PROT1_LYSEN
ID PROT1_LYSEN Reviewed; 387 AA.
AC A0A0S2DNK1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Probable serine protease FE772_23060 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000305|PubMed:28473380};
DE AltName: Full=Trypsin-like protease 1 {ECO:0000303|PubMed:35025633};
GN ORFNames=BV903_13690 {ECO:0000312|EMBL:OPD63339.1},
GN FE772_23060 {ECO:0000312|EMBL:QCW28096.1},
GN Ga0399710_4914 {ECO:0000303|PubMed:35025633},
GN GLE_4744 {ECO:0000312|EMBL:ALN60085.1};
OS Lysobacter enzymogenes.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69;
RN [1] {ECO:0000312|EMBL:ALN60085.1, ECO:0000312|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3;
RX PubMed=26597042; DOI=10.1186/s12864-015-2191-z;
RA de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J., Patel N.,
RA Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.;
RT "Comparative genomics and metabolic profiling of the genus Lysobacter.";
RL BMC Genomics 16:991-991(2015).
RN [2] {ECO:0000312|EMBL:OPD63339.1, ECO:0000312|Proteomes:UP000190203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B25;
RX PubMed=28473380; DOI=10.1128/genomea.00271-17;
RA Hernandez I., Fernandez C.;
RT "Draft Genome Sequence and Assembly of a Lysobacter enzymogenes Strain with
RT Biological Control Activity against Root Knot Nematodes.";
RL Genome Announc. 5:0-0(2017).
RN [3] {ECO:0000312|EMBL:QCW28096.1, ECO:0000312|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36;
RX PubMed=31540995; DOI=10.1128/aem.01742-19;
RA Feng T., Han Y., Li B., Li Z., Yu Y., Sun Q., Li X., Du L., Zhang X.H.,
RA Wang Y.;
RT "Interspecies and Intraspecies Signals Synergistically Regulate Lysobacter
RT enzymogenes Twitching Motility.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF SER-343.
RC STRAIN=YC36;
RX PubMed=35025633; DOI=10.1126/science.abj8432;
RA Johnson A.G., Wein T., Mayer M.L., Duncan-Lowey B., Yirmiya E.,
RA Oppenheimer-Shaanan Y., Amitai G., Sorek R., Kranzusch P.J.;
RT "Bacterial gasdermins reveal an ancient mechanism of cell death.";
RL Science 375:221-225(2022).
CC -!- FUNCTION: Possibly a dedicated protease for substrate gasdermin bGSDM;
CC cleaves the bGSDM precursor, releasing the pore-forming moiety, which
CC integrates into the membrane and triggers cell death. Involved in
CC defense against bacteriophages. When this probable 4 gene operon
CC (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it
CC provides nearly 100-fold protection against phages T5 and T6 and about
CC 8-fold against phage T4. The operon without bGSDM no longer protects
CC against phage. {ECO:0000269|PubMed:35025633}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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; CP013140; ALN60085.1; -; Genomic_DNA.
DR EMBL; MTAY01000035; OPD63339.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW28096.1; -; Genomic_DNA.
DR RefSeq; WP_057949281.1; NZ_CP013140.1.
DR EnsemblBacteria; ALN60085; ALN60085; GLE_4744.
DR EnsemblBacteria; OPD63339; OPD63339; BV903_13690.
DR KEGG; lez:GLE_4744; -.
DR PATRIC; fig|69.6.peg.4678; -.
DR OMA; VGYPAWD; -.
DR OrthoDB; 390088at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000190203; Unassembled WGS sequence.
DR Proteomes; UP000308311; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..387
FT /note="Probable serine protease FE772_23060"
FT /id="PRO_0000455584"
FT MUTAGEN 343
FT /note="S->A: 4-gene operon still protects against phage."
FT /evidence="ECO:0000269|PubMed:35025633"
SQ SEQUENCE 387 AA; 41018 MW; 02D4898C7116C6CB CRC64;
MEQERIRQLA KLLAAGARAR DAQAESMMDG GVAAAPAPAG QTLDVVEQAL STPPDDVDET
QWRAAREQLL THAHNGLVKL QRGDLQLDAD EGCAMEAVII SDGSRPSFLL CDGEIDPKDP
SIETWAGNIA AAQALGIAKL AAAVGRIQPK NGHASRYVGT GTLIDRDAGL ILTNYHVIEQ
AQQNYGVAMT RNGDRLSVDG WLEIDFVGES CSLRTHRFRI VEVALPQGYG STFHGIDAAV
ARIEPLPDSP ALPDPVPLLS ADAAYATGAI SSLALIGFPA RPSLQDGKDV DWSFVMRVLF
GNRFGVKRLA PGQFTLPLGS HALDQGRRAI GHDATTFGGA SGSLLMSWLD DRTPSFALHF
GGATGVSNYA LSFAAERNAL SAIGARF