PRTA_PHOAZ
ID PRTA_PHOAZ Reviewed; 483 AA.
AC P82115;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Serralysin;
DE EC=3.4.24.40;
DE AltName: Full=Protease PrtA;
DE AltName: Full=Secreted alkaline metalloproteinase {ECO:0000303|PubMed:15240252};
GN Name=prtA {ECO:0000303|PubMed:15240252};
OS Photorhabdus sp. (strain Az29).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus; unclassified Photorhabdus.
OX NCBI_TaxID=229779;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cabral C.M., Montiel R., Simoes N.;
RT "Cloning and sequencing of the gene for a metalloprotease with an ABC
RT transport system: a protease secreted by Photorhabdus sp. Az29 involved in
RT the inhibition of insect antibacterial peptides.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 155-162; 166-197 AND 264-277, FUNCTION, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=15240252; DOI=10.1128/aem.70.7.3831-3838.2004;
RA Cabral C.M., Cherqui A., Pereira A., Simoes N.;
RT "Purification and characterization of two distinct metalloproteases
RT secreted by the entomopathogenic bacterium Photorhabdus sp. strain Az29.";
RL Appl. Environ. Microbiol. 70:3831-3838(2004).
CC -!- FUNCTION: Involved in the inhibition of insect antibacterial peptides.
CC Reduces the antibacterial activity of G.mellonella hemolymph by 50%.
CC Reduces the antibacterial activity of cecropin A by 80% and cecropin B
CC by 75%. {ECO:0000269|PubMed:15240252}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC P1'.; EC=3.4.24.40;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07268};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P07268};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P07268};
CC -!- ACTIVITY REGULATION: Inhibited by 8 mM 1,10-phenanthroline and 10 mM
CC EDTA, but not by PMSF. {ECO:0000269|PubMed:15240252}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:15240252};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Active from 10 to 80
CC degrees Celsius. {ECO:0000269|PubMed:15240252};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15240252}.
CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000255}.
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DR EMBL; AY531111; AAS19409.1; -; Genomic_DNA.
DR AlphaFoldDB; P82115; -.
DR SMR; P82115; -.
DR MEROPS; M10.063; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 2.150.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR016294; Pept_M10B.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR PIRSF; PIRSF001205; Peptidase_M10B; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; SSF51120; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Repeat; Secreted; Zinc.
FT CHAIN 1..483
FT /note="Serralysin"
FT /id="PRO_0000078177"
FT REPEAT 342..359
FT /note="Hemolysin-type calcium-binding 1"
FT /evidence="ECO:0000255"
FT REPEAT 360..377
FT /note="Hemolysin-type calcium-binding 2"
FT /evidence="ECO:0000255"
FT ACT_SITE 185
FT /evidence="ECO:0000250|UniProtKB:P07268,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07268,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07268,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07268,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07268"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07268"
SQ SEQUENCE 483 AA; 53483 MW; F402483BD50293A1 CRC64;
MERYMSLKKK ISYSELIGSA KANELQTQLQ AYVPGKDPNI VVEHEPSKNA AKELIRGDYR
WGHQGDDKSE TFQLTYSFLE SEPDNMPWHI TGFSAFNEEQ RTAAKLSIQS WTDVANINFT
ETTDSDKAHI TFGFFDASLT GSYAFAYLPS PESKQSGTWY NLKSRTFSEN DIGVNGYGRQ
TFTHEIGHTL GLEHPAAYNA SDKERPTYKK SATYFEDSRA YTVMSYFGEK NTRTDFKGIY
SSAPLLNDIS AIQEVYGANN TTRTDDTVYG FNSNTDRDFF TAKDENSKLL FTAWDAGGND
TFDFSGFTQD QRINLNEASF SDVGGLKGNV SIARGVTIEN AIGGSGNDIL IGNDAENILK
GGAGDDIIYG GLGADQLWGG EGKDTFVYLS AKESPPLERD WIHDFVSGED KIDVSLFDLG
EAGKGGVKFV REFTGAVGEA VLRYDTVNKV NDFAINLGDK FSYDDFWVKI VGEPILESDF
ILA
