API_ACHLY
ID API_ACHLY Reviewed; 653 AA.
AC P15636;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protease 1;
DE EC=3.4.21.50;
DE AltName: Full=API;
DE AltName: Full=Lysyl endopeptidase;
DE AltName: Full=Protease I;
DE Flags: Precursor;
OS Achromobacter lyticus.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=224;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M497-1;
RX PubMed=2684982; DOI=10.1016/s0021-9258(19)47109-3;
RA Ohara T., Makino K., Shinagawa H., Nakata A., Norioka S., Sakiyama F.;
RT "Cloning, nucleotide sequence, and expression of Achromobacter protease I
RT gene.";
RL J. Biol. Chem. 264:20625-20631(1989).
RN [2]
RP PROTEIN SEQUENCE OF 206-473, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF
RP 206-473, AND DISULFIDE BOND.
RC STRAIN=M497-1;
RX PubMed=2492988; DOI=10.1016/s0021-9258(19)84926-8;
RA Tsunasawa S., Masaki T., Hirose M., Soejima M., Sakiyama F.;
RT "The primary structure and structural characteristics of Achromobacter
RT lyticus protease I, a lysine-specific serine protease.";
RL J. Biol. Chem. 264:3832-3839(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.;
CC EC=3.4.21.50;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The C-terminal extension has little effect on the function of
CC API.
CC -!- PTM: Three disulfide bonds are present. {ECO:0000269|PubMed:2492988}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; J05128; AAA78946.1; -; Genomic_DNA.
DR PIR; A32687; A32687.
DR PDB; 1ARB; X-ray; 1.20 A; A=206-473.
DR PDB; 1ARC; X-ray; 2.00 A; A=206-473.
DR PDB; 4GPG; Other; 1.90 A; A=206-473.
DR PDBsum; 1ARB; -.
DR PDBsum; 1ARC; -.
DR PDBsum; 4GPG; -.
DR AlphaFoldDB; P15636; -.
DR SMR; P15636; -.
DR DrugBank; DB08603; N-[(1S)-5-amino-1-(chloroacetyl)pentyl]-4-methylbenzenesulfonamide.
DR MEROPS; S01.280; -.
DR PRIDE; P15636; -.
DR KEGG; ag:AAA78946; -.
DR BRENDA; 3.4.21.50; 74.
DR EvolutionaryTrace; P15636; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR017323; Lysyl_endo-pept.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR Pfam; PF01483; P_proprotein; 1.
DR PIRSF; PIRSF037930; Lysyl_endopeptidase; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49299; SSF49299; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS50093; PKD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /note="Or 27"
FT /evidence="ECO:0000255"
FT PROPEP 21..205
FT /evidence="ECO:0000269|PubMed:2492988"
FT /id="PRO_0000028515"
FT CHAIN 206..473
FT /note="Protease 1"
FT /id="PRO_0000028516"
FT PROPEP 474..653
FT /note="Thr/Ser-rich"
FT /id="PRO_0000028517"
FT DOMAIN 474..553
FT /note="PKD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 555..653
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 211..421
FT /evidence="ECO:0000269|PubMed:2492988"
FT DISULFID 217..285
FT /evidence="ECO:0000269|PubMed:2492988"
FT DISULFID 241..263
FT /evidence="ECO:0000269|PubMed:2492988"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1ARB"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 435..440
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:1ARB"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:1ARB"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1ARB"
SQ SEQUENCE 653 AA; 68125 MW; 3A55159247EFFE7C CRC64;
MKRICGSLLL LGLSISAALA APASRPAAFD YANLSSVDKV ALRTMPAVDV AKAKAEDLQR
DKRGDIPRFA LAIDVDMTPQ NSGAWEYTAD GQFAVWRQRV RSEKALSLNF GFTDYYMPAG
GRLLVYPATQ APAGDRGLIS QYDASNNNSA RQLWTAVVPG AEAVIEAVIP RDKVGEFKLR
LTKVNHDYVG FGPLARRLAA ASGEKGVSGS CNIDVVCPEG DGRRDIIRAV GAYSKSGTLA
CTGSLVNNTA NDRKMYFLTA HHCGMGTAST AASIVVYWNY QNSTCRAPNT PASGANGDGS
MSQTQSGSTV KATYATSDFT LLELNNAANP AFNLFWAGWD RRDQNYPGAI AIHHPNVAEK
RISNSTSPTS FVAWGGGAGT THLNVQWQPS GGVTEPGSSG SPIYSPEKRV LGQLHGGPSS
CSATGTNRSD QYGRVFTSWT GGGAAASRLS DWLDPASTGA QFIDGLDSGG GTPNTPPVAN
FTSTTSGLTA TFTDSSTDSD GSIASRSWNF GDGSTSTATN PSKTYAAAGT YTVTLTVTDN
GGATNTKTGS VTVSGGPGAQ TYTNDTDVAI PDNATVESPI TVSGRTGNGS ATTPIQVTIY
HTYKSDLKVD LVAPDGTVYN LHNRTGGSAH NIIQTFTKDL SSEAAQRAPG SCG
