ID B2VKM3_ERWT9 Unreviewed; 267 AA.
AC B2VKM3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN Name=ydgD {ECO:0000313|EMBL:CAO96719.1};
GN OrderedLocusNames=ETA_16730 {ECO:0000313|EMBL:CAO96719.1};
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO96719.1, ECO:0000313|Proteomes:UP000001726};
RN [1] {ECO:0000313|EMBL:CAO96719.1, ECO:0000313|Proteomes:UP000001726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC {ECO:0000313|Proteomes:UP000001726};
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR EMBL; CU468135; CAO96719.1; -; Genomic_DNA.
DR RefSeq; WP_012441412.1; NC_010694.1.
DR AlphaFoldDB; B2VKM3; -.
DR STRING; 465817.ETA_16730; -.
DR MEROPS; S01.260; -.
DR KEGG; eta:ETA_16730; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_078170_0_0_6; -.
DR OrthoDB; 267336at2; -.
DR Proteomes; UP000001726; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR15462; SERINE PROTEASE; 1.
DR PANTHER; PTHR15462:SF8; SERINE PROTEASE; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:CAO96719.1};
KW Protease {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:CAO96719.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001726};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU004296}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT CHAIN 21..267
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5006990940"
FT DOMAIN 47..239
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
SQ SEQUENCE 267 AA; 28642 MW; BCDCEC8476716A13 CRC64;
MRLTAVLLMG CLACSFYTHA DNDARNEAET TTLFFGKDNR QPVNDTAQAP WDAIGQLETA
SGNLCSATLI APNLALTAGH CLLSPPGKLD KAVALRFIAN DKGWRYEIHD IEARVDPALG
KKLKADGDGW IVPSSAAPYD FGLIVLRNPP SGITPLPLFS GSRQALTSSL KETGRRITQA
GYPEDHLDTL YSHSDCLVTG WAQKAVLSHQ CDTLPGDSGS PLLLKVNGEW QLIGVQSSAP
AAKDRYLADN RAIAVTAFRD SLDALAQ
//
