P14756 (ELAS_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pseudolysin
EC=3.4.24.26

Alternative name(s):
Elastase
Neutral metalloproteinase

Gene names

Name:	lasB
Ordered Locus Names:	PA3724

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves elastin, collagen, IgG, and several complement components. Involved in the pathogenesis of P.aeruginosa infections.
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	Binds 1 calcium ion per subunit. Binds 1 zinc ion per subunit.
Subcellular location	Secreted.
Miscellaneous	The sequence shown is that of strain PAO.
Sequence similarities	Belongs to the peptidase M4 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.6

Propeptide

24 – 197

174

PRO_0000028616

Chain

198 – 498

301

Pseudolysin

PRO_0000028617

Sites

Active site

338

1

Active site

420

1

Proton donor

Metal binding

333

1

Calcium Ref.10

Metal binding

337

1

Zinc; catalytic

Metal binding

341

1

Zinc; catalytic

Metal binding

361

1

Zinc; catalytic

Metal binding

369

1

Calcium Ref.10

Metal binding

372

1

Calcium Ref.10

Metal binding

380

1

Calcium Ref.10

Amino acid modifications

Disulfide bond

227 ↔ 255

Ref.10

Disulfide bond

467 ↔ 494

Ref.10

Natural variations

Natural variant

75

1

Y → T in strain: PA103 and N-10.

Natural variant

102

1

Q → R in strain: PA103 and N-10.

Natural variant

185

1

T → Y in strain: PA103 and N-10.

Natural variant

211

1

K → I in strain: 569B.

Natural variant

241

1

S → G in strain: PA103 and N-10.

Natural variant

282

1

K → D in strain: PA103 and N-10.

Natural variant

325

1

M → V in strain: IFO 3455.

Natural variant

471

1

R → S in strain: PA103.

Secondary structure

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498

Helix Strand Turn

Details...

Beta strand

199 – 206

8

Turn

207 – 209

3

Beta strand

210 – 214

5

Beta strand

228 – 230

3

Beta strand

232 – 238

7

Helix

269 – 288

20

Beta strand

292 – 295

4

Beta strand

297 – 302

6

Turn

304 – 306

3

Beta strand

310 – 312

3

Beta strand

317 – 319

3

Beta strand

324 – 327

4

Helix

332 – 345

14

Turn

346 – 348

3

Helix

354 – 376

23

Helix

385 – 387

3

Beta strand

388 – 392

5

Beta strand

394 – 399

6

Helix

400 – 403

4

Helix

410 – 412

3

Helix

419 – 422

4

Helix

424 – 434

11

Helix

441 – 454

14

Helix

462 – 475

14

Helix

480 – 489

10

Sequences

	Sequence		Length	Mass (Da)
	P14756 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 4B6AA96A569D9615	FASTA	498	53,687
	10 20 30 40 50 60 MKKVSTLDLL FVAIMGVSPA AFAADLIDVS KLPSKAAQGA PGPVTLQAAV GAGGADELKA 70 80 90 100 110 120 IRSTTLPNGK QVTRYEQFHN GVRVVGEAIT EVKGPGKSVA AQRSGHFVAN IAADLPGSTT 130 140 150 160 170 180 AAVSAEQVLA QAKSLKAQGR KTENDKVELV IRLGENNIAQ LVYNVSYLIP GEGLSRPHFV 190 200 210 220 230 240 IDAKTGEVLD QWEGLAHAEA GGPGGNQKIG KYTYGSDYGP LIVNDRCEMD DGNVITVDMN 250 260 270 280 290 300 SSTDDSKTTP FRFACPTNTY KQVNGAYSPL NDAHFFGGVV FKLYRDWFGT SPLTHKLYMK 310 320 330 340 350 360 VHYGRSVENA YWDGTAMLFG DGATMFYPLV SLDVAAHEVS HGFTEQNSGL IYRGQSGGMN 370 380 390 400 410 420 EAFSDMAGEA AEFYMRGKND FLIGYDIKKG SGALRYMDQP SRDGRSIDNA SQYYNGIDVH 430 440 450 460 470 480 HSSGVYNRAF YLLANSPGWD TRKAFEVFVD ANRYYWTATS NYNSGACGVI RSAQNRNYSA 490 ADVTRAFSTV GVTCPSAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2842313] [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: 2493453] [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: 1917848] [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: 10828420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PST-01.
[5]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." 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. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] 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: 1544509] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-28 AND 198-212.
[7]	"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: 3034864] [Abstract] Cited for: PROTEIN SEQUENCE OF 198-237. Strain: PAO.
[8]	"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: 2123831] [Abstract] Cited for: PROTEIN SEQUENCE OF 198-217. Strain: 569B.
[9]	"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.
[10]	"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: 1899664] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19472 Genomic DNA. Translation: AAB36615.1.
M24531 Genomic DNA. Translation: AAA25811.1.
AB029328 Genomic DNA. Translation: BAB79621.1.
AE004091 Genomic DNA. Translation: AAG07111.1.

PIR

HYBSPA. A32359.

RefSeq

NP_252413.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZM	X-ray	1.50	A	198-498	[»]
1U4G	X-ray	1.40	A	198-498	[»]
3DBK	X-ray	1.40	A	198-498	[»]

ProteinModelPortal

P14756.

SMR

P14756. Positions 198-495.

ModBase

Search...

Protein family/group databases

MEROPS

M04.005.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

880368.

GenomeReviews

Gene locus PA3724 in contig AE004091_GR.

KEGG

pae:PA3724.

NMPDR

fig|208964.1.peg.3723.

PATRIC

19842075. VBIPseAer58763_3895.

Organism-specific databases

PseudoCAP

PA3724.

Phylogenomic databases

HOGENOM

HBG563277.

OMA

RWEGINH.

ProtClustDB

CLSK868187.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14569.
PAER208964:PA3724-MONOMER.

Family and domain databases

InterPro

IPR011096. FTP_domain.
IPR005075. Pept_M4_propep_PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]

Gene3D

G3DSA:3.10.170.10. Peptidase_M4. 1 hit.
G3DSA:1.10.390.10. Peptidase_M4/M36. 1 hit.

KO

K01399.

Pfam

PF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]

PRINTS

PR00730. THERMOLYSIN.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

PMAP-CutDB

P14756.

Entry information

Entry name

ELAS_PSEAE

Accession

Primary (citable) accession number: P14756

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program