ID ASPN_PSEFR Reviewed; 144 AA.
AC Q9R4J4; Q9R4J5; Q9R4J6; Q9R4J7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-MAY-2023, entry version 35.
DE RecName: Full=Peptidyl-Asp metalloendopeptidase {ECO:0000303|PubMed:7674963};
DE EC=3.4.24.33;
DE AltName: Full=Endopeptidase Asp-N {ECO:0000303|PubMed:2669754, ECO:0000303|PubMed:7674963};
DE Flags: Fragments;
OS Pseudomonas fragi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=296;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RX PubMed=7674963; DOI=10.1016/0076-6879(95)48053-6;
RA Hagmann M.L., Geuss U., Fischer S., Kresse G.B.;
RT "Peptidyl-Asp metalloendopeptidase.";
RL Methods Enzymol. 248:782-787(1995).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7188696; DOI=10.1016/s0021-9258(19)86106-9;
RA Drapeau G.R.;
RT "Substrate specificity of a proteolytic enzyme isolated from a mutant of
RT Pseudomonas fragi.";
RL J. Biol. Chem. 255:839-840(1980).
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2669754; DOI=10.1016/0006-291x(89)90848-6;
RA Ingrosso D., Fowler A.V., Bleibaum J., Clarke S.;
RT "Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at
RT glutamyl residues in two proteins.";
RL Biochem. Biophys. Res. Commun. 162:1528-1534(1989).
CC -!- FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side
CC of aspartyl, glutamyl and cysteic acid residues.
CC {ECO:0000269|PubMed:2669754, ECO:0000269|PubMed:7188696}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid
CC bonds.; EC=3.4.24.33; Evidence={ECO:0000269|PubMed:2669754,
CC ECO:0000269|PubMed:7188696};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O75173};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75173};
CC -!- SIMILARITY: Belongs to the peptidase M72 family. {ECO:0000305}.
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DR AlphaFoldDB; Q9R4J4; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Pfam; PF13688; Reprolysin_5; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Zinc.
FT CHAIN <1..144
FT /note="Peptidyl-Asp metalloendopeptidase"
FT /id="PRO_0000395560"
FT ACT_SITE 65
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT NON_CONS 13..14
FT /evidence="ECO:0000303|PubMed:7674963"
FT NON_CONS 40..41
FT /evidence="ECO:0000303|PubMed:7674963"
FT NON_CONS 53..54
FT /evidence="ECO:0000303|PubMed:7674963"
FT NON_CONS 73..74
FT /evidence="ECO:0000303|PubMed:7674963"
FT NON_CONS 127..128
FT /evidence="ECO:0000303|PubMed:7674963"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:7674963"
SQ SEQUENCE 144 AA; 16113 MW; 300BCF59C9D6F407 CRC64;
ESNQGYVNSN VGIELARYET TNYTESGSFD TDLARFRGTS DSIHTSRNTY TAADCATGYY
SFAHEIGHLQ SARDIATDSS TSPYAYGHGY RYEPATGWRT IMAYNCTRSC PRLNYWSNPN
ISYDIGPDNQ RVLVNTKATI AAFR
//
