ID   LASA_PSEAB              Reviewed;         418 AA.
AC   Q02L18;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Protease LasA;
DE            EC=3.4.24.-;
DE   AltName: Full=Staphylolytic protease;
DE   Flags: Precursor;
GN   Name=lasA; OrderedLocusNames=PA14_40290;
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, AND SUBCELLULAR LOCATION.
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: Involved in proteolysis and elastolysis (degradation of the
CC       host protein elastin). Has staphylolytic activity (degrades
CC       pentaglycine cross-links in cell wall peptidogylcan), preferring Gly-
CC       Gly-|-X substrates where X is Ala or Gly. Enhances the elastolytic but
CC       not proteolytic activity of elastase (lasB) and elastolytic activity of
CC       other proteases. Degradation of elastin is likely to contribute to the
CC       pathogenicity of P.aeruginosa. {ECO:0000250|UniProtKB:P14789}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P14789};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P14789};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}.
CC   -!- SIMILARITY: Belongs to the peptidase M23A family. {ECO:0000305}.
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DR   EMBL; CP000438; ABJ11061.1; -; Genomic_DNA.
DR   RefSeq; WP_003139897.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02L18; -.
DR   SMR; Q02L18; -.
DR   MEROPS; M23.002; -.
DR   PRIDE; Q02L18; -.
DR   EnsemblBacteria; ABJ11061; ABJ11061; PA14_40290.
DR   KEGG; pau:PA14_40290; -.
DR   HOGENOM; CLU_656977_0_0_6; -.
DR   OMA; ATNYYHM; -.
DR   BioCyc; PAER208963:G1G74-3378-MON; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR000841; Pept_M23A_Blytic.
DR   InterPro; IPR016047; Peptidase_M23.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   PRINTS; PR00933; BLYTICPTASE.
DR   SUPFAM; SSF51261; SSF51261; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..418
FT                   /note="Protease LasA"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431336"
FT   PROPEP          32..236
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT                   /id="PRO_0000431335"
FT   ACT_SITE        317
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT   ACT_SITE        356
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT   DISULFID        301..347
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
FT   DISULFID        391..406
FT                   /evidence="ECO:0000250|UniProtKB:P14789"
SQ   SEQUENCE   418 AA;  45556 MW;  28BAADA4BB1417B9 CRC64;
     MQHKRSRALA SPRSPFLFAL LALAVGGTAN AHDDGLPAFR YSAELLGQLQ LPSVALPLND
     ELFLYGRDAE AFDLEAYLAL NAPALRDKSE YLEHWSGYYS INPKVLLTLM VMQSGPLGAP
     DERALAAPLG RLSAKRGFDA QVRDVLQQLS RRYYGFEEYQ LRQAAARKAV GEDGLNAASA
     ALLGLLREGA KASAVQGGNP LGAYAQTFQR LFGTPAAELL QPRNRVARQL QAKAALAPPS
     NLMQLPWRQG YSWQPNGAHS NTGSGYPYSS FDASYDWPRW GSATYSVVAA HAGTVRVLSR
     CQVRVTHPSG WATNYYHMDQ IQVSNGQQVS ADTKLGVYAS NINTALCEGG SSTGPHLHFS
     LLYNGAFVSL QGASFGPYRI NVGTSNYDND CRRYYFYNQS AGTTHCAFRP LYNPGLAL