LOCUS       CAQ84958.1               400 aa    PRT              BCT 27-FEB-2015
DEFINITION  Photorhabdus asymbiotica penicillin-binding protein 6
            (d-alanyl-d-alanine carboxypeptidas fraction c) (dd-pept
            (dd-carboxypeptidase) (pbp-6)idase) protein.
ACCESSION   FM162591-2865
PROTEIN_ID  CAQ84958.1
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="dacC"
                     /locus_tag="PAU_02870"
                     /old_locus_tag="PAT1418"
                     /EC_number="3.4.16.4"
                     /note="present in the penicillin-binding protein family of
                     beta-lactamases, which constitute the most common
                     bacterial resistance mechanism against beta-lactam
                     antibiotics . Beta-lactamases appear to have evolved from
                     DD-transpeptidases, which are penicillin-binding proteins
                     involved in cell wall biosynthesis, and as such are one of
                     the main targets of beta-lactam antibiotics"
                     /db_xref="EnsemblGenomes-Gn:PAU_02870"
                     /db_xref="EnsemblGenomes-Tr:CAQ84958"
                     /db_xref="GOA:C7BR03"
                     /db_xref="InterPro:IPR001967"
                     /db_xref="InterPro:IPR012338"
                     /db_xref="InterPro:IPR012907"
                     /db_xref="InterPro:IPR015956"
                     /db_xref="InterPro:IPR018044"
                     /db_xref="InterPro:IPR037167"
                     /db_xref="UniProtKB/TrEMBL:C7BR03"
                     /inference="similar to DNA sequence:INSD:BX571864"
                     /inference="similar to DNA sequence:INSD:AE014075"
BEGIN
        1 MKKNLAMTVK CVTAVLAVIL VANTHAYASD EPLVPSVDAK AYVLMDYDSG KILASNNPDE
       61 RLDPASLTKI MTSYVIGQAI KAGKITPEDV VTVGKDAWAT GNPVLKGSSL MFLKPGDQVK
      121 VIDLNRGIVI QSGNDASIAL ADYVAGSQDT FVSLMNNYVK SLGLTNTHFQ TVHGLDAEGQ
      181 FSTARDMAVL SQAMIRDVPD EYVLHKEKAF TFNKIQQPNR NRLLWNKSIN VDGVKTGYTS
      241 GAGYNLVASA TEGPMRLISV VLGAPSDRVR FAESEKLLSW GFRFYETVTP IKASESFVSE
      301 KVWYGDRSDV VLGVEKDAAI TIPRGQLKNL KASYTLNQTP LEAPLAKNQV VGVINFQLGD
      361 KVIGHRPLVV KETVEEGGFF SRIWDFIVMK VSSWFNAIFD
//