ID   PRTL5_LYSSX             Reviewed;          12 AA.
AC   P85158;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Proteinase L5;
DE            EC=3.4.-.-;
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, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   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: Peptidase. Has bacteriolytic activity. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 80 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Hydrolase; Protease; Secreted.
FT   CHAIN           1..>12
FT                   /note="Proteinase L5"
FT                   /id="PRO_0000292607"
FT   NON_TER         12
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   12 AA;  1304 MW;  28714A4F4FE05878 CRC64;
     ATVQGGIXYR MP