D3NT97 · D3NT97_AZOS1

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.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

164550100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site196-203ATP (UniProtKB | ChEBI)
Binding site418Zn2+ (UniProtKB | ChEBI); catalytic
Active site419
Binding site422Zn2+ (UniProtKB | ChEBI); catalytic
Binding site496Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

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

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      hflB
    • Synonyms
      ftsH
    • Ordered locus names
      AZL_009880

Organism names

  • Taxonomic identifier
  • Strain
    • B510
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Azospirillaceae > Azospirillum

Accessions

  • Primary accession
    D3NT97

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane104-124Helical

Keywords

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain188-327AAA+ ATPase
Region599-645Disordered
Compositional bias623-645Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    645
  • Mass (Da)
    70,176
  • Last updated
    2010-04-20 v1
  • Checksum
    0A37D0263DB152AE
MNNFGKNLALWIIIGLLLVALFNLFQSSSTRSPQTTVPFSELLAEVDRGQVADVTIKGNQVSGHFSDGRSFSTYVPPEAGLVERLTNKNVRINAVPDDSNVPSLFSVLLSWFPMLLLIGVWIFFMRQMQSGGGKAMGFGKSRARLLTEKVGRVTFDDVAGIDEAKQELTEIVEFLKDPQKFQRLGGKIPKGCLLVGPPGTGKTLTARAVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQGKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGVILIAATNRPDVLDPALLRPGRFDRQVVVPNPDVLGREKILKVHMRKVPLSPDVDAKVIARGTPGFSGADLANLVNEAALLAARIGKRVVGMAEFEAAKDKVMMGAERRSMVMTEDEKKLTAYHEAGHAICAIHCADSDPVHKATIIPRGRALGMVMRLPEGDRISLSQAKLLADLTVAMGGRIAEELIFGKERVTTGASGDIKMATEMSRRMVTEWGMSDKLGPLLYGEPTQEVFLGHSVTQHKNMSDRTAQLVDEEIRRIVDEAYDRARTILTENIDQLHTLAKGLLEYETLSGDEINRLLRGEAIPRDEERETMAVPPRPTPGSGRRSSVPPSTGQESGGMGPEPQGT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias623-645Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP010946
EMBL· GenBank· DDBJ
BAI71626.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp