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Reviewed, UniProtKB/Swiss-Prot Q54873 (HYSA_STRPN)

Last modified November 25, 2008. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hyaluronate lyase
    EC=4.2.2.1
Alternative name(s):
    Hyaluronidase
      Short name=HYase
Gene names
Ordered Locus Names: SP_0314
OrganismStreptococcus pneumoniae [Complete proteome] [HAMAP]
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

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Protein attributes

Sequence length1066 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.

Subcellular location

Secreted › cell wall; Peptidoglycan-anchorPotential.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

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Ontologies

Keywords

   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionLyase
   PTMPeptidoglycan-anchor
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell surface

Inferred from electronic annotation. Source: InterPro

cell wall

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

hyaluronate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 10391009Hyaluronate lyase
PRO_0000024933
Propeptide1040 – 106627Removed by sortase Potential
PRO_0000024934

Regions

Motif1036 – 10405LPXTG sorting signal Potential

Sites

Active site4661
Active site5161
Active site5251

Amino acid modifications

Modified residue10391Pentaglycyl murein peptidoglycan amidated threonine Potential

Experimental info

Mutagenesis3601R → V: Retains 67% of wild-type activity Ref.4
Mutagenesis4661N → A: Almost complete loss of activity Ref.4
Mutagenesis5161H → A: Almost complete loss of activity Ref.4
Mutagenesis5251Y → F: Complete loss of activity Ref.4
Mutagenesis6971N → G: Slightly increased activity Ref.4
Sequence conflict1081H → P Ref.2
Sequence conflict1151L → V Ref.2
Sequence conflict1391I → V in AAA53685. Ref.2
Sequence conflict2111L → P in AAA53685. Ref.2
Sequence conflict2361S → P in AAA53685. Ref.2
Sequence conflict2901A → T in AAA53685 and AAA53686. Ref.2
Sequence conflict3131E → D in AAA53685 and AAA53686. Ref.2
Sequence conflict3401T → I in AAA53685 and AAA53686. Ref.2
Sequence conflict6131C → R in AAA53685 and AAA53686. Ref.2
Sequence conflict6581P → T in AAA53685 and AAA53686. Ref.2
Sequence conflict8211G → S in AAA53685 and AAA53686. Ref.2
Sequence conflict8481V → G in AAA53685 and AAA53686. Ref.2
Sequence conflict8531F → S in AAA53685 and AAA53686. Ref.2
Sequence conflict9071R → G in AAA53685 and AAA53686. Ref.2

Secondary structure

1 ............................................................................................................................. 1066
Helix Strand Turn

Details...