ID Q6MJY6_BDEBA Unreviewed; 256 AA.
AC Q6MJY6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:CAE80423.1};
GN OrderedLocusNames=Bd2630 {ECO:0000313|EMBL:CAE80423.1};
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:CAE80423.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE80423.1, 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).
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DR EMBL; BX842653; CAE80423.1; -; Genomic_DNA.
DR RefSeq; WP_011165026.1; NC_005363.1.
DR AlphaFoldDB; Q6MJY6; -.
DR STRING; 264462.Bd2630; -.
DR MEROPS; S01.234; -.
DR KEGG; bba:Bd2630; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_006842_0_4_7; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
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; PTHR24264:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24264; TRYPSIN-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; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..256
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004278264"
FT DOMAIN 29..256
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 256 AA; 26965 MW; DB0ED8C0517BF010 CRC64;
MKMNHLVIAG LMMMSAPVFA KSGSVGAKIV GGVEASIGEF PYIVSLQSGS HFCGGSLIKK
NWVLTAAHCV RGGTVKKVVI GLHDRTNAVN AESIAPKRII AHPNYNARTM ENDFALIELS
QDSSYAPVAL NPAEIALPTD GSEIMTTVAG WGATREGSYS LPTKLQKVDV PLVSSEACNK
AYNNGITDSM ICAGYEGGGK DSCQGDSGGP LVAQDENNQT YLVGVVSWGQ GCARAKYFGV
YAKVSNAIEW INNTAQ
//
