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A0A1A2PG84 · A0A1A2PG84_9MYCO

  • 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.

Caution

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.

1785100200300400500600700
Type
IDPosition(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 Processcell division
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
      A5693_04045

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • E1319
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium

Accessions

  • Primary accession
    A0A1A2PG84

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.

Type
IDPosition(s)Description
Domain195-334AAA+ ATPase
Region662-785Disordered
Compositional bias672-686Polar residues
Compositional bias705-720Pro residues
Compositional bias743-764Pro residues
Compositional bias768-785Basic 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
    785
  • Mass (Da)
    84,970
  • Last updated
    2016-10-05 v1
  • MD5 Checksum
    99BCCF1A1338F36E3E1CC9078F730C10
MNRKNVIRTIAVIAVVVLLGWSFFYFSDDTRGYKPVDTSVAMSQIRGDNVKSAQIDDREQQLRLTLKKANGDTDNSDKVITKYPSGYAVDLFNALNDKNAKVSTVVNQGSILGELLVYVLPLLLLVGLFVMFSRMQGGARMGFGFGKSRAKQLSKDMPKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPVTNPDLAGRRAVLRVHSKGKPIAPDADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITSAALEEAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIDPVYKVTILARGRTGGHAVAVPEEDKGLRTRSEMVAQLVFAMGGRAAEELVFREPTTGAVSDIEQATKTARAMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGNQADYSHEVARDIDDEIRKLIEAAHTEAWEILTEHRDVLDTLAGELLEKETLHRPELERIFADVEKRPRLTMFDDFGGRIPSDKPPIKTPGELAIERGEPWPPPVPEPAFKVAIAAAAEAARADAERNANGGNGSHGTQGAPNGPTQPDYGAPAGWHAPGWPPQHQQPWYPPGQPPQQQYWPQPATNHPGQPGYPGHPGQQGQPYPSYPPYPPYPPPAQPSPQGGNSPERRDDDVSRSNPPAHG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias672-686Polar residues
Compositional bias705-720Pro residues
Compositional bias743-764Pro residues
Compositional bias768-785Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LZJL01000104
EMBL· GenBank· DDBJ
OBH26300.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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