ID D4I370_ERWAC Unreviewed; 268 AA.
AC D4I370;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN Name=ydgD {ECO:0000313|EMBL:CBA20793.1};
GN OrderedLocusNames=EAMY_1843 {ECO:0000313|EMBL:CBA20793.1};
OS Erwinia amylovora (strain CFBP1430).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA20793.1, ECO:0000313|Proteomes:UP000001841};
RN [1] {ECO:0000313|EMBL:CBA20793.1, ECO:0000313|Proteomes:UP000001841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA Duffy B.;
RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT CFBP 1430 and comparison to other Erwinia spp.";
RL Mol. Plant Microbe Interact. 23:384-393(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR EMBL; FN434113; CBA20793.1; -; Genomic_DNA.
DR RefSeq; WP_004157647.1; NC_013961.1.
DR AlphaFoldDB; D4I370; -.
DR STRING; 665029.EAMY_1843; -.
DR MEROPS; S01.260; -.
DR GeneID; 8911660; -.
DR KEGG; eam:EAMY_1843; -.
DR PATRIC; fig|665029.3.peg.1771; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_078170_0_0_6; -.
DR OrthoDB; 267336at2; -.
DR Proteomes; UP000001841; 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:CBA20793.1};
KW Protease {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:CBA20793.1};
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..268
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5006991212"
FT DOMAIN 48..240
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
SQ SEQUENCE 268 AA; 28851 MW; FDE00DB1213956E4 CRC64;
MRLTAVLLVG CFACSFYTHA DEDTRNEADT TTLFFGKDNR QPVDNTAHPP WEAIGQLETA
SGNLCSATLI APNLALTAGH CLLSPPGRLD KAVALRFIAN TKGGWRYEIH DIEARVDPAL
GRKLKADGDG WIVPSSAAPY DFGLIILRNP PSGIVPLPLF SGSRQDLTSA LKESGRQITQ
AGYPEDHLDT LYAHNDCMVT GWAQKAVLSH QCDTLPGDSG SPLLLKVNGE WKLIGVQSSA
PAAKDRYLAD NRAIAVTAFR DSLDALAQ
//
