ID   ALP_FUSCU               Reviewed;          62 AA.
AC   P83610;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2003, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Alkaline proteinase;
DE            Short=ALP;
DE            EC=3.4.21.-;
DE   Flags: Fragments;
OS   Fusarium culmorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5516;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, INDUCTION, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=MUCL 28166 / VTT-D-80148;
RX   PubMed=11846781; DOI=10.1046/j.0014-2956.2001.02697.x;
RA   Pekkarinen A.I., Jones B.L., Niku-Paavola M.-L.;
RT   "Purification and properties of an alkaline proteinase of Fusarium
RT   culmorum.";
RL   Eur. J. Biochem. 269:798-807(2002).
CC   -!- FUNCTION: Serine protease. May be involved in the invasion of grains
CC       and hydrolyzation of grain proteins. {ECO:0000269|PubMed:11846781}.
CC   -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF)
CC       and chymostatin (CST), but not by Bowman-Birk type trypsin-chymotrypsin
CC       inhibitor (BBI). {ECO:0000269|PubMed:11846781}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.1 mM for N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (at pH 6.0
CC         with dimethylsulfoxide);
CC         KM=2.3 mM for N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (at pH 9.0
CC         with dimethylsulfoxide);
CC         KM=1.1 mM for N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (at pH 9.0
CC         without dimethylsulfoxide);
CC       pH dependence:
CC         Optimum pH is 8.3-9.6.;
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: By gluten. {ECO:0000269|PubMed:11846781}.
CC   -!- MASS SPECTROMETRY: Mass=28663; Mass_error=50; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11846781};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   AlphaFoldDB; P83610; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           <1..>62
FT                   /note="Alkaline proteinase"
FT                   /id="PRO_0000076406"
FT   DOMAIN          <1..>62
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        21
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10080"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000305"
FT   NON_CONS        41..42
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         62
SQ   SEQUENCE   62 AA;  6493 MW;  C62D3046A5F16D82 CRC64;
     GSTSYIYDTS AGSGTYAYIV DTGIITSHNG FNWAANDIIS KSYSNYGTVL DIFAPGTSVL
     SS