D1L2X1 · DPOL2_BPK32

Function

function

Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K21-type polysaccharides Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor (PubMed:30405575, PubMed:32386574, PubMed:33947754).

Features

Showing features for active site.

157650100150200250300350400450500550
TypeIDPosition(s)Description
Active site170
Active site229
Active site239
Active site241

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
Cellular Componentvirus tail
Biological Processadhesion receptor-mediated virion attachment to host cell
Biological Processsymbiont entry into host cell via disruption of host cell envelope
Biological Processsymbiont entry into host cell via disruption of host cell glycocalyx

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Depolymerase 2, capsule K21-specific
  • Alternative names
    • Gene product 38
      (gp38
      )
    • KP32gp38
    • Probable tail spike protein

Gene names

    • Name
      38

Organism names

Accessions

  • Primary accession
    D1L2X1

Proteomes

Subcellular Location

Virion
Note: Tail appendage (Probable). Depolymerase 1 is connected to the phage tail via an N-terminal anchor domain, while depolymerase 2 is attached to depolymerase 1 (PubMed:33947754).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis1678 times decreased enzymatic activity.
Mutagenesis1702000 times decreased enzymatic activity.
Mutagenesis229256 times decreased enzymatic activity.
Mutagenesis2392000 times decreased enzymatic activity.
Mutagenesis24115000 times decreased enzymatic activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004587101-576Depolymerase 2, capsule K21-specific

Interaction

Subunit

Homotrimer (PubMed:30405575, PubMed:32386574).
The 3 parallel chains are tightly packed together to form an elongated structure of approximately 7 x 12 nm (PubMed:32386574).
Interacts (via N-terminus) with depolymerase 1 (via N-terminus); this interaction probably gives rise to a branched tailspike (PubMed:32386574).

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region34-360Catalytic
Region380-487Carbohydrate binding
Region488-576Lectin-like

Domain

Consists in a catalytic region, a carbohydrate binding region and a lectin-like region (PubMed:32386574).
The active site consists of catalytic dyads Asp-Glu located at the interface between 2 adjacent subunits (PubMed:32386574).
The lectin-like region is probably involved in trimerization (PubMed:32386574).

Sequence similarities

In the N-terminal section; belongs to the Przondovirus depolymerase 2 family.
In the C-terminal section; belongs to the K21-specific depolymerase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    576
  • Mass (Da)
    61,687
  • Last updated
    2010-01-19 v1
  • Checksum
    F57CAAA54812646E
MLDNFNQPKGSTIGVLKDGRTIQEAFDSLPRLESFSGSTATDKLRAAITLGVSEVAIGPVEGNGGRPYEFGDVVIPYPLRIVGCGSQGINVTKGTVLKRSAGASFMFHFTGEGQAQRPMGGGLFNINLNGDTATALGDIIKVTQWSYFKANNCAFQNMAGWGIRLKDVMESNISGNLFRRLGGPSGGGILFDDVRSAVTDNVNNLHIEDNTFALMSGPWIGSTANSNPDLIWIVRNKFEFDGTPAAPNTVDSYVLDFQQLSRAFIQDNGFTHFTTERNRYVGVLRVGATAVGTIKFEDNLLFACESAGLIAGGIVVSRGNVNNQGSATTAIKQFTNTSSKLCKLERVINVQSNGNVSVGQQILPDGYINMAELPGNTRLPSEYDADGETTSVLRVPANTQVRQWSVPKMYKDGLTVTKVTVRAKGAAAGAILSLQSGSTVLSTKSIDAGVWKNYVFYVKANQLQETLQLRNTGTADVLADGMVFGKVDYIDWDFAIAPGTLAAGAKYTTPNQSYLDVAGMRVQAVSIPMFDGPTTGLQVWVEATSANGSFVVVMKNDTGSELVTTVTRCRVRAFVS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GQ413937
EMBL· GenBank· DDBJ
ACY66700.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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