LYS1_LYSSX
ID LYS1_LYSSX Reviewed; 20 AA.
AC P85152;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 11-DEC-2019, entry version 19.
DE RecName: Full=Lysozyme;
DE EC=3.2.1.17;
DE AltName: Full=Endolysin;
DE AltName: Full=Lysis protein;
DE AltName: Full=Muramidase L3;
DE Flags: Fragment;
OS Lysobacter sp. (strain XL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter; unclassified Lysobacter.
OX NCBI_TaxID=186334;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RA Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S.;
RT "Identification of extracellular bacteriolytic enzymes from Lysobacter sp.
RT XL1.";
RL Submitted (MAY-2007) to UniProtKB.
CC -!- FUNCTION: Has bacteriolytic activity. {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW Glycosidase; Hydrolase; Secreted.
FT CHAIN 1..>20
FT /note="Lysozyme"
FT /id="PRO_0000291306"
FT NON_TER 20
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 20 AA; 2094 MW; 8F48EE97DE5EC7AB CRC64;
IAIQGGXGYL XQPGDGYKYA