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P85152

- LYS1_LYSSX

UniProt

P85152 - LYS1_LYSSX

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Protein
Lysozyme
Gene
N/A
Organism
Lysobacter sp. (strain XL1)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Has bacteriolytic activity.1 Publication

Catalytic activityi

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.1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.1 Publication

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
Endolysin
Lysis protein
Muramidase L3
OrganismiLysobacter sp. (strain XL1)
Taxonomic identifieri186334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20Lysozyme
PRO_0000291306Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Sequencei

Sequence statusi: Fragment.

P85152-1 [UniParc]FASTAAdd to Basket

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IAIQGGXGYL XQPGDGYKYA                                    20
Length:20
Mass (Da):2,094
Last modified:June 12, 2007 - v1
Checksum:i8F48EE97DE5EC7AB
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei20 – 201

Cross-referencesi

3D structure databases

ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiLYS1_LYSSX
AccessioniPrimary (citable) accession number: P85152
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries

External Data

Dasty 3

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