THES_BACSJ
ID THES_BACSJ Reviewed; 401 AA.
AC Q45670;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Thermophilic serine proteinase;
DE EC=3.4.21.-;
DE AltName: Full=Ak.1 protease;
DE Flags: Precursor;
OS Bacillus sp. (strain AK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=268807;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7993087; DOI=10.1128/aem.60.11.3981-3988.1994;
RA Maciver B., McHale R.H., Saul D.J., Bergquist P.L.;
RT "Cloning and sequencing of a serine proteinase gene from a thermophilic
RT Bacillus species and its expression in Escherichia coli.";
RL Appl. Environ. Microbiol. 60:3981-3988(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 122-401.
RX PubMed=10588904; DOI=10.1006/jmbi.1999.3291;
RA Smith C.A., Toogood H.S., Baker H.M., Daniel R.M., Baker E.N.;
RT "Calcium-mediated thermostability in the subtilisin superfamily: the
RT crystal structure of Bacillus Ak.1 protease at 1.8-A resolution.";
RL J. Mol. Biol. 294:1027-1040(1999).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10588904};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:10588904};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:10588904};
CC Note=Binds 1 sodium ion per subunit. {ECO:0000269|PubMed:10588904};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5.;
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; L29506; AAA63688.1; -; Genomic_DNA.
DR PIR; I39974; I39974.
DR PDB; 1DBI; X-ray; 1.80 A; A=122-401.
DR PDBsum; 1DBI; -.
DR AlphaFoldDB; Q45670; -.
DR SMR; Q45670; -.
DR MEROPS; S08.009; -.
DR BRENDA; 3.4.21.62; 691.
DR EvolutionaryTrace; Q45670; -.
DR GO; GO:0005576; C:extracellular region; 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; cd07484; Peptidases_S8_Thermitase_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
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; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034084; Thermitase-like_dom.
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; Calcium; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW Secreted; Serine protease; Signal; Sodium; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..121
FT /id="PRO_0000027193"
FT CHAIN 122..401
FT /note="Thermophilic serine proteinase"
FT /id="PRO_0000027194"
FT DOMAIN 133..399
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:10588904"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:10588904"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:10588904"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 297
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 300
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10588904"
FT BINDING 323
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10588904"
FT DISULFID 258..260
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1DBI"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1DBI"
FT TURN 168..173
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1DBI"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1DBI"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:1DBI"
FT TURN 382..386
FT /evidence="ECO:0007829|PDB:1DBI"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:1DBI"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:1DBI"
SQ SEQUENCE 401 AA; 42835 MW; 1C736EF4A89F256F CRC64;
MKFKAIVSLS LAVSMSLFPF LVEAASNDGV ESPKTVSEIN VSHEKGAYVQ GEVIVQFKEQ
VNAEEKAKAL KEVGATAVPD NDRVKSKFNV LKVGNVEAVV KALNNNPLVE YAEPNYLFNA
AWTPNDTYYQ GYQYGPQNTY TDYAWDVTKG SSGQEIAVID TGVDYTHPDL DGKVIKGYDF
VDNDYDPMDL NNHGTHVAGI AAAETNNATG IAGMAPNTRI LAVRALDRNG SGTLSDIADA
IIYAADSGAE VINLSLGCDC HTTTLENAVN YAWNKGSVVV AAAGNNGSST TFEPASYENV
IAVGAVDQYD RLASFSNYGT WVDVVAPGVD IVSTITGNRY AYMSGTSMAS PHVAGLAALL
ASQGRNNIEI RQAIEQTADK ISGTGTYFKY GRINSYNAVT Y
