ID Q6MQB3_BDEBA Unreviewed; 277 AA.
AC Q6MQB3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=Serine protease trypsin family {ECO:0000313|EMBL:CAE78534.1};
DE EC=3.4.21.4 {ECO:0000313|EMBL:CAE78534.1};
GN OrderedLocusNames=Bd0564 {ECO:0000313|EMBL:CAE78534.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE78534.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE78534.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; BX842647; CAE78534.1; -; Genomic_DNA.
DR RefSeq; WP_011163136.1; NC_005363.1.
DR AlphaFoldDB; Q6MQB3; -.
DR STRING; 264462.Bd0564; -.
DR KEGG; bba:Bd0564; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_073536_0_0_7; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF98; FI18310P1-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:CAE78534.1};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:CAE78534.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004276779"
FT DOMAIN 36..269
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 277 AA; 30172 MW; 7ED6A0076F963BB2 CRC64;
MKKCFLIFLF LLSACAPALQ EPVTEHLLQE DLDSAIVGGR RVRANDPRAN WVVMVRGTKG
FFLFKGSGIC TGAFITEDIV LTAAHCVTEK GATYEVAYGL SPLEEKRKVI KIDKVLVHED
YAPSTESLNP NDIALIKIRG TKPARLKVLG LQVEPPLEQP TTFLAIGYGN TAAGPKINER
GILHSTPTII TDINDTHLIG NQRNGIGICQ GDSGGPLLKA DEKGEPAIIG ITHATFRYKG
DPVNSNECYN RAAYVNIAHQ MAWIQKNVAL ISDEPLK
//