | ||||||
Domain | 418-619 | Helicase C-terminal | ||||
Sequence: VVEDIAERVEKKQPVLVGTASVERSEHLSKLLTRKGIKHHVLNAKFHASEAQIIAQAGRPGAVTVATNMAGRGTDIVLGGNADIIADLNLRERGLDPVTTPEEYEQAWDTEIERMRTLTKEEAERVRQAGGLYVLGTERHDSRRIDNQLRGRSGRQGDPGESRFYLSLGDELMRRFNGAAVEAIMNRLSLPDDVPIEAGMVS | ||||||
Region | 872-925 | Disordered | ||||
Sequence: ADQMQFSGPSESGDPELVDEGASANRAERRSQERQQRAERRERAAKAATRGRRD | ||||||
Compositional bias | 892-925 | Basic and acidic residues | ||||
Sequence: GASANRAERRSQERQQRAERRERAAKAATRGRRD |
Sequence similarities
Belongs to the SecA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length925
- Mass (Da)103,354
- Last updated2018-11-07 v1
- ChecksumE7A25365C3A8C818
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 892-925 | Basic and acidic residues | ||||
Sequence: GASANRAERRSQERQQRAERRERAAKAATRGRRD |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QNTT01000005 EMBL· GenBank· DDBJ | RBA39467.1 EMBL· GenBank· DDBJ | Genomic DNA |