ID Q9AER8_GEOSE Unreviewed; 401 AA.
AC Q9AER8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 03-MAY-2023, entry version 88.
DE SubName: Full=Thermophilic alkaline protease {ECO:0000313|EMBL:AAK29176.1};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422 {ECO:0000313|EMBL:AAK29176.1};
RN [1] {ECO:0000313|EMBL:AAK29176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F1 {ECO:0000313|EMBL:AAK29176.1};
RA Fu Z.B., Hamid S., Razak C.N.A., Salleh A.B., Basri M., Rahman R.N.Z.;
RT "Cloning and sequencing of the thermophilic alkaline protease gene from
RT Bacillus stearothermophilus F1 and extracellular expression in E. coli.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAK29176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F1 {ECO:0000313|EMBL:AAK29176.1};
RX PubMed=12651108; DOI=10.1016/S1046-5928(02)00637-X;
RA Fu Z., Hamid S.B., Razak C.N., Basri M., Salleh A.B., Rahman R.N.;
RT "Secretory expression in Escherichia coli and single-step purification of a
RT heat-stable alkaline protease.";
RL Protein Expr. Purif. 28:63-68(2003).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AY028615; AAK29176.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AER8; -.
DR MEROPS; S08.009; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 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; 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 PANTHER; PTHR43806:SF59; EXTRACELLULAR PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..401
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004323034"
FT DOMAIN 152..391
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 401 AA; 42815 MW; 1C22F08D6B5E607B CRC64;
MKFKAIVSLS LAVSMSLFPF LVEAASNDGV ESPKTVSEIN VSHEKGAYVQ GEVIVQFKEQ
VNAEEKAKAL KEVGATAVPD NDRVKSKFNV LKVGNVEAVV KALNHNPLVE YAEPNYLFNA
AWTPNDTYYQ GYQYGPQNTY TAYAWDVTKG 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
//