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A0A087AID0 · A0A087AID0_9BIFI

  • Protein
    ATP-dependent zinc metalloprotease FtsH
  • Gene
    ftsH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

169550100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site255-262ATP (UniProtKB | ChEBI)
Binding site477Zn2+ (UniProtKB | ChEBI); catalytic
Active site478
Binding site481Zn2+ (UniProtKB | ChEBI); catalytic
Binding site553Zn2+ (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 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
      ftsH
    • ORF names
      BcFMB_04920
      , BCHO_0577

Organism names

  • Taxonomic identifier
  • Strains
    • LMG 10510
    • FMB-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A087AID0

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane49-67Helical
Transmembrane161-183Helical

Keywords

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-22Polar residues
Region1-41Disordered
Domain247-386AAA+ ATPase
Region662-695Disordered

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
    695
  • Mass (Da)
    75,610
  • Last updated
    2014-10-29 v1
  • MD5 Checksum
    EF95186F9DD2E47D20357D504915E0F9
MSIPQGPQQPRGNRNGSPGNRPNPFNPSDPNNPGDGNQNGRRNAWRSPWFWGTIVALVALVIIFFSMNGGAKTITTEQGLSILKSNASNITNATIVDNQNLVELKLKDAYSGKDPNSGNERNYGTDVQFYFATAQDADIVKAVEDAKPANGWTATIKTQGALTYMLTSLLPILIILGFGWFLMSRMSSTSGMLGMGGKKNAGKLADGQIPKTKFSDVAGEEAAVQEVEEIKDFLKDPAKYKALGARIPRGVLLYGPPGTGKTLLARAIAGEAGVPFYSMAGSDFVEMFVGLGASRVRDLFDEAKKNAPAIIFIDEIDAVGRKRGSGMGGGHDEREQTLNQLLVEMDGFDNDTNLIIIAATNRPDVLDPALLRPGRFDRQVAVEAPDLEGREEILKVHAKGKPFVPDIDLHAIAVRTPGFTGADLANVLNEAALLCARVGAQLIDNRAIDEAIDRVMSGPRRRTRGMALDELRNTAYHEGGHALVAAALHNTDPVTKVTILPRGRALGYTAVMPTEDRYSQSRNELLDQMAYAMGGRTAEEIVFHDPTTGASNDIEKATNIARHMVGEYGLSSQLGAVKWIDSDDDQGLDGLRPRNYSNATAEMIDEQVLDLIETAHQEAWQILTDNRAILDELVRRLLVKQTLNEKELKEVFADIKMAPERPVWLSNPNRPDSDVPPVPIPESLKESAGIPQQQF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP018044
EMBL· GenBank· DDBJ
ATU20367.1
EMBL· GenBank· DDBJ
Genomic DNA
JGYU01000001
EMBL· GenBank· DDBJ
KFI58530.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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