LOCUS       CAQ85805.1               419 aa    PRT              BCT 27-FEB-2015
DEFINITION  Photorhabdus asymbiotica PirB similarities with putative
            juvenile hormone esterase protein.
ACCESSION   FM162591-3712
PROTEIN_ID  CAQ85805.1
SOURCE      Photorhabdus asymbiotica
  ORGANISM  Photorhabdus asymbiotica
            Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
            Morganellaceae; Photorhabdus.
REFERENCE   1  (bases 1 to 5064808)
  AUTHORS   Crossman L.C.
  JOURNAL   Submitted (21-MAY-2008) to the INSDC. Crossman L.C., Pathogen
            Sequencing Unit, The Wellcome Trust Sanger Institute, Hinxton,
            Cambridge, Cambridgeshire, CB10 1SA, UNITED KINGDOM.
REFERENCE   2
  AUTHORS   Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
            Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
            Doggett J., Ormond D., Mayho M., Bason N., Smith F., Simmonds M.,
            Arrowsmith C., Churcher C., Harris D., Thompson N.R., Quail M.,
            Parkhill J., Ffrench-Constant R.H.
  TITLE     Comparative genomics of the emerging human pathogen Photorhabdus
            asymbiotica with the insect pathogen Photorhabdus luminescens
  JOURNAL   BMC Genomics 10(1), 302-302(2009).
   PUBMED   19583835
FEATURES             Qualifiers
     source          /organism="Photorhabdus asymbiotica"
                     /isolate="ATCC43949"
                     /mol_type="genomic DNA"
                     /db_xref="taxon:291112"
     protein         /transl_table=11
                     /gene="PirB"
                     /locus_tag="PAU_03717"
                     /old_locus_tag="PAT0561"
                     /note="This family contains insecticidal toxins produced
                     by Bacillus species of bacteria. During spore formation
                     the bacteria produce crystals of this protein. When an
                     insect ingests these proteins they are activated by
                     proteolytic cleavage. The N-terminus is cleaved in all of
                     the proteins and a C-terminal extension is cleaved in some
                     members. Once activated the endotoxin binds to the gut
                     epithelium and causes cell lysis by the formation of
                     cation-selective channels, which leads to death. The
                     activated toxin is composed of three distinct domains: an
                     N-terminal helical bundle domain involved in membrane
                     insertion and pore formation; a beta-sheet domain involved
                     in receptor binding; and a C-terminal beta-sandwich domain
                     that interacts with the N-terminal domain to form a
                     channel , . This entry represents the conserved N-terminal
                     domain."
                     /db_xref="EnsemblGenomes-Gn:PAU_03717"
                     /db_xref="EnsemblGenomes-Tr:CAQ85805"
                     /db_xref="GOA:C7BLU9"
                     /db_xref="InterPro:IPR005639"
                     /db_xref="InterPro:IPR036716"
                     /db_xref="UniProtKB/TrEMBL:C7BLU9"
                     /inference="similar to DNA sequence:INSD:BX571872"
                     /inference="similar to DNA sequence:INSD:AF039135"
BEGIN
        1 MQTENVLDIR TIVANEYAVK TSALEWDVTD IVKNAIIGGI SFIPSVGPAI SFLVGLFWPQ
       61 SKENIWEGIV KQIERMIEES ALKTIKGILA GDIAYIQERM ATVADLLEKH PGSAEARNAF
      121 NNLAENIDGY HKKFNNFSDD VNYQILPMFS TTVMMQITYW VAGLERKEEI GLSDIDIEKV
      181 RGLVKKTVEQ ANSYINNIYD RELNDALNNS TADTVVNNVM SVHGHCRLHG IEYISIWDRL
      241 SETESVNNRI YVDVLSYSTF FDRQTAKARI QALTPEKDMT PPLKPALNGG KRRKINSLMG
      301 HIVRIGGAPR VGGLTVVFDD GSRHQLGTIS GETASISLDS SRITSLEVWG NGAVDKAVFT
      361 LSDGRSLSFG EPGTSRYRKF YVGESHYISG IYLSSDYSPL VGQAANIAVS YQLINDDEK
//