ID F3GBC3_PSESJ Unreviewed; 379 AA.
AC F3GBC3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=PSYPI_19071 {ECO:0000313|EMBL:EGH44373.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH44373.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH44373.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH44373.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH44373.1}.
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DR EMBL; AEAI01000945; EGH44373.1; -; Genomic_DNA.
DR AlphaFoldDB; F3GBC3; -.
DR PATRIC; fig|629263.4.peg.3128; -.
DR HOGENOM; CLU_061781_0_0_6; -.
DR BioCyc; PSYR629263:G11X0-3374-MONOMER; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06974; TerD_like; 1.
DR Gene3D; 2.60.60.30; sav2460 like domains; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR003325; TerD.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR PANTHER; PTHR43019:SF62; SERINE ENDOPROTEASE DEGS; 1.
DR Pfam; PF02342; TerD; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|RuleBase:RU004296};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 72..154
FT /note="TerD"
FT /evidence="ECO:0000259|Pfam:PF02342"
FT REGION 161..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 304
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
SQ SEQUENCE 379 AA; 40466 MW; 02489B4956AD1BD3 CRC64;
MKLLAPGANT ALANAHCTWN LESGKSSVFG EYAAVALLAA NDKRQPMGDP ALLQQEQGWM
EWSGGPQDVG CTLRLDRLPT GSDRVLLMVY VYAAMGPIRD IASLHLKVDG DIEHRLDLRD
NGEAAIIIGE FYKRNEQWKF RALSEGSAYG LSAFGRKIGL DVDDRHPRRP SAGSGGGPRH
ESATGTAFVV GPAHVMTCAH VIEDMGVFYI TSLEGRYKAE PVVIDRRNDI ALLRVQGAPL
LSPVTFRDGQ GCEPGDTVAV LGYPLASISG GGLQVTQGGI SGLFGLHNDA SLFQFTAPIQ
PGSSGSPLFD NGGAVIGMVT STVPDGQNMN FAVKSALLLA FLQACRIDAA HARPERSYTT
TEISRTAQSS LWLVEASRQ
//
