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Protein

Elastase

Gene

lasB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+3 PublicationsNote: Binds 1 Ca2+ ion per subunit.3 Publications
  • Zn2+3 PublicationsNote: Binds 1 Zn2+ ion per subunit.3 Publications

Enzyme regulationi

Inhibited by phosphoramidon.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi333 – 3331Calcium3 Publications
Metal bindingi337 – 3371Zinc; catalytic3 Publications
Active sitei338 – 33811 Publication
Metal bindingi341 – 3411Zinc; catalytic3 Publications
Metal bindingi361 – 3611Zinc; catalytic3 Publications
Metal bindingi369 – 3691Calcium3 Publications
Metal bindingi372 – 3721Calcium3 Publications
Metal bindingi380 – 3801Calcium3 Publications
Metal bindingi382 – 3821Calcium; via carbonyl oxygen3 Publications
Active sitei420 – 4201Proton donor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Virulence

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14569.
BRENDAi3.4.24.26. 5087.

Protein family/group databases

MEROPSiM04.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Elastase (EC:3.4.24.26)
Alternative name(s):
Neutral metalloproteinase
PAE1 Publication
Pseudolysin
Cleaved into the following chain:
Gene namesi
Name:lasB
Ordered Locus Names:PA3724
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3724.

Subcellular locationi

  • Secreted 3 Publications

  • Note: Secreted in an Xcp-dependent fashion (a type II secretion pathway).1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

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).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi420 – 4201H → D or Y: Loss of proteolytic and elastolytic activity; significantly decreased processing of proelastase, proelastase accumulates in the periplasm (in E.coli). 1 Publication

Chemistry

ChEMBLiCHEMBL1075146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 498475Pro-elastasePRO_0000431322Add
BLAST
Propeptidei24 – 1971744 PublicationsPRO_0000028616Add
BLAST
Chaini198 – 498301Elastase4 PublicationsPRO_0000028617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi227 ↔ 2553 Publications
Disulfide bondi467 ↔ 4942 Publications

Post-translational modificationi

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).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei197 – 1982Cleavage; by autolysis1 Publication

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Zymogen

Proteomic databases

PaxDbiP14756.

Miscellaneous databases

PMAP-CutDBP14756.

Expressioni

Inductioni

Optimal protein expression in vivo requires both Zn2+ and Ca2+ during growth (at protein level).2 Publications

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA3724.

Chemistry

BindingDBiP14756.

Structurei

Secondary structure

1
498
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi199 – 2068Combined sources
Turni207 – 2093Combined sources
Beta strandi210 – 2145Combined sources
Turni215 – 2173Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi232 – 2387Combined sources
Helixi269 – 28820Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi297 – 3026Combined sources
Turni304 – 3063Combined sources
Beta strandi310 – 3123Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi324 – 3274Combined sources
Helixi332 – 34514Combined sources
Turni346 – 3483Combined sources
Helixi354 – 37623Combined sources
Beta strandi381 – 3833Combined sources
Helixi385 – 3873Combined sources
Beta strandi388 – 3925Combined sources
Beta strandi394 – 3996Combined sources
Helixi400 – 4034Combined sources
Helixi410 – 4123Combined sources
Helixi419 – 4224Combined sources
Helixi424 – 43411Combined sources
Helixi441 – 45414Combined sources
Helixi462 – 47514Combined sources
Helixi480 – 48910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZMX-ray1.50A198-498[»]
1U4GX-ray1.40A198-498[»]
3DBKX-ray1.40A198-498[»]
ProteinModelPortaliP14756.
SMRiP14756. Positions 44-495.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14756.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105D4Y. Bacteria.
COG3227. LUCA.
HOGENOMiHOG000272374.
InParanoidiP14756.
KOiK01399.
OMAiYWVMVSG.
OrthoDBiEOG6DJXWM.
PhylomeDBiP14756.

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVSTLDLL FVAIMGVSPA AFAADLIDVS KLPSKAAQGA PGPVTLQAAV
60 70 80 90 100
GAGGADELKA IRSTTLPNGK QVTRYEQFHN GVRVVGEAIT EVKGPGKSVA
110 120 130 140 150
AQRSGHFVAN IAADLPGSTT AAVSAEQVLA QAKSLKAQGR KTENDKVELV
160 170 180 190 200
IRLGENNIAQ LVYNVSYLIP GEGLSRPHFV IDAKTGEVLD QWEGLAHAEA
210 220 230 240 250
GGPGGNQKIG KYTYGSDYGP LIVNDRCEMD DGNVITVDMN SSTDDSKTTP
260 270 280 290 300
FRFACPTNTY KQVNGAYSPL NDAHFFGGVV FKLYRDWFGT SPLTHKLYMK
310 320 330 340 350
VHYGRSVENA YWDGTAMLFG DGATMFYPLV SLDVAAHEVS HGFTEQNSGL
360 370 380 390 400
IYRGQSGGMN EAFSDMAGEA AEFYMRGKND FLIGYDIKKG SGALRYMDQP
410 420 430 440 450
SRDGRSIDNA SQYYNGIDVH HSSGVYNRAF YLLANSPGWD TRKAFEVFVD
460 470 480 490
ANRYYWTATS NYNSGACGVI RSAQNRNYSA ADVTRAFSTV GVTCPSAL
Length:498
Mass (Da):53,687
Last modified:April 1, 1990 - v1
Checksum:i4B6AA96A569D9615
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751Y → T in strain: PA103 and N-10.
Natural varianti102 – 1021Q → R in strain: PA103 and N-10.
Natural varianti185 – 1851T → Y in strain: PA103 and N-10.
Natural varianti211 – 2111K → I in strain: 569B.
Natural varianti241 – 2411S → G in strain: PA103 and N-10.
Natural varianti282 – 2821K → D in strain: PA103 and N-10.
Natural varianti325 – 3251M → V in strain: IFO 3455.
Natural varianti471 – 4711R → S in strain: PA103.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19472 Genomic DNA. Translation: AAB36615.1.
M24531 Genomic DNA. Translation: AAA25811.1.
AB029328 Genomic DNA. Translation: BAB79621.1.
AE004091 Genomic DNA. Translation: AAG07111.1.
PIRiA32359. HYBSPA.
RefSeqiNP_252413.1. NC_002516.2.
WP_003113835.1. NZ_ASJY01000598.1.

Genome annotation databases

EnsemblBacteriaiAAG07111; AAG07111; PA3724.
GeneIDi880368.
KEGGipae:PA3724.
PATRICi19842075. VBIPseAer58763_3895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19472 Genomic DNA. Translation: AAB36615.1.
M24531 Genomic DNA. Translation: AAA25811.1.
AB029328 Genomic DNA. Translation: BAB79621.1.
AE004091 Genomic DNA. Translation: AAG07111.1.
PIRiA32359. HYBSPA.
RefSeqiNP_252413.1. NC_002516.2.
WP_003113835.1. NZ_ASJY01000598.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZMX-ray1.50A198-498[»]
1U4GX-ray1.40A198-498[»]
3DBKX-ray1.40A198-498[»]
ProteinModelPortaliP14756.
SMRiP14756. Positions 44-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3724.

Chemistry

BindingDBiP14756.
ChEMBLiCHEMBL1075146.

Protein family/group databases

MEROPSiM04.005.

Proteomic databases

PaxDbiP14756.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07111; AAG07111; PA3724.
GeneIDi880368.
KEGGipae:PA3724.
PATRICi19842075. VBIPseAer58763_3895.

Organism-specific databases

PseudoCAPiPA3724.

Phylogenomic databases

eggNOGiENOG4105D4Y. Bacteria.
COG3227. LUCA.
HOGENOMiHOG000272374.
InParanoidiP14756.
KOiK01399.
OMAiYWVMVSG.
OrthoDBiEOG6DJXWM.
PhylomeDBiP14756.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14569.
BRENDAi3.4.24.26. 5087.

Miscellaneous databases

EvolutionaryTraceiP14756.
PMAP-CutDBP14756.

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene."
    Bever R.A., Iglewski B.H.
    J. Bacteriol. 170:4309-4314(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: PAO.
  2. "Structural gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase."
    Fukushima J., Yamamoto S., Morihara K., Atsumi Y., Takeuchi H., Kawamoto S., Okuda K.
    J. Bacteriol. 171:1698-1704(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NBRC 13130 / JCM 20134.
  3. "Detection of elastase production in Escherichia coli with the elastase structural gene from several non-elastase-producing strains of Pseudomonas aeruginosa."
    Tanaka E., Kawamoto S., Fukushima J., Hamajima K., Onishi H., Miyagi Y., Inami S., Morihara K., Okuda K.
    J. Bacteriol. 173:6153-6158(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29260 / PA103 and N-10.
  4. "Cloning and sequencing of a gene of organic solvent-stable protease secreted from Pseudomonas aeruginosa PST-01 and its expression in Escherichia coli."
    Ogino H., Yokoo J., Watanabe F., Ishikawa H.
    Biochem. Eng. J. 5:191-200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: PST-01.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  6. "Identification of cleavage sites involved in proteolytic processing of Pseudomonas aeruginosa preproelastase."
    Kessler E., Safrin M., Peretz M., Burstein Y.
    FEBS Lett. 299:291-293(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-28 AND 198-212.
  7. "Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa."
    Braun P., de Groot A., Bitter W., Tommassen J.
    J. Bacteriol. 180:3467-3469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-28, FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, DISRUPTION PHENOTYPE.
    Strain: PAO1 / PAO25.
  8. "Cloning and characterization of elastase genes from Pseudomonas aeruginosa."
    Schad P.A., Bever R.A., Nicas T.I., Leduc F., Hanne L.F., Iglewski B.H.
    J. Bacteriol. 169:2691-2696(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 198-237.
    Strain: PAO.
  9. "Comparison of the Vibrio cholerae hemagglutinin/protease and the Pseudomonas aeruginosa elastase."
    Haese C.C., Finkelstein R.A.
    Infect. Immun. 58:4011-4015(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 198-217.
    Strain: 569B.
  10. "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."
    McIver K., Kessler E., Ohman D.E.
    J. Bacteriol. 173:7781-7789(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 198-212, FUNCTION, EXPRESSION IN E.COLI, MUTAGENESIS OF HIS-420.
    Strain: FRD1.
  11. "Biofouling in water treatment systems: effect of membrane properties on biofilm formation."
    Liddor M.
    Thesis (2005), Ben-Gurion University, Israel
    Cited for: PROTEIN SEQUENCE OF 212-226; 354-376 AND 429-442.
    Strain: ATCC 33467 / type 1 smooth and ATCC 33468 / type 2 mucoid.
  12. "Synthesis, processing, and transport of Pseudomonas aeruginosa elastase."
    Kessler E., Safrin M.
    J. Bacteriol. 170:5241-5247(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION, PROTEOLYTIC CLEAVAGE.
    Strain: Habs serotype I.
  13. "Efficient production and processing of elastase and LasA by Pseudomonas aeruginosa require zinc and calcium ions."
    Olson J.C., Ohman D.E.
    J. Bacteriol. 174:4140-4147(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228, DG1 and FRD1 / FRD2.
  14. "A secreted aminopeptidase of Pseudomonas aeruginosa. Identification, primary structure, and relationship to other aminopeptidases."
    Cahan R., Axelrad I., Safrin M., Ohman D.E., Kessler E.
    J. Biol. Chem. 276:43645-43652(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228, FRD1 and Habs serotype 1.
  15. "Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution."
    Thayer M.M., Flaherty K.M., McKay D.B.
    J. Biol. Chem. 266:2864-2871(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 198-498 IN COMPLEX WITH CALCIUM AND ZINC, COFACTOR, SUBUNIT, DISULFIDE BOND, ACTIVE SITE.
  16. "Elastase of Pseudomonas aeruginosa with an inhibitor."
    Bitto E., McKay D.B.
    Submitted (JUL-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 198-498 IN COMPLEX WITH CALCIUM AND ZINC AND AN INHIBITOR, COFACTOR, DISULFIDE BOND.
  17. "Structure of the elastase of Pseudomonas aeruginosa complexed with phosphoramidon."
    Overgaard M.T., McKay D.B.
    Submitted (JUN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 198-498 IN COMPLEX WITH CALCIUM AND ZINC AND AN INHIBITOR, COFACTOR, DISULFIDE BOND.

Entry informationi

Entry nameiELAS_PSEAE
AccessioniPrimary (citable) accession number: P14756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 9, 2015
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.