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Protein

Elastase

Gene

lasB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi333Calcium3 Publications1
Metal bindingi337Zinc; catalytic3 Publications1
Active sitei3381 Publication1
Metal bindingi341Zinc; catalytic3 Publications1
Metal bindingi361Zinc; catalytic3 Publications1
Metal bindingi369Calcium3 Publications1
Metal bindingi372Calcium3 Publications1
Metal bindingi380Calcium3 Publications1
Metal bindingi382Calcium; via carbonyl oxygen3 Publications1
Active sitei420Proton donor1 Publication1

GO - Molecular functioni

GO - Biological processi

  • bacterial-type flagellum-dependent swarming motility Source: PseudoCAP
  • interaction with host via protein secreted by type II secretion system Source: PseudoCAP
  • pathogenesis Source: UniProtKB-KW
  • protein secretion by the type II secretion system Source: PseudoCAP
  • protein transport by the Sec complex Source: PseudoCAP
  • proteolysis Source: PseudoCAP
  • single-species biofilm formation Source: PseudoCAP

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processVirulence
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14569
PAER208964:G1FZ6-3794-MONOMER
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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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

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)DescriptionActionsGraphical viewLength
Mutagenesisi420H → D or Y: Loss of proteolytic and elastolytic activity; significantly decreased processing of proelastase, proelastase accumulates in the periplasm (in E.coli). 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075146
DrugBankiDB02307 N-(1-Carboxy-3-Phenylpropyl)Phenylalanyl-Alpha-Asparagine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000043132224 – 498Pro-elastaseAdd BLAST475
PropeptideiPRO_000002861624 – 1974 PublicationsAdd BLAST174
ChainiPRO_0000028617198 – 498Elastase4 PublicationsAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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)DescriptionActionsGraphical viewLength
Sitei197 – 198Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Zymogen

Proteomic databases

PaxDbiP14756
PRIDEiP14756

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 databases

BindingDBiP14756

Structurei

Secondary structure

1498
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi199 – 206Combined sources8
Turni207 – 209Combined sources3
Beta strandi210 – 214Combined sources5
Turni215 – 217Combined sources3
Beta strandi228 – 230Combined sources3
Beta strandi232 – 238Combined sources7
Helixi269 – 288Combined sources20
Beta strandi292 – 295Combined sources4
Beta strandi297 – 302Combined sources6
Turni304 – 306Combined sources3
Beta strandi310 – 312Combined sources3
Beta strandi317 – 319Combined sources3
Beta strandi324 – 327Combined sources4
Helixi332 – 345Combined sources14
Turni346 – 348Combined sources3
Helixi354 – 376Combined sources23
Beta strandi381 – 383Combined sources3
Helixi385 – 387Combined sources3
Beta strandi388 – 392Combined sources5
Beta strandi394 – 399Combined sources6
Helixi400 – 403Combined sources4
Helixi410 – 412Combined sources3
Helixi419 – 422Combined sources4
Helixi424 – 434Combined sources11
Helixi441 – 454Combined sources14
Helixi462 – 475Combined sources14
Helixi480 – 489Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EZMX-ray1.50A198-498[»]
1U4GX-ray1.40A198-498[»]
3DBKX-ray1.40A198-498[»]
ProteinModelPortaliP14756
SMRiP14756
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
OMAiHKRTTLA
PhylomeDBiP14756

Family and domain databases

CDDicd09597 M4_neutral_protease, 1 hit
Gene3Di1.10.390.10, 1 hit
InterProiView protein in InterPro
IPR011096 FTP_domain
IPR025711 PepSY
IPR023612 Peptidase_M4
IPR027268 Peptidase_M4/M1_CTD_sf
IPR001570 Peptidase_M4_C_domain
IPR013856 Peptidase_M4_domain
PfamiView protein in Pfam
PF07504 FTP, 1 hit
PF03413 PepSY, 1 hit
PF01447 Peptidase_M4, 1 hit
PF02868 Peptidase_M4_C, 1 hit
PRINTSiPR00730 THERMOLYSIN
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

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)DescriptionActionsGraphical viewLength
Natural varianti75Y → T in strain: PA103 and N-10. 1
Natural varianti102Q → R in strain: PA103 and N-10. 1
Natural varianti185T → Y in strain: PA103 and N-10. 1
Natural varianti211K → I in strain: 569B. 1
Natural varianti241S → G in strain: PA103 and N-10. 1
Natural varianti282K → D in strain: PA103 and N-10. 1
Natural varianti325M → V in strain: IFO 3455. 1
Natural varianti471R → S in strain: PA103. 1

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, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG07111; AAG07111; PA3724
GeneIDi880368
KEGGipae:PA3724
PATRICifig|208964.12.peg.3895

Similar proteinsi

Entry informationi

Entry nameiELAS_PSEAE
AccessioniPrimary (citable) accession number: P14756
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: March 28, 2018
This is version 159 of the entry and version 1 of the sequence. See 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

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