LOCUS       CAQ84874.1               265 aa    PRT              BCT 27-FEB-2015
DEFINITION  Photorhabdus asymbiotica type 4 prepilin-like proteins
            leader peptide processing enzyme (pecti enzymes secretion
            protein outo) protein.
ACCESSION   FM162591-2781
PROTEIN_ID  CAQ84874.1
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="pppA"
                     /locus_tag="PAU_02785"
                     /old_locus_tag="PAT1501"
                     /EC_number="2.1.1.-"
                     /note="The bifunctional enzyme prepilin peptidase (PilD)
                     from Pseudomonas aeruginosa is a key determinant in both
                     type-IV pilus biogenesis and extracellular protein
                     secretion, in its roles as a leader peptidase and methyl
                     transferase (MTase). It is responsible for endopeptidic
                     cleavage of the unique leader peptides that characterise
                     type-IV pilin precursors, as well as proteins with
                     homologous leader sequences that are essential components
                     of the general secretion pathway found in a variety of
                     Gram-negative pathogens."
                     /db_xref="EnsemblGenomes-Gn:PAU_02785"
                     /db_xref="EnsemblGenomes-Tr:CAQ84874"
                     /db_xref="GOA:C7BQ99"
                     /db_xref="InterPro:IPR000045"
                     /db_xref="InterPro:IPR010627"
                     /db_xref="InterPro:IPR014032"
                     /db_xref="UniProtKB/TrEMBL:C7BQ99"
                     /inference="similar to DNA sequence:INSD:BX571864"
                     /inference="similar to DNA sequence:INSD:CP000243"
BEGIN
        1 MMMGWLQSSI GCLVLTSGLL GLCVGSFLNV VICRLPIMII SESNNETTGF NLCFPSSHCP
       61 RCGRVLAVRD NIPLLSYLCR KGRCRYCNGM ISLRYPLVEG TMAALFSLLA LFTGWHYSLL
      121 GLWGLSSMLV ALAVIDVEYM LLPDQLTLSL LWLGLLFNLD SAGFVALPLA ISGAVCGYLF
      181 FRLVEWIARQ LFQRDALGMG DAKFLAALGA WLGVAALPWV VLLAASLTLI SYLTIWRFRS
      241 IRTAPQIPFG PGLAVAGLIV AFCQR
//