A0A6F8UWL0 · A0A6F8UWL0_9HYPH

  • Protein
    serine-type D-Ala-D-Ala carboxypeptidase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.

Catalytic activity

  • Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
    EC:3.4.16.4 (UniProtKB | ENZYME | Rhea)

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for active site, binding site.

140750100150200250300350400
TypeIDPosition(s)Description
Active site74Acyl-ester intermediate
Active site77Proton acceptor
Active site139
Binding site241substrate

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionserine-type D-Ala-D-Ala carboxypeptidase activity
Biological Processpeptidoglycan biosynthetic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    serine-type D-Ala-D-Ala carboxypeptidase
  • EC number

Gene names

    • ORF names
      OCUBac02_27690

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ANAM02
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Boseaceae > Bosea

Accessions

  • Primary accession
    A0A6F8UWL0

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain291-381Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-terminal

Sequence similarities

Belongs to the peptidase S11 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    407
  • Mass (Da)
    43,671
  • Last updated
    2020-08-12 v1
  • Checksum
    35DB32250219ED78
MSAFCHQRLRAVPPRAASGRLVAVLALLLGLIVLGPPALAQNFQSQAPFAVLMDSDTGAVLYEKAADEPMVPASMAKLATVLVAFQDLNAGRLTLDSEIGISENAWRKGGGPSGGSAMFAVLNSRIKLSDILQGIIVQSGNDAAIALAEAIAGDEATFARIMTERVRGIGLTKSVFRNATGMPDPQQRVTARELALLADHIIKTYPELYRIFGQREFTWNKIRQQNRNPLLAMDIGADGLKTGNLDESGFGLVGSAVQNDQRLIVVVNGLKTGRDRANEARKLLEWGFRAFERRQLFAAGETVGEASVYGGEKGRVALRSKAAVSLLLPRGGSERLAARIIYRGPLSVPVQEGAEVARLVVTRGDIKTLDIPLYAAESVQAGTLQSRVLDALFEATTGWVRKALSRS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP022848
EMBL· GenBank· DDBJ
BCB19875.1
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