A0A3S0QUX0 · A0A3S0QUX0_9HYPH

  • Protein
    Probable periplasmic serine endoprotease DegP-like
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Predicted
  • Annotation score
    2/5

Function

function

Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions.

Caution

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

Catalytic activity

  • Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.
    EC:3.4.21.107 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

157150100150200250300350400450500550
TypeIDPosition(s)Description
Active site157Charge relay system
Active site187Charge relay system
Active site261Charge relay system

GO annotations

AspectTerm
Cellular Componentperiplasmic space
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable periplasmic serine endoprotease DegP-like
  • EC number
  • Alternative names
    • Protease Do

Gene names

    • ORF names
      EFQ99_16935

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CCBAU 65647
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A3S0QUX0

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-33
ChainPRO_503887426834-571Probable periplasmic serine endoprotease DegP-like

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region38-77Disordered
Region96-135Disordered
Compositional bias121-135Polar residues
Domain305-396PDZ
Region403-472Disordered
Compositional bias442-458Polar residues
Domain477-526PDZ

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    571
  • Mass (Da)
    58,666
  • Last updated
    2019-04-10 v1
  • Checksum
    9D603095ABC073A4
MAPTIRSPFRRTLALLASAAILAQAGVSGIAHAQTAPEAAAPGMATPPAAAQTAPAPAAPQQVPPIQSTVPNNGPASVADLAEGLLDAVVNISTSQNVKDDEGAGPAPRAPDGSPFQEFFNDFFNKKQGNKGPNHNVSSLGSGFVIDPTGYIVTNNHVIEGADDIEINFANGSKLKAKLIGTDTKTDLSVLKVEPKTPLKSVKFGDSSTMRIGDWVMAIGNPFGFGGSVTVGIISGRGRNINAGPYDNFIQTDAAINKGNSGGPLFNMKGEVIGINTAIISPSGGSIGIGFSVPSELASGVVEQLRQFGETRRGWLGVRIQPVTDDIADSLGLDSAKGALVAGVIKGGPVDDGSIKAGDVILKFDGKAVIEMRDLPRVVAESAVGKQVDVVVLRDGKEQTVKVTLGRLEDSDQPGGSDDAAPDGSQDDGVITPDPGENNDMDQPDTGDQAQPAPTAPDQHQGQGHAAPDAATPKNVLGLSLSLLSPETRKAFGIAESVDGVVVTEVTPGSASAEKGLKPGDVIVEVAQEFMKSPDAVAAKVQSLKQEGRRNAQLMIASANGDLRFVAVPME

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias121-135Polar residues
Compositional bias442-458Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RJTH01000005
EMBL· GenBank· DDBJ
RUM24463.1
EMBL· GenBank· DDBJ
Genomic DNA

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