A0A2U2EB27 · A0A2U2EB27_MYCAV

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.

1799100200300400500600700
TypeIDPosition(s)Description
Binding site203-210ATP (UniProtKB | ChEBI)
Binding site425Zn2+ (UniProtKB | ChEBI); catalytic
Active site426
Binding site429Zn2+ (UniProtKB | ChEBI); catalytic
Binding site501Zn2+ (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

Names & Taxonomy

Protein names

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

Gene names

    • Name
      ftsH
    • ORF names
      DFS55_22370
      , JPH1_04490
      , QRB41_19755

Organism names

  • Taxonomic identifier
  • Strains
    • MAC109
    • JP-H-1
    • FLAC0813
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)

Accessions

  • Primary accession
    A0A2U2EB27

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane7-26Helical
Transmembrane115-132Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain195-334AAA+ ATPase
Region616-649Disordered
Region671-799Disordered
Compositional bias675-690Polar residues
Compositional bias713-727Pro residues
Compositional bias739-779Pro residues
Compositional bias782-799Basic and acidic 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    799
  • Mass (Da)
    86,097
  • Last updated
    2018-09-12 v1
  • Checksum
    E45992FA832ACBF4
MNRKNVIRTITAIAVVVLLGWSFFYFSDDTRGYKPVDTSVAMAQINGDNVKSAQIDDREQQLRLTLKKGNGDTDNSDKVITKYPSGYAVDLFNALSAKNAKVSTVVNQGSILGELLVYVLPLLLLVGLFVMFSRMQGGARMGFGFGKSRAKQLSKDMPKTTFADVAGVDEAVEELYEIKDFLQNPGRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFDQAKQNNPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFDPRAGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLAVHSKGKPIAPDADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITSAALEEAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREPTTGAVSDIEQATKIARAMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQADYSHEVARDIDDEIRKLIEAAHTEAWEILTEYRDILDTLAGQLLEKETLHRAELESIFAGVEKRPRLTMFDDFGGRIPSDKPPIKTPGELAIERGEPWPPPAPEPAFKAAIARASEAAAAARLEADRNANGGNGSHANQGGNRQGPTQPDYGAPAGWRAPGWPPQQSQQPNYWHPPAQPPYWQQPAHGYPGQQPYPGQQPYPGQPGGPAQSGPPQARPPYPPYPPYPPPGQPAPEGGSPDRQDDDVSRSNPPAHG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias675-690Polar residues
Compositional bias713-727Pro residues
Compositional bias739-779Pro residues
Compositional bias782-799Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP029332
EMBL· GenBank· DDBJ
AXO25018.1
EMBL· GenBank· DDBJ
Genomic DNA
AP020326
EMBL· GenBank· DDBJ
BBN45974.1
EMBL· GenBank· DDBJ
Genomic DNA
JAULCP010000024
EMBL· GenBank· DDBJ
MDO2385602.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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