AQL1_THEAQ
ID AQL1_THEAQ Reviewed; 513 AA.
AC P08594;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Aqualysin-1;
DE EC=3.4.21.111;
DE AltName: Full=Aqualysin-I;
DE Flags: Precursor;
GN Name=pstI;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 15-23.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=2182621; DOI=10.1016/s0021-9258(19)39186-0;
RA Terada I., Kwon S.-T., Miyata Y., Matsuzawa H., Ohta T.;
RT "Unique precursor structure of an extracellular protease, aqualysin I, with
RT NH2- and COOH-terminal pro-sequences and its processing in Escherichia
RT coli.";
RL J. Biol. Chem. 265:6576-6581(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-442, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=3286255; DOI=10.1111/j.1432-1033.1988.tb14025.x;
RA Kwon S.-T., Terada I., Matsuzawa H., Ohta T.;
RT "Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline
RT serine protease) of Thermus aquaticus YT-1 and characteristics of the
RT deduced primary structure of the enzyme.";
RL Eur. J. Biochem. 173:491-497(1988).
RN [3]
RP PROTEIN SEQUENCE OF 128-170.
RX PubMed=3162211; DOI=10.1111/j.1432-1033.1988.tb13809.x;
RA Matsuzawa H., Tokugawa K., Hamaoki M., Mizoguchi M., Taguchi H., Terada I.,
RA Kwon S.-T., Ohta T.;
RT "Purification and characterization of aqualysin I (a thermophilic alkaline
RT serine protease) produced by Thermus aquaticus YT-1.";
RL Eur. J. Biochem. 171:441-447(1988).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=18216068; DOI=10.1093/jb/mvn007;
RA Sakaguchi M., Takezawa M., Nakazawa R., Nozawa K., Kusakawa T.,
RA Nagasawa T., Sugahara Y., Kawakita M.;
RT "Role of disulphide bonds in a thermophilic serine protease aqualysin I
RT from Thermus aquaticus YT-1.";
RL J. Biochem. 143:625-632(2008).
CC -!- FUNCTION: Aqualysin I is a thermophilic alkaline serine protease.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exhibits low specificity toward esters of amino acids with
CC small hydrophobic or aromatic residues at the P1 position.;
CC EC=3.4.21.111;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius for caseinolytic activity.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Secreted from the early stationary phase until the
CC time the cells cease to grow.
CC -!- PTM: The N- and C-terminal Pro-sequences are successively removed
CC through the proteolytic activity of PstI itself. The C-terminal Pro-
CC sequence is required for translocation of the proteases across the
CC outer membrane.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; D90108; BAA14135.1; -; Genomic_DNA.
DR EMBL; X07734; CAA30559.1; -; Genomic_DNA.
DR PIR; A35742; A35742.
DR PDB; 4DZT; X-ray; 1.95 A; A=128-403.
DR PDBsum; 4DZT; -.
DR AlphaFoldDB; P08594; -.
DR SMR; P08594; -.
DR MEROPS; S08.051; -.
DR KEGG; ag:BAA14135; -.
DR BioCyc; MetaCyc:MON-12998; -.
DR BRENDA; 3.4.21.111; 6334.
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 CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..14
FT /evidence="ECO:0000269|PubMed:2182621"
FT PROPEP 15..127
FT /evidence="ECO:0000269|PubMed:3162211"
FT /id="PRO_0000026992"
FT CHAIN 128..408
FT /note="Aqualysin-1"
FT /id="PRO_0000026993"
FT PROPEP 409..513
FT /id="PRO_0000026994"
FT DOMAIN 54..125
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 134..409
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DISULFID 194..226
FT /evidence="ECO:0000269|PubMed:18216068"
FT DISULFID 290..321
FT /evidence="ECO:0000269|PubMed:18216068"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:4DZT"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4DZT"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 348..365
FT /evidence="ECO:0007829|PDB:4DZT"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:4DZT"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:4DZT"
SQ SEQUENCE 513 AA; 53913 MW; DDFDFE6D4A50B785 CRC64;
MRKTYWLMAL FAVLVLGGCQ MASRSDPTPT LAEAFWPKEA PVYGLDDPEA IPGRYIVVFK
KGKGQSLLQG GITTLQARLA PQGVVVTQAY TGALQGFAAE MAPQALEAFR QSPDVEFIEA
DKVVRAWATQ SPAPWGLDRI DQRDLPLSNS YTYTATGRGV NVYVIDTGIR TTHREFGGRA
RVGYDALGGN GQDCNGHGTH VAGTIGGVTY GVAKAVNLYA VRVLDCNGSG STSGVIAGVD
WVTRNHRRPA VANMSLGGGV STALDNAVKN SIAAGVVYAV AAGNDNANAC NYSPARVAEA
LTVGATTSSD ARASFSNYGS CVDLFAPGAS IPSAWYTSDT ATQTLNGTSM ATPHVAGVAA
LYLEQNPSAT PASVASAILN GATTGRLSGI GSGSPNRLLY SLLSSGSGST APCTSCSYYT
GSLSGPGDYN FQPNGTYYYS PAGTHRAWLR GPAGTDFDLY LWRWDGSRWL TVGSSTGPTS
EESLSYSGTA GYYLWRIYAY SGSGMYEFWL QRP
