ID K7ZG86_BDEBC Unreviewed; 256 AA.
AC K7ZG86;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:AFY02227.1};
GN ORFNames=Bdt_2544 {ECO:0000313|EMBL:AFY02227.1};
OS Bdellovibrio bacteriovorus str. Tiberius.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY02227.1, ECO:0000313|Proteomes:UP000010074};
RN [1] {ECO:0000313|EMBL:AFY02227.1, ECO:0000313|Proteomes:UP000010074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tiberius {ECO:0000313|EMBL:AFY02227.1,
RC ECO:0000313|Proteomes:UP000010074};
RX PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA Sockett R.E.;
RT "Genome analysis of a simultaneously predatory and prey-independent, novel
RT Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT predictions of both ancient and recent lateral gene transfer from diverse
RT bacteria.";
RL BMC Genomics 13:670-670(2012).
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DR EMBL; CP002930; AFY02227.1; -; Genomic_DNA.
DR RefSeq; WP_015091663.1; NC_019567.1.
DR AlphaFoldDB; K7ZG86; -.
DR STRING; 1069642.Bdt_2544; -.
DR MEROPS; S01.234; -.
DR KEGG; bbat:Bdt_2544; -.
DR PATRIC; fig|1069642.3.peg.2519; -.
DR HOGENOM; CLU_006842_0_4_7; -.
DR Proteomes; UP000010074; 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; PTHR24253:SF153; FI06405P-RELATED; 1.
DR PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 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|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW 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_5003914233"
FT DOMAIN 29..256
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 256 AA; 26979 MW; B11819A9D2813F1A CRC64;
MKMNHLVIAG LMMMSAPVFA KSGSVGAKIV GGVEASIGEF PYIVSLQSSS HFCGGSLIKK
NWVLTAAHCV RGGTVKKVVI GLHDRTNALN AESIAPKRII AHPNYNARTM ENDFALIELS
QDSSYAPVAL NPAEITLPTD GSEILTTVAG WGATREGSYS LPTKLQKVDV PLVSTAACNK
AYNNGITDSM ICAGYEGGGK DSCQGDSGGP LVAQDENNQT YLVGVVSWGQ GCARANYYGV
YAKVSNAIEW INNTAQ
//