C0ZPK5 · FTSH_RHOE4
- ProteinATP-dependent zinc metalloprotease FtsH
- GeneftsH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids854 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent zinc metalloprotease FtsH
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus > Rhodococcus erythropolis group
Accessions
- Primary accessionC0ZPK5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-5 | Cytoplasmic | ||||
Sequence: MNRKT | ||||||
Transmembrane | 6-26 | Helical | ||||
Sequence: VFRNVLLVAVVLLVIYAFSYF | ||||||
Topological domain | 27-112 | Extracellular | ||||
Sequence: SNDTRDFKTVDTSVAISQLDAKNVASAQIDDREQQVRLWLKNGNDATDGKTQILAKYPASASEQIFDKVEGAGADKFNTTVTQESW | ||||||
Transmembrane | 113-133 | Helical | ||||
Sequence: LTSILLFVLPMIILFGIFFFV | ||||||
Topological domain | 134-854 | Cytoplasmic | ||||
Sequence: MNRMQGGGGRGGVMGFGKSKAKQLTKDMPKTTFADVAGADEAVEELYEIKDFLQNPARYQALGAKIPRGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRTGIILIAATNRPDILDPALLRPGRFDRQIPVGAPDLAGRRAILRVHSQGKPIDPNADLEGLAKRTVGMSGADLANVINEAALLTARENGTVITEASLEESVDRVVGGPRRKSRIISEHEKKITAYHEGGHTLAAWAMPDIEPVYKVTILARGRTGGHAMTVPEDDKGLMTRSEMIARLVMAMGGRAAEELVFHEPTTGASSDIDMATKIARAMVTEYGMSAKLGAVRYGQEGGDPFLGRSMGVQSDYSHEIAREIDEEVRNLIEAAHTEAWAILNEYRDALDLIATELLERETLTRKDLEKILAGVEKRPRITAFNDFGGRTPSDRPPVKTPRELAIERGETWPEPAAAPVLVKAGAPNSGVPNGGVPNNGGLPNNGNQGPSNGYAQPSYPQPSAPQQTPQPGTPDYGAPAGWSAPGWPPRENPSPTYPGQQSGGYTGGQNPTPPNQSQGQYGQPQHGQPQPDQGQYGQPHPGQQAYPEQPHPGRRYPAQPDYPVQYPDGGPFADPNRGNPSGENQWQSPTPEQPQTPPPHHSAEDDGPSTARWDGPDGSR |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000400382 | 1-854 | ATP-dependent zinc metalloprotease FtsH | |||
Sequence: MNRKTVFRNVLLVAVVLLVIYAFSYFSNDTRDFKTVDTSVAISQLDAKNVASAQIDDREQQVRLWLKNGNDATDGKTQILAKYPASASEQIFDKVEGAGADKFNTTVTQESWLTSILLFVLPMIILFGIFFFVMNRMQGGGGRGGVMGFGKSKAKQLTKDMPKTTFADVAGADEAVEELYEIKDFLQNPARYQALGAKIPRGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRTGIILIAATNRPDILDPALLRPGRFDRQIPVGAPDLAGRRAILRVHSQGKPIDPNADLEGLAKRTVGMSGADLANVINEAALLTARENGTVITEASLEESVDRVVGGPRRKSRIISEHEKKITAYHEGGHTLAAWAMPDIEPVYKVTILARGRTGGHAMTVPEDDKGLMTRSEMIARLVMAMGGRAAEELVFHEPTTGASSDIDMATKIARAMVTEYGMSAKLGAVRYGQEGGDPFLGRSMGVQSDYSHEIAREIDEEVRNLIEAAHTEAWAILNEYRDALDLIATELLERETLTRKDLEKILAGVEKRPRITAFNDFGGRTPSDRPPVKTPRELAIERGETWPEPAAAPVLVKAGAPNSGVPNGGVPNNGGLPNNGNQGPSNGYAQPSYPQPSAPQQTPQPGTPDYGAPAGWSAPGWPPRENPSPTYPGQQSGGYTGGQNPTPPNQSQGQYGQPQHGQPQPDQGQYGQPHPGQQAYPEQPHPGRRYPAQPDYPVQYPDGGPFADPNRGNPSGENQWQSPTPEQPQTPPPHHSAEDDGPSTARWDGPDGSR |
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 658-854 | Disordered | ||||
Sequence: AGAPNSGVPNGGVPNNGGLPNNGNQGPSNGYAQPSYPQPSAPQQTPQPGTPDYGAPAGWSAPGWPPRENPSPTYPGQQSGGYTGGQNPTPPNQSQGQYGQPQHGQPQPDQGQYGQPHPGQQAYPEQPHPGRRYPAQPDYPVQYPDGGPFADPNRGNPSGENQWQSPTPEQPQTPPPHHSAEDDGPSTARWDGPDGSR | ||||||
Compositional bias | 666-695 | Polar residues | ||||
Sequence: PNGGVPNNGGLPNNGNQGPSNGYAQPSYPQ | ||||||
Compositional bias | 730-776 | Polar residues | ||||
Sequence: TYPGQQSGGYTGGQNPTPPNQSQGQYGQPQHGQPQPDQGQYGQPHPG |
Sequence similarities
In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length854
- Mass (Da)92,150
- Last updated2009-05-26 v1
- Checksum8BA653D8B8B794E3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 666-695 | Polar residues | ||||
Sequence: PNGGVPNNGGLPNNGNQGPSNGYAQPSYPQ | ||||||
Compositional bias | 730-776 | Polar residues | ||||
Sequence: TYPGQQSGGYTGGQNPTPPNQSQGQYGQPQHGQPQPDQGQYGQPHPG |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008957 EMBL· GenBank· DDBJ | BAH31333.1 EMBL· GenBank· DDBJ | Genomic DNA |