ID   LYSC_PSEAB              Reviewed;         462 AA.
AC   Q02SZ7;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Lysyl endopeptidase;
DE            EC=3.4.21.50;
DE   AltName: Full=Protease IV;
DE   AltName: Full=PvdS-regulated endoprotease;
DE   Flags: Precursor;
GN   Name=prpL; OrderedLocusNames=PA14_09900;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION AT TYR-429.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=24965220; DOI=10.1002/pmic.201400190;
RA   Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT   "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT   aeruginosa PA14 strain.";
RL   Proteomics 14:2017-2030(2014).
CC   -!- FUNCTION: Lysine-specific endoprotease. Involved in corneal virulence.
CC       {ECO:0000250|UniProtKB:Q9HWK6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.;
CC         EC=3.4.21.50;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}.
CC   -!- PTM: Processing of pro-protein to mature protein is probably
CC       autocatalytic. {ECO:0000250|UniProtKB:Q9HWK6}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; CP000438; ABJ13453.1; -; Genomic_DNA.
DR   RefSeq; WP_003110541.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02SZ7; -.
DR   SMR; Q02SZ7; -.
DR   MEROPS; S01.281; -.
DR   iPTMnet; Q02SZ7; -.
DR   PRIDE; Q02SZ7; -.
DR   EnsemblBacteria; ABJ13453; ABJ13453; PA14_09900.
DR   KEGG; pau:PA14_09900; -.
DR   HOGENOM; CLU_047007_0_0_6; -.
DR   OMA; ANHCIST; -.
DR   BioCyc; PAER208963:G1G74-822-MON; -.
DR   Proteomes; UP000000653; Chromosome.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Disulfide bond; Hydrolase; Phosphoprotein;
KW   Protease; Secreted; Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..211
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWK6"
FT                   /id="PRO_0000431341"
FT   CHAIN           212..462
FT                   /note="Lysyl endopeptidase"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWK6"
FT                   /id="PRO_0000431342"
FT   ACT_SITE        283
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWK6"
FT   ACT_SITE        333
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWK6"
FT   ACT_SITE        409
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HWK6"
FT   MOD_RES         429
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:24965220"
FT   DISULFID        224..435
FT                   /evidence="ECO:0000250"
FT   DISULFID        230..305
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  48178 MW;  20F078CB7C59ABD4 CRC64;
     MHKRTYLNAC LVLALAAGAS QASAAPGASE MAGDVAVLQA SPASTGHARF ANPNAATSAA
     GIHFAAPPAR RVARAAPLAP KPGTPLQVGV GLKTATPEID LATLEWIDTP DGRHTARFPI
     SAAGAASLRA AIRLETRSGS LPDDVLLHFA GAGKEIFEAS GKDLSLNRPY WSPVIEGDTL
     TVELVLPANL QPGDLRLSVP QVSYFADSLY KAGYRDGFGA SGSCEVDAVC ATQSGTRAYD
     NATAAVAKMV FTSSADGGSY ICTGTLLNNG NSPKRQLFWS AAHCIEDQAT AATLQTIWFY
     NTTQCYGDAS TINQSVTVLT GGANILHRDA KRDTLLLELK RTPPAGVFYQ GWSATPIANG
     SLGHDIHHPR GDAKKYSQGN VSAVGVTYDG HTALTRVDWP SAVVEGGSSG SGLLTVAGDG
     SYQLRGGLYG GPSYCGAPTS QRNDYFSDFS GVYSQISRYF AP