ORYZ_ASPOR
ID ORYZ_ASPOR Reviewed; 403 AA.
AC P12547; Q2UJX3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Alkaline protease 1;
DE Short=ALP;
DE EC=3.4.21.63;
DE AltName: Full=Aspergillopeptidase B;
DE AltName: Full=Aspergillus proteinase B;
DE AltName: Full=Elastase;
DE AltName: Full=Elastinolytic serine proteinase;
DE AltName: Full=Oryzin;
DE Flags: Precursor;
GN Name=alp1; Synonyms=alk1, alp, alpA; ORFNames=AO090003001036;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 20386 / 460;
RX PubMed=2693947; DOI=10.1007/bf00261154;
RA Tatsumi H., Ogawa Y., Murakami S., Ishida Y., Murakami K., Masaki A.,
RA Kawabe H., Arimura H., Nakano E., Motai H.;
RT "A full length cDNA clone for the alkaline protease from Aspergillus
RT oryzae: structural analysis and expression in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 219:33-38(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=U 212;
RX PubMed=1840548; DOI=10.1016/0378-1119(91)90501-2;
RA Cheevadhanarak S., Renno D.V., Saunders G., Holt G.;
RT "Cloning and selective overexpression of an alkaline protease-encoding gene
RT from Aspergillus oryzae.";
RL Gene 108:151-155(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20386 / 460;
RX PubMed=1368748; DOI=10.1271/bbb1961.55.2807;
RA Murakami K., Ishida Y., Masaki A., Tatsumi H., Murakami S., Nakano E.,
RA Motai H., Kawabe H., Arimura H.;
RT "Isolation and characterization of the alkaline protease gene of
RT Aspergillus oryzae.";
RL Agric. Biol. Chem. 55:2807-2811(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-403, AND PARTIAL PROTEIN SEQUENCE.
RA Tatsumi H., Ohsawa M., Tsuji R.F., Murakami S., Nakano E., Motai H.,
RA Masaki A., Ishida Y., Murakami K., Kawabe H., Arimura H.;
RT "Cloning and sequencing of the alkaline protease cDNA from Aspergillus
RT oryzae.";
RL Agric. Biol. Chem. 52:1887-1888(1988).
RN [6]
RP INDUCTION.
RX PubMed=18930158; DOI=10.1016/j.fgb.2008.09.007;
RA Punt P.J., Schuren F.H., Lehmbeck J., Christensen T., Hjort C.,
RA van den Hondel C.A.;
RT "Characterization of the Aspergillus niger prtT, a unique regulator of
RT extracellular protease encoding genes.";
RL Fungal Genet. Biol. 45:1591-1599(2008).
RN [7]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18226921; DOI=10.1016/j.pep.2007.12.005;
RA Guo J.P., Ma Y.;
RT "High-level expression, purification and characterization of recombinant
RT Aspergillus oryzae alkaline protease in Pichia pastoris.";
RL Protein Expr. Purif. 58:301-308(2008).
CC -!- FUNCTION: Secreted alkaline protease that allows assimilation of
CC proteinaceous substrates. {ECO:0000269|PubMed:18226921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-
CC OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:18226921};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:18226921};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Expression is controlled by the prtT transcription factor.
CC {ECO:0000269|PubMed:18930158}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; X17561; CAA35594.1; -; mRNA.
DR EMBL; S75278; AAB20819.1; -; Genomic_DNA.
DR EMBL; X54726; CAA38527.2; -; Genomic_DNA.
DR EMBL; S79617; AAC60533.1; -; Genomic_DNA.
DR EMBL; D10062; BAA00951.1; -; Genomic_DNA.
DR EMBL; AP007155; BAE58142.1; -; Genomic_DNA.
DR EMBL; D00350; BAA00258.1; -; mRNA.
DR PIR; JU0278; SUASO.
DR RefSeq; XP_001820144.1; XM_001820092.2.
DR AlphaFoldDB; P12547; -.
DR SMR; P12547; -.
DR STRING; 510516.P12547; -.
DR Allergome; 3132; Asp o 13.0101.
DR Allergome; 84; Asp o 13.
DR MEROPS; S08.053; -.
DR EnsemblFungi; BAE58142; BAE58142; AO090003001036.
DR GeneID; 5992127; -.
DR KEGG; aor:AO090003001036; -.
DR VEuPathDB; FungiDB:AO090003001036; -.
DR HOGENOM; CLU_011263_1_4_1; -.
DR OMA; GEGVWAY; -.
DR BRENDA; 3.4.21.63; 522.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
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 Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT PROPEP 22..121
FT /id="PRO_0000027084"
FT CHAIN 122..403
FT /note="Alkaline protease 1"
FT /id="PRO_0000027085"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..403
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
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 CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 42571 MW; 39A8AC8B8790E010 CRC64;
MQSIKRTLLL LGAILPAVLG APVQETRRAA EKLPGKYIVT FKPGIDEAKI QEHTTWATNI
HQRSLERRGA TGGDLPVGIE RNYKINKFAA YAGSFDDATI EEIRKNEDVA YVEEDQIYYL
DGLTTQKSAP WGLGSISHKG QQSTDYIYDT SAGEGTYAYV VDSGVNVDHE EFEGRASKAY
NAAGGQHVDS IGHGTHVSGT IAGKTYGIAK KASILSVKVF QGESSSTSVI LDGFNWAAND
IVSKKRTSKA AINMSLGGGY SKAFNDAVEN AFEQGVLSVV AAGNENSDAG QTSPASAPDA
ITVAAIQKSN NRASFSNFGK VVDVFAPGQD ILSAWIGSSS ATNTISGTSM ATPHIVGLSL
YLAALENLDG PAAVTKRIKE LATKDVVKDV KGSPNLLAYN GNA
