ID PICP_PSESR Reviewed; 587 AA.
AC P42790;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Pseudomonalisin;
DE EC=3.4.21.100;
DE AltName: Full=Pepstatin-insensitive carboxyl proteinase;
DE AltName: Full=Pseudomonapepsin;
DE Flags: Precursor;
GN Name=pcp;
OS Pseudomonas sp. (strain 101) (Achromobacter parvulus T1).
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=33067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 216-224.
RX PubMed=7929375; DOI=10.1016/s0021-9258(18)47225-0;
RA Oda K., Takahashi T., Tokuda Y., Shibano Y., Takahashi S.;
RT "Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-
RT insensitive carboxyl proteinase gene from Pseudomonas sp. 101.";
RL J. Biol. Chem. 269:26518-26524(1994).
RN [2]
RP PROTEIN SEQUENCE OF 216-585.
RX PubMed=8576087; DOI=10.1093/oxfordjournals.jbchem.a124974;
RA Hayashi K., Izu H., Oda K., Fukuhara K., Matsuo M., Takano R., Hara S.;
RT "The primary structure of pepstatin-insensitive carboxyl proteinase
RT produced by Pseudomonas sp. No. 101.";
RL J. Biochem. 118:738-744(1995).
RN [3]
RP MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES, AND ACTIVE SITES.
RX PubMed=10488127; DOI=10.1074/jbc.274.39.27815;
RA Oyama H., Abe S., Ushiyama S., Takahashi S., Oda K.;
RT "Identification of catalytic residues of pepstatin-insensitive carboxyl
RT proteinases from prokaryotes by site-directed mutagenesis.";
RL J. Biol. Chem. 274:27815-27822(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 217-585.
RX PubMed=11747435; DOI=10.1021/bi011817n;
RA Wlodawer A., Li M., Gustchina A., Dauter Z., Uchida K., Oyama H.,
RA Goldfarb N.E., Dunn B.M., Oda K.;
RT "Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase.";
RL Biochemistry 40:15602-15611(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 216-587.
RX PubMed=11323721; DOI=10.1038/87610;
RA Wlodawer A., Li M., Dauter Z., Gustchina A., Uchida K., Oyama H.,
RA Dunn B.M., Oda K.;
RT "Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-
RT like enzymes.";
RL Nat. Struct. Biol. 8:442-446(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 216-585 IN COMPLEX WITH INHIBITOR,
RP AND CALCIUM-BINDING SITES.
RX PubMed=14733955; DOI=10.1016/j.bbrc.2003.12.130;
RA Wlodawer A., Li M., Gustchina A., Oyama H., Oda K., Beyer B.B.,
RA Clemente J., Dunn B.M.;
RT "Two inhibitor molecules bound in the active site of Pseudomonas sedolisin:
RT a model for the bi-product complex following cleavage of a peptide
RT substrate.";
RL Biochem. Biophys. Res. Commun. 314:638-645(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-
CC Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5.
CC A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO2)-Arg-
CC Leu.; EC=3.4.21.100;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Autocatalytically processed.
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DR EMBL; D37970; BAA07188.1; -; Genomic_DNA.
DR PDB; 1GA1; X-ray; 1.40 A; A=216-587.
DR PDB; 1GA4; X-ray; 1.40 A; A=216-587.
DR PDB; 1GA6; X-ray; 1.00 A; A=216-587.
DR PDB; 1NLU; X-ray; 1.30 A; A=216-585.
DR PDB; 6M8W; X-ray; 1.10 A; A=217-585.
DR PDB; 6M8Y; X-ray; 1.10 A; A=217-585.
DR PDB; 6M9C; X-ray; 1.80 A; A=218-585.
DR PDB; 6M9D; X-ray; 2.00 A; A=218-585.
DR PDB; 6M9F; X-ray; 1.30 A; A=218-585.
DR PDBsum; 1GA1; -.
DR PDBsum; 1GA4; -.
DR PDBsum; 1GA6; -.
DR PDBsum; 1NLU; -.
DR PDBsum; 6M8W; -.
DR PDBsum; 6M8Y; -.
DR PDBsum; 6M9C; -.
DR PDBsum; 6M9D; -.
DR PDBsum; 6M9F; -.
DR AlphaFoldDB; P42790; -.
DR SMR; P42790; -.
DR DrugBank; DB03660; 4-Iodo-L-phenylalanine.
DR DrugBank; DB03750; Isovaleric Acid.
DR DrugBank; DB03978; Tyrosinal.
DR MEROPS; S53.001; -.
DR KEGG; ag:BAA07188; -.
DR BRENDA; 3.4.21.100; 5085.
DR EvolutionaryTrace; P42790; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Metal-binding; Periplasm; Protease; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..215
FT /note="Removed in mature form"
FT /id="PRO_0000027362"
FT CHAIN 216..585
FT /note="Pseudomonalisin"
FT /id="PRO_0000027363"
FT PROPEP 586..587
FT /note="Removed in mature form"
FT /id="PRO_0000027364"
FT DOMAIN 219..583
FT /note="Peptidase S53"
FT REGION 276..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 295
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10488127"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10488127"
FT ACT_SITE 502
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10488127"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 352..391
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 240..252
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6M8W"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:1GA6"
FT TURN 390..395
FT /evidence="ECO:0007829|PDB:1GA6"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 413..423
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 501..518
FT /evidence="ECO:0007829|PDB:1GA6"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 527..536
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:1GA6"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:1GA6"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:1GA6"
FT HELIX 573..583
FT /evidence="ECO:0007829|PDB:1GA6"
SQ SEQUENCE 587 AA; 61073 MW; E193D8B2C225829A CRC64;
MKSSAAKQTV LCLNRYAVVA LPLAIASFAA FGASPASTLW APTDTKAFVT PAQVEARSAA
PLLELAAGET AHIVVSLKLR DEAQLKQLAQ AVNQPGNAQF GKFLKRRQFL SQFAPTEAQV
QAVVAHLRKN GFVNIHVVPN RLLISADGSA GAVKAAFNTP LVRYQLNGKA GYANTAPAQV
PQDLGEIVGS VLGLQNVTRA HPMLKVGERS AAKTLAAGTA KGHNPTEFPT IYDASSAPTA
ANTTVGIITI GGVSQTLQDL QQFTSANGLA SVNTQTIQTG SSNGDYSDDQ QGQGEWDLDS
QSIVGSAGGA VQQLLFYMAD QSASGNTGLT QAFNQAVSDN VAKVINVSLG WCEADANADG
TLQAEDRIFA TAAAQGQTFS VSSGDEGVYE CNNRGYPDGS TYSVSWPASS PNVIAVGGTT
LYTTSAGAYS NETVWNEGLD SNGKLWATGG GYSVYESKPS WQSVVSGTPG RRLLPDISFD
AAQGTGALIY NYGQLQQIGG TSLASPIFVG LWARLQSANS NSLGFPAASF YSAISSTPSL
VHDVKSGNNG YGGYGYNAGT GWDYPTGWGS LDIAKLSAYI RSNGFGH
//
