ID   PRLA_LYSSX              Reviewed;          62 AA.
AC   P85142;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Alpha-lytic protease L1;
DE            EC=3.4.21.12;
DE   AltName: Full=Alpha-lytic endopeptidase L1;
DE   Flags: Fragments;
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.
RX   PubMed=15193123; DOI=10.1023/b:biry.0000029847.40511.26;
RA   Muranova T.A., Krasovskaya L.A., Tsfasman I.M., Stepnaya O.A., Kulaev I.S.;
RT   "Structural investigations and identification of the extracellular
RT   bacteriolytic endopeptidase L1 from Lysobacter sp. XL1.";
RL   Biochemistry (Mosc.) 69:501-505(2004).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, 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 (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Has bacteriolytic activity. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell
CC         walls, elastin and other proteins.; EC=3.4.21.12;
CC         Evidence={ECO:0000250|UniProtKB:P00778, ECO:0000269|Ref.2};
CC   -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF)
CC       and p-chloromercuribenzoate (PCMB). {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 7.0 to 11.0. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   AlphaFoldDB; P85142; -.
DR   SMR; P85142; -.
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.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           1..>62
FT                   /note="Alpha-lytic protease L1"
FT                   /id="PRO_0000287680"
FT   ACT_SITE        48
FT                   /note="Charge relay system"
FT   DISULFID        17..?
FT                   /evidence="ECO:0000250|UniProtKB:P00778,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        42..?
FT                   /evidence="ECO:0000250|UniProtKB:P00778,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000303|PubMed:15193123"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000303|PubMed:15193123"
FT   NON_CONS        54..55
FT                   /evidence="ECO:0000303|PubMed:15193123"
FT   NON_CONS        58..59
FT                   /evidence="ECO:0000303|PubMed:15193123"
FT   NON_TER         62
FT                   /evidence="ECO:0000303|PubMed:15193123"
SQ   SEQUENCE   62 AA;  6611 MW;  2C602878C9E3BFDE CRC64;
     VNVLGGIEYS INNATLCSVG FSVRVFNYAE GAVRGLTQGN ACMGRGDSGG SWFTLFERQY
     GL