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Elastase (EC 3.4.24.26) (Neutral metalloproteinase) (PAE) (Pseudolysin) [Cleaved into: Pro-elastase]

 ELAS_PSEAE              Reviewed;         498 AA.
P14756;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
05-JUL-2017, entry version 157.
RecName: Full=Elastase;
EC=3.4.24.26;
AltName: Full=Neutral metalloproteinase;
AltName: Full=PAE {ECO:0000303|PubMed:1899664};
AltName: Full=Pseudolysin;
Contains:
RecName: Full=Pro-elastase;
Flags: Precursor;
Name=lasB; OrderedLocusNames=PA3724;
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PAO;
PubMed=2842313; DOI=10.1128/jb.170.9.4309-4314.1988;
Bever R.A., Iglewski B.H.;
"Molecular characterization and nucleotide sequence of the Pseudomonas
aeruginosa elastase structural gene.";
J. Bacteriol. 170:4309-4314(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NBRC 13130 / JCM 20134;
PubMed=2493453; DOI=10.1128/jb.171.3.1698-1704.1989;
Fukushima J., Yamamoto S., Morihara K., Atsumi Y., Takeuchi H.,
Kawamoto S., Okuda K.;
"Structural gene and complete amino acid sequence of Pseudomonas
aeruginosa IFO 3455 elastase.";
J. Bacteriol. 171:1698-1704(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29260 / PA103, and N-10;
PubMed=1917848; DOI=10.1128/jb.173.19.6153-6158.1991;
Tanaka E., Kawamoto S., Fukushima J., Hamajima K., Onishi H.,
Miyagi Y., Inami S., Morihara K., Okuda K.;
"Detection of elastase production in Escherichia coli with the
elastase structural gene from several non-elastase-producing strains
of Pseudomonas aeruginosa.";
J. Bacteriol. 173:6153-6158(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PST-01;
PubMed=10828420; DOI=10.1016/S1369-703X(00)00060-7;
Ogino H., Yokoo J., Watanabe F., Ishikawa H.;
"Cloning and sequencing of a gene of organic solvent-stable protease
secreted from Pseudomonas aeruginosa PST-01 and its expression in
Escherichia coli.";
Biochem. Eng. J. 5:191-200(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
[6]
PROTEIN SEQUENCE OF 24-28 AND 198-212.
PubMed=1544509; DOI=10.1016/0014-5793(92)80134-3;
Kessler E., Safrin M., Peretz M., Burstein Y.;
"Identification of cleavage sites involved in proteolytic processing
of Pseudomonas aeruginosa preproelastase.";
FEBS Lett. 299:291-293(1992).
[7]
PROTEIN SEQUENCE OF 24-28, FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC
CLEAVAGE, AND DISRUPTION PHENOTYPE.
STRAIN=PAO1 / PAO25;
PubMed=9642203;
Braun P., de Groot A., Bitter W., Tommassen J.;
"Secretion of elastinolytic enzymes and their propeptides by
Pseudomonas aeruginosa.";
J. Bacteriol. 180:3467-3469(1998).
[8]
PROTEIN SEQUENCE OF 198-237.
STRAIN=PAO;
PubMed=3034864; DOI=10.1128/jb.169.6.2691-2696.1987;
Schad P.A., Bever R.A., Nicas T.I., Leduc F., Hanne L.F.,
Iglewski B.H.;
"Cloning and characterization of elastase genes from Pseudomonas
aeruginosa.";
J. Bacteriol. 169:2691-2696(1987).
[9]
PROTEIN SEQUENCE OF 198-217.
STRAIN=569B;
PubMed=2123831;
Haese C.C., Finkelstein R.A.;
"Comparison of the Vibrio cholerae hemagglutinin/protease and the
Pseudomonas aeruginosa elastase.";
Infect. Immun. 58:4011-4015(1990).
[10]
PROTEIN SEQUENCE OF 198-212, FUNCTION, EXPRESSION IN E.COLI, AND
MUTAGENESIS OF HIS-420.
STRAIN=FRD1;
PubMed=1744034; DOI=10.1128/jb.173.24.7781-7789.1991;
McIver K., Kessler E., Ohman D.E.;
"Substitution of active-site His-223 in Pseudomonas aeruginosa
elastase and expression of the mutated lasB alleles in Escherichia
coli show evidence for autoproteolytic processing of proelastase.";
J. Bacteriol. 173:7781-7789(1991).
[11]
PROTEIN SEQUENCE OF 212-226; 354-376 AND 429-442.
STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
Liddor M.;
"Biofouling in water treatment systems: effect of membrane properties
on biofilm formation.";
Thesis (2005), Ben-Gurion University, Israel.
[12]
SUBCELLULAR LOCATION, INDUCTION, AND PROTEOLYTIC CLEAVAGE.
STRAIN=Habs serotype I;
PubMed=3141383; DOI=10.1128/jb.170.11.5241-5247.1988;
Kessler E., Safrin M.;
"Synthesis, processing, and transport of Pseudomonas aeruginosa
elastase.";
J. Bacteriol. 170:5241-5247(1988).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1, DG1, and FRD1 / FRD2;
PubMed=1597429; DOI=10.1128/jb.174.12.4140-4147.1992;
Olson J.C., Ohman D.E.;
"Efficient production and processing of elastase and LasA by
Pseudomonas aeruginosa require zinc and calcium ions.";
J. Bacteriol. 174:4140-4147(1992).
[14]
FUNCTION, ENZYME REGULATION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1, FRD1, and Habs serotype 1;
PubMed=11533066; DOI=10.1074/jbc.M106950200;
Cahan R., Axelrad I., Safrin M., Ohman D.E., Kessler E.;
"A secreted aminopeptidase of Pseudomonas aeruginosa. Identification,
primary structure, and relationship to other aminopeptidases.";
J. Biol. Chem. 276:43645-43652(2001).
[15]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 198-498 IN COMPLEX WITH
CALCIUM AND ZINC, COFACTOR, SUBUNIT, DISULFIDE BOND, AND ACTIVE SITE.
PubMed=1899664;
Thayer M.M., Flaherty K.M., McKay D.B.;
"Three-dimensional structure of the elastase of Pseudomonas aeruginosa
at 1.5-A resolution.";
J. Biol. Chem. 266:2864-2871(1991).
[16]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 198-498 IN COMPLEX WITH
CALCIUM AND ZINC AND AN INHIBITOR, COFACTOR, AND DISULFIDE BOND.
Bitto E., McKay D.B.;
"Elastase of Pseudomonas aeruginosa with an inhibitor.";
Submitted (JUL-2004) to the PDB data bank.
[17]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 198-498 IN COMPLEX WITH
CALCIUM AND ZINC AND AN INHIBITOR, COFACTOR, AND DISULFIDE BOND.
Overgaard M.T., McKay D.B.;
"Structure of the elastase of Pseudomonas aeruginosa complexed with
phosphoramidon.";
Submitted (JUN-2008) to the PDB data bank.
-!- FUNCTION: Cleaves host elastin, collagen, IgG, and several
complement components as well as endogenous pro-aminopeptidase
(PubMed:11533066). Autocatalyses processing of its pro-peptide
(PubMed:9642203, PubMed:1744034). Processes the pro-peptide of
pro-chitin-binding protein (cbpD) (PubMed:9642203). Involved in
the pathogenesis of P.aeruginosa infections.
{ECO:0000269|PubMed:11533066, ECO:0000269|PubMed:1597429,
ECO:0000269|PubMed:1744034, ECO:0000269|PubMed:9642203}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins including elastin,
collagen types III and IV, fibronectin and immunoglobulin A,
generally with bulky hydrophobic group at P1'. Insulin B chain
cleavage pattern identical to that of thermolysin, but specificity
differs in other respects.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
ECO:0000269|Ref.17};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
ECO:0000269|Ref.17};
Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17};
-!- ENZYME REGULATION: Inhibited by phosphoramidon.
{ECO:0000269|PubMed:11533066}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1899664}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1597429,
ECO:0000269|PubMed:3141383, ECO:0000269|PubMed:9642203}.
Note=Secreted in an Xcp-dependent fashion (a type II secretion
pathway). {ECO:0000269|PubMed:9642203}.
-!- INDUCTION: Optimal protein expression in vivo requires both Zn(2+)
and Ca(2+) during growth (at protein level).
{ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:3141383}.
-!- PTM: Made as a membrane-associated pre-pro-protein, which is
exported to the periplasm (yielding pro-elastase) with removal of
the signal peptide. Under certain conditions pro-elastase can
accumulate. The pro-peptide is removed in the periplasm yielding a
(mature length) 33 kDa protein, probably by autocatalysis
(PubMed:1744034). The pro-peptide probably remains associated with
elastase and can be secreted (PubMed:9642203). Further alterations
(perhaps processing) seems to be required before secretion into
the extracellular space (PubMed:1744034).
{ECO:0000269|PubMed:11533066, ECO:0000269|PubMed:1744034,
ECO:0000269|PubMed:3141383, ECO:0000269|PubMed:9642203}.
-!- DISRUPTION PHENOTYPE: Loss of processing of its own pro-peptide
and pro-chitin-binding protein CbpD (PubMed:9642203). Loss of
processing of pro-aminopeptidase to mature aminopeptidase
(PubMed:11533066). {ECO:0000269|PubMed:11533066,
ECO:0000269|PubMed:9642203}.
-!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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EMBL; M19472; AAB36615.1; -; Genomic_DNA.
EMBL; M24531; AAA25811.1; -; Genomic_DNA.
EMBL; AB029328; BAB79621.1; -; Genomic_DNA.
EMBL; AE004091; AAG07111.1; -; Genomic_DNA.
PIR; A32359; HYBSPA.
RefSeq; NP_252413.1; NC_002516.2.
RefSeq; WP_003113835.1; NC_002516.2.
PDB; 1EZM; X-ray; 1.50 A; A=198-498.
PDB; 1U4G; X-ray; 1.40 A; A=198-498.
PDB; 3DBK; X-ray; 1.40 A; A=198-498.
PDBsum; 1EZM; -.
PDBsum; 1U4G; -.
PDBsum; 3DBK; -.
ProteinModelPortal; P14756; -.
SMR; P14756; -.
STRING; 208964.PA3724; -.
BindingDB; P14756; -.
ChEMBL; CHEMBL1075146; -.
DrugBank; DB02307; N-(1-Carboxy-3-Phenylpropyl)Phenylalanyl-Alpha-Asparagine.
MEROPS; M04.005; -.
PaxDb; P14756; -.
PRIDE; P14756; -.
EnsemblBacteria; AAG07111; AAG07111; PA3724.
GeneID; 880368; -.
KEGG; pae:PA3724; -.
PATRIC; fig|208964.12.peg.3895; -.
PseudoCAP; PA3724; -.
eggNOG; ENOG4105D4Y; Bacteria.
eggNOG; COG3227; LUCA.
HOGENOM; HOG000272374; -.
InParanoid; P14756; -.
KO; K01399; -.
OMA; HKRTTLA; -.
PhylomeDB; P14756; -.
BioCyc; MetaCyc:MONOMER-14569; -.
BRENDA; 3.4.24.26; 5087.
EvolutionaryTrace; P14756; -.
PMAP-CutDB; P14756; -.
PRO; PR:P14756; -.
Proteomes; UP000002438; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:PseudoCAP.
GO; GO:0052051; P:interaction with host via protein secreted by type II secretion system; IDA:PseudoCAP.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
GO; GO:0006508; P:proteolysis; IDA:PseudoCAP.
GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
CDD; cd09597; M4_neutral_protease; 1.
InterPro; IPR011096; FTP_domain.
InterPro; IPR025711; PepSY.
InterPro; IPR023612; Peptidase_M4.
InterPro; IPR001570; Peptidase_M4_C_domain.
InterPro; IPR013856; Peptidase_M4_domain.
Pfam; PF07504; FTP; 1.
Pfam; PF03413; PepSY; 1.
Pfam; PF01447; Peptidase_M4; 1.
Pfam; PF02868; Peptidase_M4_C; 1.
PRINTS; PR00730; THERMOLYSIN.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Secreted; Signal;
Virulence; Zinc; Zymogen.
SIGNAL 1 23 {ECO:0000269|PubMed:1544509}.
CHAIN 24 498 Pro-elastase.
/FTId=PRO_0000431322.
PROPEP 24 197 {ECO:0000269|PubMed:1544509,
ECO:0000269|PubMed:2123831,
ECO:0000269|PubMed:3034864,
ECO:0000269|PubMed:9642203}.
/FTId=PRO_0000028616.
CHAIN 198 498 Elastase. {ECO:0000269|PubMed:1544509,
ECO:0000269|PubMed:1744034,
ECO:0000269|PubMed:2123831,
ECO:0000269|PubMed:3034864}.
/FTId=PRO_0000028617.
ACT_SITE 338 338 {ECO:0000305|PubMed:1899664}.
ACT_SITE 420 420 Proton donor.
{ECO:0000305|PubMed:1899664}.
METAL 333 333 Calcium. {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 337 337 Zinc; catalytic.
{ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 341 341 Zinc; catalytic.
{ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 361 361 Zinc; catalytic.
{ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 369 369 Calcium. {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 372 372 Calcium. {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 380 380 Calcium. {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
METAL 382 382 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
SITE 197 198 Cleavage; by autolysis.
{ECO:0000269|PubMed:1744034}.
DISULFID 227 255 {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.16, ECO:0000269|Ref.17}.
DISULFID 467 494 {ECO:0000269|PubMed:1899664,
ECO:0000269|Ref.17}.
VARIANT 75 75 Y -> T (in strain: PA103 and N-10).
VARIANT 102 102 Q -> R (in strain: PA103 and N-10).
VARIANT 185 185 T -> Y (in strain: PA103 and N-10).
VARIANT 211 211 K -> I (in strain: 569B).
VARIANT 241 241 S -> G (in strain: PA103 and N-10).
VARIANT 282 282 K -> D (in strain: PA103 and N-10).
VARIANT 325 325 M -> V (in strain: IFO 3455).
VARIANT 471 471 R -> S (in strain: PA103).
MUTAGEN 420 420 H->D,Y: Loss of proteolytic and
elastolytic activity; significantly
decreased processing of proelastase,
proelastase accumulates in the periplasm
(in E.coli).
{ECO:0000269|PubMed:1744034}.
STRAND 199 206 {ECO:0000244|PDB:1U4G}.
TURN 207 209 {ECO:0000244|PDB:1U4G}.
STRAND 210 214 {ECO:0000244|PDB:1U4G}.
TURN 215 217 {ECO:0000244|PDB:1EZM}.
STRAND 228 230 {ECO:0000244|PDB:1U4G}.
STRAND 232 238 {ECO:0000244|PDB:1U4G}.
HELIX 269 288 {ECO:0000244|PDB:1U4G}.
STRAND 292 295 {ECO:0000244|PDB:1U4G}.
STRAND 297 302 {ECO:0000244|PDB:1U4G}.
TURN 304 306 {ECO:0000244|PDB:1U4G}.
STRAND 310 312 {ECO:0000244|PDB:1U4G}.
STRAND 317 319 {ECO:0000244|PDB:1U4G}.
STRAND 324 327 {ECO:0000244|PDB:1U4G}.
HELIX 332 345 {ECO:0000244|PDB:1U4G}.
TURN 346 348 {ECO:0000244|PDB:1U4G}.
HELIX 354 376 {ECO:0000244|PDB:1U4G}.
STRAND 381 383 {ECO:0000244|PDB:3DBK}.
HELIX 385 387 {ECO:0000244|PDB:1U4G}.
STRAND 388 392 {ECO:0000244|PDB:1U4G}.
STRAND 394 399 {ECO:0000244|PDB:1U4G}.
HELIX 400 403 {ECO:0000244|PDB:1U4G}.
HELIX 410 412 {ECO:0000244|PDB:1U4G}.
HELIX 419 422 {ECO:0000244|PDB:1U4G}.
HELIX 424 434 {ECO:0000244|PDB:1U4G}.
HELIX 441 454 {ECO:0000244|PDB:1U4G}.
HELIX 462 475 {ECO:0000244|PDB:1U4G}.
HELIX 480 489 {ECO:0000244|PDB:1U4G}.
SEQUENCE 498 AA; 53687 MW; 4B6AA96A569D9615 CRC64;
MKKVSTLDLL FVAIMGVSPA AFAADLIDVS KLPSKAAQGA PGPVTLQAAV GAGGADELKA
IRSTTLPNGK QVTRYEQFHN GVRVVGEAIT EVKGPGKSVA AQRSGHFVAN IAADLPGSTT
AAVSAEQVLA QAKSLKAQGR KTENDKVELV IRLGENNIAQ LVYNVSYLIP GEGLSRPHFV
IDAKTGEVLD QWEGLAHAEA GGPGGNQKIG KYTYGSDYGP LIVNDRCEMD DGNVITVDMN
SSTDDSKTTP FRFACPTNTY KQVNGAYSPL NDAHFFGGVV FKLYRDWFGT SPLTHKLYMK
VHYGRSVENA YWDGTAMLFG DGATMFYPLV SLDVAAHEVS HGFTEQNSGL IYRGQSGGMN
EAFSDMAGEA AEFYMRGKND FLIGYDIKKG SGALRYMDQP SRDGRSIDNA SQYYNGIDVH
HSSGVYNRAF YLLANSPGWD TRKAFEVFVD ANRYYWTATS NYNSGACGVI RSAQNRNYSA
ADVTRAFSTV GVTCPSAL


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E1785r ELISA Atriopeptidase,Enkephalinase,Mme,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Rat,Rattus norvegicus,SFE,Skin fibroblast elastase 96T
E1785m ELISA kit Atriopeptidase,Enkephalinase,Mme,Mouse,Mus musculus,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elastase 96T
U1785r CLIA Atriopeptidase,Enkephalinase,Mme,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,Rat,Rattus norvegicus,SFE,Skin fibroblast elastase 96T
U1785m CLIA Atriopeptidase,Enkephalinase,Mme,Mouse,Mus musculus,NEP,Neprilysin,Neutral endopeptidase,Neutral endopeptidase 24.11,SFE,Skin fibroblast elastase 96T


 

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