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Database: UniProt/TrEMBL
Entry: K7ZG86_BDEBC
LinkDB: K7ZG86_BDEBC
Original site: K7ZG86_BDEBC 
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
//
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