PRT1_PECCC
ID PRT1_PECCC Reviewed; 347 AA.
AC Q99132;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Extracellular metalloprotease;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=prt1;
OS Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS carotovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC14;
RX PubMed=1917878; DOI=10.1128/jb.173.20.6537-6546.1991;
RA Kyoestioe S.R.M., Cramer C.L., Lacy G.H.;
RT "Erwinia carotovora subsp. carotovora extracellular protease:
RT characterization and nucleotide sequence of the gene.";
RL J. Bacteriol. 173:6537-6546(1991).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; M36651; AAA24858.1; -; Genomic_DNA.
DR PIR; A41048; A41048.
DR AlphaFoldDB; Q99132; -.
DR SMR; Q99132; -.
DR MEROPS; M04.027; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR032475; Protealysin_N_PP.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF16485; PLN_propep; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..?
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028622"
FT CHAIN ?..347
FT /note="Extracellular metalloprotease"
FT /id="PRO_0000028623"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 347 AA; 38828 MW; CD39174431E7760C CRC64;
MKSRPICSVI PPYILHRIIA NGTDEQRHCA QQTLMHVQSL MVSHHPRPEP HEKLPAGQAN
RSIHDAEQQQ QLPGKLVRAE GQPSNGDIAV DEAYSYLGVT YDFFWKIFQR NSLDAEGLPL
AGTVHYGQDY QNAFWNGQQM VFGDGDGKIF NRFTIALDVV AHELTHGITE NEAGLIYFRQ
SGALNESLSD VFGSMVKQYH LGQTTEQADW LIGAELLADG IHGMGLRSMS HPGTAYDDEL
LGIDPQPSHM NEYVNTREDN GGVHLNSGIP NRAFYLAAIA LGGHSWEKAG RIWYDTLCDK
TLPQNADFEI FARHTIQHAA KRFNHTVADI VQQSWETVGV EVRQEFL
