A0A178A553 · A0A178A553_9BACI

  • Protein
    ATP-dependent Clp protease ATP-binding subunit ClpX
  • Gene
    clpX
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Features

Showing features for binding site.

142050100150200250300350400
TypeIDPosition(s)Description
Binding site13Zn2+ (UniProtKB | ChEBI)
Binding site16Zn2+ (UniProtKB | ChEBI)
Binding site35Zn2+ (UniProtKB | ChEBI)
Binding site38Zn2+ (UniProtKB | ChEBI)
Binding site117-124ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentHslUV protease complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionpeptidase activity
Molecular Functionprotein dimerization activity
Molecular Functionunfolded protein binding
Molecular Functionzinc ion binding
Biological Processcell division
Biological Processproteolysis involved in protein catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent Clp protease ATP-binding subunit ClpX

Gene names

    • Name
      clpX
    • ORF names
      ABB05_04900

Organism names

Accessions

  • Primary accession
    A0A178A553

Proteomes

Subcellular Location

Interaction

Subunit

Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-54ClpX-type ZB

Sequence similarities

Belongs to the ClpX chaperone family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    420
  • Mass (Da)
    46,750
  • Last updated
    2016-09-07 v1
  • Checksum
    9DEBA988EB0E91A0
MFKFNEEKGQLKCSFCGKTQEQVRKLVAGPGVYICDECIELCTEIVEEELGTEEEVEFKDIPKPREIREILDEYVIGQEQAKKSLAVAVYNHYKRINANSKIDDVELAKSNICLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLKLIQSADYDVEKAERGIIYIDEIDKVARKSENTSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNILFICGGAFDGVEQIIKRRLGQKVIGFGADVKGQEENKEILSEILPEDLLRFGLIPEFIGRLPVIANLEQLDEEALIEILTQPKNALVKQYKKMLDMDEVDLAFEDEALHEIAKKAIERKTGARGLRSIIEMLMLDVMFDLPSRDDIKKCIITKDSVLHNNPPKLVLEDGTVIKGSEKNSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LDJR01000027
EMBL· GenBank· DDBJ
OAK74228.1
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.
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