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P85152 (LYS1_LYSSX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme

EC=3.2.1.17
Alternative name(s):
Endolysin
Lysis protein
Muramidase L3
OrganismLysobacter sp. (strain XL1)
Taxonomic identifier186334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has bacteriolytic activity. Ref.1

Catalytic activity

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Ref.1

Subunit structure

Monomer. Ref.1

Subcellular location

Secreted Ref.1.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0. Ref.1

Temperature dependence:

Optimum temperature is 60 degrees Celsius. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionAntibiotic
Antimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Lysozyme
PRO_0000291306

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P85152 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 8F48EE97DE5EC7AB

FASTA202,094
        10         20 
IAIQGGXGYL XQPGDGYKYA 

« Hide

References

[1]"Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1."
Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S.
Submitted (MAY-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameLYS1_LYSSX
AccessionPrimary (citable) accession number: P85152
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: June 12, 2007
Last modified: October 16, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries