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Q9HWK6 (LYSC_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysyl endopeptidase

EC=3.4.21.50
Alternative name(s):
Protease IV
pvdS-regulated endoprotease
Gene names
Name:prpL
Ordered Locus Names:PA4175
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lysine-specific endoprotease. Involved in corneal virulence.

Catalytic activity

Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase S1 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 211187
PRO_0000228678
Chain212 – 462251Lysyl endopeptidase
PRO_0000228679

Sites

Active site2831Charge relay system By similarity
Active site3331Charge relay system By similarity
Active site4091Charge relay system By similarity

Amino acid modifications

Disulfide bond224 ↔ 435 By similarity
Disulfide bond230 ↔ 305 By similarity
Disulfide bond262 ↔ 284 By similarity

Experimental info

Mutagenesis2831H → A: Loss of activity. Ref.1
Mutagenesis3271H → A: No loss of activity. Ref.1
Mutagenesis3331D → A: Loss of activity. Ref.1
Mutagenesis4081S → A: Loss of activity. Ref.1
Mutagenesis4091S → A: Loss of activity. Ref.1
Mutagenesis4111S → A: No loss of activity. Ref.1
Sequence conflict231L → S in AAL47683. Ref.1
Sequence conflict571I → T in AAL47683. Ref.1
Sequence conflict1021T → A in AAL47683. Ref.1
Sequence conflict1371H → R Ref.1
Sequence conflict1371H → R Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9HWK6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 8988A6AE53E9C816

FASTA46248,213
        10         20         30         40         50         60 
MHKRTYLNAC LVLALAAGAS QALAAPGASE MAGDVAVLQA SPASTGHARF ANPNAAISAA 

        70         80         90        100        110        120 
GIHFAAPPAR RVARAAPLAP KPGTPLQVGV GLKTATPEID LTTLEWIDTP DGRHTARFPI 

       130        140        150        160        170        180 
SAAGAASLRA AIRLETHSGS LPDDVLLHFA GAGKEIFEAS GKDLSVNRPY WSPVIEGDTL 

       190        200        210        220        230        240 
TVELVLPANL QPGDLRLSVP QVSYFADSLY KAGYRDGFGA SGSCEVDAVC ATQSGTRAYD 

       250        260        270        280        290        300 
NATAAVAKMV FTSSADGGSY ICTGTLLNNG NSPKRQLFWS AAHCIEDQAT AATLQTIWFY 

       310        320        330        340        350        360 
NTTQCYGDAS TINQSVTVLT GGANILHRDA KRDTLLLELK RTPPAGVFYQ GWSATPIANG 

       370        380        390        400        410        420 
SLGHDIHHPR GDAKKYSQGN VSAVGVTYDG HTALTRVDWP SAVVEGGSSG SGLLTVAGDG 

       430        440        450        460 
SYQLRGGLYG GPSYCGAPTS QRNDYFSDFS GVYSQISRYF AP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the active site residues of Pseudomonas aeruginosa protease IV. Importance of enzyme activity in autoprocessing and activation."
Traidej M., Marquart M.E., Caballero A.R., Thibodeaux B.A., O'Callaghan R.J.
J. Biol. Chem. 278:2549-2553(2003) [PubMed: 12419815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF HIS-283; HIS-327; ASP-333; SER-408; SER-409 AND SER-411.
Strain: PA103-29.
[2]"PrpL protease of Pseudomonas aeruginosa: an important virulence determinant in corneal infections."
Parveen N., Parker D.S., Fan L., Leong J.M., Goguen J.D.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PA4481.
[3]"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. expand/collapse author list , 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.
[4]Lahnstein J.
Submitted (APR-2000) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 212-226.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY062882 Genomic DNA. Translation: AAL47683.1.
AY850373 Genomic DNA. Translation: AAW33983.1.
AE004091 Genomic DNA. Translation: AAG07562.1.
PIRB83123.
RefSeqNP_252864.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9HWK6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880208.
GenomeReviewsGene locus PA4175 in contig AE004091_GR.
KEGGpae:PA4175.
NMPDRfig|208964.1.peg.4174.
PATRIC19843036. VBIPseAer58763_4374.

Organism-specific databases

PseudoCAPPA4175.

Phylogenomic databases

HOGENOMHBG752136.
OMAPIANGSL.
ProtClustDBCLSK2297761.

Enzyme and pathway databases

BioCycPAER208964:PA4175-MONOMER.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLYSC_PSEAE
AccessionPrimary (citable) accession number: Q9HWK6
Secondary accession number(s): P82468, Q5I6A6, Q8VPA4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families