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P42790 (PICP_PSESR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Pseudomonalisin

EC=3.4.21.100
Alternative name(s):
Pepstatin-insensitive carboxyl proteinase
Pseudomonapepsin
Gene names
Name:pcp
OrganismPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Taxonomic identifier33067 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO2)-Arg-Leu.

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Periplasm.

Post-translational modification

Autocatalytically processed.

Sequence similarities

Contains 1 peptidase S53 domain.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Propeptide? – 215Removed in mature formPRO_0000027362
Chain216 – 585370Pseudomonalisin
PRO_0000027363
Propeptide586 – 5872Removed in mature form
PRO_0000027364

Regions

Domain219 – 583365Peptidase S53

Sites

Active site2951Charge relay system Ref.3
Active site2991Charge relay system Ref.3
Active site5021Charge relay system Ref.3
Metal binding5431Calcium
Metal binding5441Calcium; via carbonyl oxygen
Metal binding5591Calcium; via carbonyl oxygen
Metal binding5611Calcium; via carbonyl oxygen
Metal binding5631Calcium

Amino acid modifications

Disulfide bond352 ↔ 391

Secondary structure

.................................................................. 587
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42790 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E193D8B2C225829A

FASTA58761,073
        10         20         30         40         50         60 
MKSSAAKQTV LCLNRYAVVA LPLAIASFAA FGASPASTLW APTDTKAFVT PAQVEARSAA 

        70         80         90        100        110        120 
PLLELAAGET AHIVVSLKLR DEAQLKQLAQ AVNQPGNAQF GKFLKRRQFL SQFAPTEAQV 

       130        140        150        160        170        180 
QAVVAHLRKN GFVNIHVVPN RLLISADGSA GAVKAAFNTP LVRYQLNGKA GYANTAPAQV 

       190        200        210        220        230        240 
PQDLGEIVGS VLGLQNVTRA HPMLKVGERS AAKTLAAGTA KGHNPTEFPT IYDASSAPTA 

       250        260        270        280        290        300 
ANTTVGIITI GGVSQTLQDL QQFTSANGLA SVNTQTIQTG SSNGDYSDDQ QGQGEWDLDS 

       310        320        330        340        350        360 
QSIVGSAGGA VQQLLFYMAD QSASGNTGLT QAFNQAVSDN VAKVINVSLG WCEADANADG 

       370        380        390        400        410        420 
TLQAEDRIFA TAAAQGQTFS VSSGDEGVYE CNNRGYPDGS TYSVSWPASS PNVIAVGGTT 

       430        440        450        460        470        480 
LYTTSAGAYS NETVWNEGLD SNGKLWATGG GYSVYESKPS WQSVVSGTPG RRLLPDISFD 

       490        500        510        520        530        540 
AAQGTGALIY NYGQLQQIGG TSLASPIFVG LWARLQSANS NSLGFPAASF YSAISSTPSL 

       550        560        570        580 
VHDVKSGNNG YGGYGYNAGT GWDYPTGWGS LDIAKLSAYI RSNGFGH 

« Hide

References

[1]"Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101."
Oda K., Takahashi T., Tokuda Y., Shibano Y., Takahashi S.
J. Biol. Chem. 269:26518-26524(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 216-224.
[2]"The primary structure of pepstatin-insensitive carboxyl proteinase produced by Pseudomonas sp. No. 101."
Hayashi K., Izu H., Oda K., Fukuhara K., Matsuo M., Takano R., Hara S.
J. Biochem. 118:738-744(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 216-585.
[3]"Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis."
Oyama H., Abe S., Ushiyama S., Takahashi S., Oda K.
J. Biol. Chem. 274:27815-27822(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES, ACTIVE SITES.
[4]"Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase."
Wlodawer A., Li M., Gustchina A., Dauter Z., Uchida K., Oyama H., Goldfarb N.E., Dunn B.M., Oda K.
Biochemistry 40:15602-15611(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 216-585.
[5]"Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes."
Wlodawer A., Li M., Dauter Z., Gustchina A., Uchida K., Oyama H., Dunn B.M., Oda K.
Nat. Struct. Biol. 8:442-446(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 216-587.
[6]"Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate."
Wlodawer A., Li M., Gustchina A., Oyama H., Oda K., Beyer B.B., Clemente J., Dunn B.M.
Biochem. Biophys. Res. Commun. 314:638-645(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 216-585 IN COMPLEX WITH INHIBITOR, CALCIUM-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37970 Genomic DNA. Translation: BAA07188.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GA1X-ray1.40A216-587[»]
1GA4X-ray1.40A216-587[»]
1GA6X-ray1.00A216-587[»]
1KDVX-ray1.10A216-585[»]
1KDYX-ray1.10A216-585[»]
1KDZX-ray1.40A216-585[»]
1KE1X-ray1.80A216-585[»]
1KE2X-ray2.00A216-585[»]
1NLUX-ray1.30A216-585[»]
ProteinModelPortalP42790.
SMRP42790. Positions 218-587.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS53.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR023828. Peptidase_S8_Ser-AS.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEPS51695. SEDOLISIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP42790.

Entry information

Entry namePICP_PSESR
AccessionPrimary (citable) accession number: P42790
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 22, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references