ID W8YU76_BACTU Unreviewed; 322 AA.
AC W8YU76;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=BTDB27_000502 {ECO:0000313|EMBL:CDN34160.1};
OS Bacillus thuringiensis DB27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1431339 {ECO:0000313|EMBL:CDN34160.1};
RN [1] {ECO:0000313|EMBL:CDN34160.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB27 {ECO:0000313|EMBL:CDN34160.1};
RA Iatsenko I., Pickard D., Corton C., Dougan G., Sommer R.J.;
RT "Draft genome sequence of highly nematicidal Bacillus thuringiensis DB27.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDN34160.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB27 {ECO:0000313|EMBL:CDN34160.1};
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR EMBL; HG810016; CDN34160.1; -; Genomic_DNA.
DR RefSeq; WP_030023344.1; NZ_HG810016.1.
DR AlphaFoldDB; W8YU76; -.
DR HOGENOM; CLU_073589_0_2_9; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR000126; V8_ser_AS.
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; PS00673; V8_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004296};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004296}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..308
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
SQ SEQUENCE 322 AA; 36245 MW; B50D0CBB45400AD5 CRC64;
MLDSFISIRC RLALYSFGVL FIFFCTVFLV NQKVYAEDVP WTSVSNEGER VLFQEQSLYS
NDRRGEDLVS PSFEGRKHGG EDWGAFLENT KLNYSPNILT YSVIGIDDRI RVNDTTSYPY
SAVVHIATQY NSGEIYGCTG ALISKDTVLT AGHCIYNKEI GGWATNVIVT PGRNGGQAPY
LPYKGTKLYS VSGWTDNKNS NYDYGTIKLN GSPGDYTGWF GYRTTYVESP KGLLAVIPGY
PADKIGNERY TMWRDYGPIE GVNPSRLTYK IDTYEGQSGS PVYHYFDTGI KIIAIHTRGN
KNMNFGNRIT DNVFNNIKRW SE
//
