ELAS_PSEAB
ID ELAS_PSEAB Reviewed; 498 AA.
AC Q02RJ6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Elastase;
DE EC=3.4.24.26;
DE Contains:
DE RecName: Full=Pro-elastase;
DE Flags: Precursor;
GN Name=lasB; OrderedLocusNames=PA14_16250;
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 THR-236.
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: Cleaves host elastase, collagen, IgI and several complement
CC components as well as endogenous pro-aminopeptidase, pro-chitin-binding
CC protein (cbpD). Cleaves its own pro-peptide. Involved in the
CC pathogenesis of P.aeruginosa infections.
CC {ECO:0000250|UniProtKB:P14756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins including elastin, collagen types III
CC and IV, fibronectin and immunoglobulin A, generally with bulky
CC hydrophobic group at P1'. Insulin B chain cleavage pattern identical
CC to that of thermolysin, but specificity differs in other respects.;
CC EC=3.4.24.26;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14756};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14756};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P14756};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14756};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}.
CC -!- PTM: Made as a pre-pro-protein which is exported to the periplasm.
CC Probably autocatalyzes cleavage of its pro-peptide. The pro-peptide can
CC be secreted with mature elastase. {ECO:0000250|UniProtKB:P14756}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ12957.1; -; Genomic_DNA.
DR RefSeq; WP_003092588.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02RJ6; -.
DR SMR; Q02RJ6; -.
DR MEROPS; M04.005; -.
DR iPTMnet; Q02RJ6; -.
DR PRIDE; Q02RJ6; -.
DR EnsemblBacteria; ABJ12957; ABJ12957; PA14_16250.
DR KEGG; pau:PA14_16250; -.
DR HOGENOM; CLU_008590_4_2_6; -.
DR OMA; QLYWTAN; -.
DR BioCyc; PAER208963:G1G74-1337-MON; -.
DR BRENDA; 3.4.24.26; 5087.
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; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Secreted; Signal; Virulence;
KW Zinc; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..498
FT /note="Pro-elastase"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT /id="PRO_0000431338"
FT PROPEP 24..197
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT /id="PRO_0000431339"
FT CHAIN 198..498
FT /note="Elastase"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT /id="PRO_0000431340"
FT ACT_SITE 338
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT ACT_SITE 420
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT SITE 197..198
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24965220"
FT DISULFID 227..255
FT /evidence="ECO:0000250|UniProtKB:P14756"
FT DISULFID 467..494
FT /evidence="ECO:0000250|UniProtKB:P14756"
SQ SEQUENCE 498 AA; 53601 MW; FDDF0C817A6D98E5 CRC64;
MKKVSTLDLL FVAIMGVSPA AFAADLIDVS KLPSKAAQGA PGPVTLQAAV GAGGADELKA
IRSTTLPNGK QVTRYEQFHN GVRVVGEAIT EVKGPGKSVA ARRSGHFVAN IAADLPGSTT
AAVSAEQVLA QAKSLKAQGR KTENDKVELV IRLGENNIAQ LVYNVSYLIP GEGLSRPHFV
IDAKTGEVLD QWEGLAHAEA GGPGGNQKIG KYTYGSDYGP LIVNDRCEMD DGNVITVDMN
GSTNDSKTTP FRFACPTNTY KQVNGAYSPL NDAHFFGGVV FNLYRDWFGT SPLTHKLYMK
VHYGRSVENA YWDGTAMLFG DGATMFYPLV SLDVAAHEVS HGFTEQNSGL IYRGQSGGMN
EAFSDMAGEA AEFYMRGKND FLIGYDIKKG SGALRYMDQP SRDGRSIDNA SQYYNGIDVH
HSSGVYNRAF YLLANSPGWD TRKAFEVFVD ANRYYWTATS NYNSGACGVI SSAQNRNYSA
ADVTRAFSTV GVTCPSAL
