ID   ENPL4_LYSSX             Reviewed;          15 AA.
AC   P85155;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Endopeptidase L4;
DE            EC=3.4.21.-;
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, 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.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-14, FUNCTION, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16266276; DOI=10.1007/s10541-005-0221-1;
RA   Stepnaya O.A., Tsfasman I.M., Logvina I.A., Ryazanova L.P., Muranova T.A.,
RA   Kulaev I.S.;
RT   "Isolation and characterization of a new extracellular bacteriolytic
RT   endopeptidase of Lysobacter sp. XL1.";
RL   Biochemistry (Mosc.) 70:1031-1037(2005).
CC   -!- FUNCTION: Diaminopimelinoyl-alanine endopeptidase. Has antibacterial
CC       activity. {ECO:0000269|PubMed:16266276}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF and p-chloromercuribenzoate.
CC       Unaffected by EDTA. {ECO:0000269|PubMed:16266276}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:16266276};
CC       Temperature dependence:
CC         Optimum temperature is 50-55 degrees Celsius. Retains 50% of its
CC         maximal activity after incubation at 52 degrees Celsius for 15 min.
CC         {ECO:0000269|PubMed:16266276};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; 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; Direct protein sequencing; Hydrolase; Protease;
KW   Secreted; Serine protease.
FT   CHAIN           1..>15
FT                   /note="Endopeptidase L4"
FT                   /id="PRO_0000292608"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   15 AA;  1465 MW;  1C6918761FD4BCDE CRC64;
     AVVNGVNYVG ETTAA