ID   PRTS_PHOAZ              Reviewed;         371 AA.
AC   A9YWT8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Protease PrtS;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=prtS {ECO:0000312|EMBL:ABY26041.1};
OS   Photorhabdus sp. (strain Az29).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus; unclassified Photorhabdus.
OX   NCBI_TaxID=229779;
RN   [1] {ECO:0000312|EMBL:ABY26041.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cabral C.M., Montiel R., Simoes N.;
RT   "Cloning and sequencing of the gene for PrtS a M4 family metalloprotease
RT   secreted by Photorhabdus sp. Az29.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 56-67; 103-112; 290-297 AND 314-322, 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: Metalloprotease involved in the inhibition of insect
CC       antibacterial peptides. Reduces the antibacterial activity of
CC       G.mellonella hemolymph by 50%. Reduces the antibacterial activity of
CC       cecropin A by 80% and completely inhibits cecropin B.
CC       {ECO:0000269|PubMed:15240252}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P05806};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P05806};
CC   -!- ACTIVITY REGULATION: Inhibited by 8 mM 1,10-phenanthroline, but not by
CC       EDTA or PMSF. {ECO:0000269|PubMed:15240252}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {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 M4 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU307118; ABY26041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9YWT8; -.
DR   SMR; A9YWT8; -.
DR   MEROPS; M04.024; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..371
FT                   /note="Protease PrtS"
FT                   /id="PRO_0000397930"
FT   REGION          352..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000250|UniProtKB:P05806,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        273
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P05806,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P05806,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P05806,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P05806,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CONFLICT        57
FT                   /note="T -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="V -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   371 AA;  41773 MW;  D69F180F84871D5B CRC64;
     MQIQNNNYKG LIPPYILQNI YKNTSESEKD NVLMTLNHTQ SLMLDSVIKT SDSIDNTDDE
     VVSDTLHRSI YDAKNETKLP GTLVRDEGDP DNGDVAVDNA YKYLEATYNF YKEVFNRNSL
     DDKGMKLIAT VHYGKEYMNA YWGRGQMVFG DGDGKVFNNF TTSIDVIGHE LSHGVIEKTA
     DLIYFFQSGA LNESIADVFG SLVRQHYLKQ KADEASWVVG EELLAKGIKG VGIRSMKEPG
     KAYDDPLLGK NPQPGHMDDF KDYPIYRDNG GVHVNSGIPN KAFYNLAIKL GGYAWEKAGK
     IWYNTLLDKD LARDTTFLSF AKLTVKHARD LFDEDVEKAT IDSWKEVGIK VKEEDKDKGK
     DEGKDKAETK V