PEPA_ASPPE
ID PEPA_ASPPE Reviewed; 390 AA.
AC A0A146F0J0;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Aspergillopepsin-1 {ECO:0000305};
DE EC=3.4.23.18 {ECO:0000269|PubMed:23044751};
DE AltName: Full=Aspartic protease pepA;
DE AltName: Full=Aspergillopepsin I;
DE AltName: Full=Aspergillopeptidase A;
DE Flags: Precursor;
GN Name=pepA;
OS Aspergillus pseudoglaucus (Eurotium repens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1405805;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 68-73; 133-145
RP AND 175-184.
RC STRAIN=MK82;
RX PubMed=26919469; DOI=10.1002/jsfa.7688;
RA Takenaka S., Umeda M., Senba H., Koyama D., Tanaka K., Yoshida K.I.,
RA Doi M.;
RT "Heterologous expression and characterization of the Aspergillus aspartic
RT protease involved in the hydrolysis and decolorization of red-pigmented
RT proteins.";
RL J. Sci. Food Agric. 97:95-101(2017).
RN [2]
RP PROTEIN SEQUENCE OF 68-73; 133-145 AND 175-184, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=MK82;
RX PubMed=23044751; DOI=10.1002/jsfa.5896;
RA Aoki K., Matsubara S., Umeda M., Tachibana S., Doi M., Takenaka S.;
RT "Aspartic protease from Aspergillus (Eurotium) repens strain MK82 is
RT involved in the hydrolysis and decolourisation of dried bonito
RT (Katsuobushi).";
RL J. Sci. Food Agric. 93:1349-1355(2013).
CC -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC proteinaceous substrates. The scissile peptide bond is attacked by a
CC nucleophilic water molecule activated by two aspartic residues in the
CC active site. Shows a broad primary substrate specificity. Favors
CC hydrophobic residues at the P1 and P1' positions, but also accepts a
CC lysine residue in the P1 position, leading to the activation of
CC trypsinogen and chymotrypsinogen A (By similarity). Hydrolyzes
CC myoglobin, hemoglobin and other natural proteins. Hydrolyzes equine
CC myoglobin between positions 'Met-1' and 'Gly-2', 'Lys-43' and 'Phe-44',
CC and 'Leu-70' and 'Thr-71' (PubMed:23044751).
CC {ECO:0000250|UniProtKB:Q12567, ECO:0000269|PubMed:23044751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity. Generally
CC favors hydrophobic residues in P1 and P1', but also accepts Lys in
CC P1, which leads to activation of trypsinogen. Does not clot milk.;
CC EC=3.4.23.18; Evidence={ECO:0000269|PubMed:23044751};
CC -!- ACTIVITY REGULATION: Inhibited by the microbial peptide pepstatin A.
CC {ECO:0000269|PubMed:23044751}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for equine myoglobin {ECO:0000269|PubMed:23044751};
CC KM=7.9 uM for bovine hemoglobin {ECO:0000269|PubMed:23044751};
CC Note=kcat is 0.05 min(-1) with equine myoglobin as substrate and
CC 0.0646 min(-1) with bovine hemoglobin as substrate.
CC {ECO:0000269|PubMed:23044751};
CC pH dependence:
CC Optimum pH is 2-4. Stable from pH 2 to pH 6.
CC {ECO:0000269|PubMed:23044751};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:23044751};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC -!- MISCELLANEOUS: Used in Japanese cuisine. During the fermentation
CC process of Katsuobushi - dried, smoked and fermented meat of the
CC skipjack tuna (bonito) Katsuwonus pelamis - aspartic protease plays a
CC role in the decolorisation of Katsuobushi from a dark reddish-brown to
CC pale pink by the hydrolysis of heme proteins. The change in color gives
CC Katsuobushi a higher ranking and price. {ECO:0000305|PubMed:23044751}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; LC101500; BAU68268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A146F0J0; -.
DR SMR; A0A146F0J0; -.
DR BRENDA; 3.4.23.18; 527.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Hydrolase; Protease;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..67
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:26919469"
FT /id="PRO_0000438797"
FT CHAIN 68..390
FT /note="Aspergillopepsin-1"
FT /id="PRO_5007523443"
FT DOMAIN 84..387
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CONFLICT 70..72
FT /note="TGS -> AAA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="TW -> YP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 40623 MW; 1BC7F9AF77ADAC71 CRC64;
MVNTSLLAAL TAYAVAVAAA PTAPQVKGFS VNQVAVPKGV YRHPAAQLAK AYGKYHATVP
TQVAAAAAAT GSVTTNPTSN DEEYITQVTV GDDTLGLDFD TGSADLWVFS SQTPSSERSG
HDYYTPGSSA QKIDGATWSI SYGDGSSASG DVYKDKVTVG GVSYDSQAVE SAEKVSSEFT
QDTENDGLLG LAFSSINTVQ PTPQKTFFDN VKSSLSEPIF AVALKHNAPG VYDFGYTDSS
KYTGSITYTD VDNSQGFWSF TADGYSIGSD SSSDSITGIA DTGTTLLLLD DSIVDAYYEQ
VNGASYDSSQ GGYVFPSSAS LPDFSVTIGD YTATVPGEYI SFADVGNGQT FGGIQSNSGI
GFSIFGDVFL KSQYVVFDAS GPRLGFAAQA
