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P42790

- PICP_PSESR

UniProt

P42790 - PICP_PSESR

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Protein
Pseudomonalisin
Gene
pcp
Organism
Pseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Cofactori

Binds 1 calcium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei295 – 2951Charge relay system1 Publication
Active sitei299 – 2991Charge relay system1 Publication
Active sitei502 – 5021Charge relay system1 Publication
Metal bindingi543 – 5431Calcium
Metal bindingi544 – 5441Calcium; via carbonyl oxygen
Metal bindingi559 – 5591Calcium; via carbonyl oxygen
Metal bindingi561 – 5611Calcium; via carbonyl oxygen
Metal bindingi563 – 5631Calcium

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    MEROPSiS53.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pseudomonalisin (EC:3.4.21.100)
    Alternative name(s):
    Pepstatin-insensitive carboxyl proteinase
    Pseudomonapepsin
    Gene namesi
    Name:pcp
    OrganismiPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
    Taxonomic identifieri33067 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 215Removed in mature formPRO_0000027362
    Signal peptidei1 – ? Reviewed prediction
    Chaini216 – 585370Pseudomonalisin
    PRO_0000027363Add
    BLAST
    Propeptidei586 – 5872Removed in mature form
    PRO_0000027364

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi352 ↔ 391

    Post-translational modificationi

    Autocatalytically processed.

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi225 – 2273
    Helixi228 – 2314
    Beta strandi240 – 25213
    Helixi254 – 26613
    Beta strandi274 – 2785
    Helixi290 – 30617
    Beta strandi311 – 3199
    Beta strandi321 – 3244
    Helixi327 – 33913
    Beta strandi343 – 3475
    Helixi353 – 3586
    Helixi361 – 37414
    Beta strandi378 – 3825
    Turni390 – 3956
    Turni407 – 4093
    Beta strandi413 – 42311
    Beta strandi429 – 4346
    Beta strandi436 – 4394
    Beta strandi445 – 4473
    Beta strandi451 – 4577
    Helixi460 – 4645
    Beta strandi470 – 4745
    Beta strandi476 – 4805
    Helixi483 – 4853
    Beta strandi487 – 4915
    Beta strandi494 – 4985
    Helixi501 – 51818
    Turni519 – 5213
    Helixi527 – 53610
    Helixi538 – 5403
    Beta strandi548 – 5514
    Beta strandi560 – 5634
    Turni564 – 5663
    Helixi573 – 58311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP42790.
    SMRiP42790. Positions 218-587.

    Miscellaneous databases

    EvolutionaryTraceiP42790.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini219 – 583365Peptidase S53
    Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.200. 1 hit.
    InterProiIPR015366. Peptidase_S53_propep.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PfamiPF00082. Peptidase_S8. 1 hit.
    PF09286. Pro-kuma_activ. 1 hit.
    [Graphical view]
    SMARTiSM00944. Pro-kuma_activ. 1 hit.
    [Graphical view]
    SUPFAMiSSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEiPS51695. SEDOLISIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P42790-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSSAAKQTV LCLNRYAVVA LPLAIASFAA FGASPASTLW APTDTKAFVT    50
    PAQVEARSAA PLLELAAGET AHIVVSLKLR DEAQLKQLAQ AVNQPGNAQF 100
    GKFLKRRQFL SQFAPTEAQV QAVVAHLRKN GFVNIHVVPN RLLISADGSA 150
    GAVKAAFNTP LVRYQLNGKA GYANTAPAQV PQDLGEIVGS VLGLQNVTRA 200
    HPMLKVGERS AAKTLAAGTA KGHNPTEFPT IYDASSAPTA ANTTVGIITI 250
    GGVSQTLQDL QQFTSANGLA SVNTQTIQTG SSNGDYSDDQ QGQGEWDLDS 300
    QSIVGSAGGA VQQLLFYMAD QSASGNTGLT QAFNQAVSDN VAKVINVSLG 350
    WCEADANADG TLQAEDRIFA TAAAQGQTFS VSSGDEGVYE CNNRGYPDGS 400
    TYSVSWPASS PNVIAVGGTT LYTTSAGAYS NETVWNEGLD SNGKLWATGG 450
    GYSVYESKPS WQSVVSGTPG RRLLPDISFD AAQGTGALIY NYGQLQQIGG 500
    TSLASPIFVG LWARLQSANS NSLGFPAASF YSAISSTPSL VHDVKSGNNG 550
    YGGYGYNAGT GWDYPTGWGS LDIAKLSAYI RSNGFGH 587
    Length:587
    Mass (Da):61,073
    Last modified:November 1, 1995 - v1
    Checksum:iE193D8B2C225829A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37970 Genomic DNA. Translation: BAA07188.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37970 Genomic DNA. Translation: BAA07188.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GA1 X-ray 1.40 A 216-587 [» ]
    1GA4 X-ray 1.40 A 216-587 [» ]
    1GA6 X-ray 1.00 A 216-587 [» ]
    1KDV X-ray 1.10 A 216-585 [» ]
    1KDY X-ray 1.10 A 216-585 [» ]
    1KDZ X-ray 1.40 A 216-585 [» ]
    1KE1 X-ray 1.80 A 216-585 [» ]
    1KE2 X-ray 2.00 A 216-585 [» ]
    1NLU X-ray 1.30 A 216-585 [» ]
    ProteinModelPortali P42790.
    SMRi P42790. Positions 218-587.
    ModBasei Search...

    Protein family/group databases

    MEROPSi S53.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P42790.

    Family and domain databases

    Gene3Di 3.40.50.200. 1 hit.
    InterProi IPR015366. Peptidase_S53_propep.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    Pfami PF00082. Peptidase_S8. 1 hit.
    PF09286. Pro-kuma_activ. 1 hit.
    [Graphical view ]
    SMARTi SM00944. Pro-kuma_activ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEi PS51695. SEDOLISIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPICP_PSESR
    AccessioniPrimary (citable) accession number: P42790
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: May 14, 2014
    This is version 85 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, Direct protein sequencing

    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

    External Data

    Dasty 3

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