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Database: UniProt
Entry: Q9AER8_GEOSE
LinkDB: Q9AER8_GEOSE
Original site: Q9AER8_GEOSE 
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
//
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