A0A552CJC6 · A0A552CJC6_9CHRO

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

165450100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site244-251ATP (UniProtKB | ChEBI)
Binding site469Zn2+ (UniProtKB | ChEBI); catalytic
Active site470
Binding site473Zn2+ (UniProtKB | ChEBI); catalytic
Binding site546Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentplasma membrane-derived thylakoid membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processprotein catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent zinc metalloprotease FtsH
  • EC number

Gene names

    • Name
      hflB
    • Synonyms
      ftsH
    • ORF names
      EWV60_10375

Organism names

  • Taxonomic identifier
  • Strain
    • Msp_OC_L_20101000_S702
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Microcystaceae > Microcystis

Accessions

  • Primary accession
    A0A552CJC6

Proteomes

Subcellular Location

Cellular thylakoid membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane17-35Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region84-113Disordered
Compositional bias96-112Polar residues
Domain236-378AAA+ ATPase

Sequence similarities

Belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    654
  • Mass (Da)
    71,194
  • Last updated
    2019-10-16 v1
  • MD5 Checksum
    AA9C725851C523073861F4EF39F2D1C8
MTNQEDNQFSWSRLPRLGKILIICSGVAALGYFLIPRPSELSNIPLEPYSEFINKVERGDISRVRIGNQVILYQLKNPLESLAIPGNPPLNPPESSNPFHSDSSSLASKPSSNLAPGRVLATIPVDNPQLPQLLQQKGVIFEAIPVAENSWISTLLAWVVPPLILVAAMQFLLYRNDDTRKSLLFNKNLAKVYGDDEKYPITFTDVAGAEEAKTELKEIVEFLKDAERFNKIGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVTFFSISASEFVELFVGTGAARVRDLFAQAKKNAPSIIFIDELDAIGKSRSSGSGTSGSNDEREQTLNQLLTEMDGFSPKEAVVIVLAATNRPETLDAALLRPGRFDRQVLVDRPDLAGRLAILEIYAQRVQMGEDVNLKAIATQTPGFAGADLANLVNEAALLAARNNREKVSQIDFKEAIERVIAGLEKKSRVLSEKEKKIVAYHEVGHALVGAVMPGGGRVEKISIVPRGLSALGYTLKIPTEDRFLMTETEFKEQITMLLGGRAAEELIFGSVTNGASDDLQRATDIAERMVTIYGMSKSLGPLAYDKTGQANFLGNNQGSPRRSIGENTAKVIDEEVKQIIDASYQKALAILSYNRNLLESITANLLTTEVIEGEELQELLNQAQMV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias96-112Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SFBO01000090
EMBL· GenBank· DDBJ
TRU10068.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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