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Lysozyme (EC 3.2.1.17) (Endolysin) (Lysis protein) (Muramidase L3) (Fragment)

 LYS1_LYSSX              Reviewed;          20 AA.
P85152;
12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 1.
05-DEC-2018, entry version 17.
RecName: Full=Lysozyme;
EC=3.2.1.17;
AltName: Full=Endolysin;
AltName: Full=Lysis protein;
AltName: Full=Muramidase L3;
Flags: Fragment;
Lysobacter sp. (strain XL1).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Lysobacter.
NCBI_TaxID=186334;
[1] {ECO:0000305}
PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S.;
"Identification of extracellular bacteriolytic enzymes from Lysobacter
sp. XL1.";
Submitted (MAY-2007) to UniProtKB.
-!- FUNCTION: Has bacteriolytic activity. {ECO:0000269|Ref.1}.
-!- CATALYTIC ACTIVITY:
Reaction=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.; EC=3.2.1.17; Evidence={ECO:0000269|Ref.1};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0. {ECO:0000269|Ref.1};
Temperature dependence:
Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1};
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
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GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Bacteriolytic enzyme;
Direct protein sequencing; Glycosidase; Hydrolase; Secreted.
CHAIN 1 >20 Lysozyme.
/FTId=PRO_0000291306.
NON_TER 20 20 {ECO:0000303|Ref.1}.
SEQUENCE 20 AA; 2094 MW; 8F48EE97DE5EC7AB CRC64;
IAIQGGXGYL XQPGDGYKYA


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