M48 family metalloprotease [Pseudomonas aeruginosa].

LOCUS       WP_003113755             485 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_003113755
VERSION     WP_003113755.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Quigley,A., Dong,Y.Y., Pike,A.C., Dong,L., Shrestha,L.,
            Berridge,G., Stansfeld,P.J., Sansom,M.S., Edwards,A.M., Bountra,C.,
            von Delft,F., Bullock,A.N., Burgess-Brown,N.A. and Carpenter,E.P.
  TITLE     The structural basis of ZMPSTE24-dependent laminopathies
  JOURNAL   Science 339 (6127), 1604-1607 (2013)
   PUBMED   23539603
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Pryor,E.E. Jr., Horanyi,P.S., Clark,K.M., Fedoriw,N.,
            Connelly,S.M., Koszelak-Rosenblum,M., Zhu,G., Malkowski,M.G.,
            Wiener,M.C. and Dumont,M.E.
  TITLE     Structure of the integral membrane protein CAAX protease Ste24p
  JOURNAL   Science 339 (6127), 1600-1604 (2013)
   PUBMED   23539602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF013594.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF01435.24
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..485
                     /product="M48 family metalloprotease"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53932
     Region          <60..481
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          218..446
                     /region_name="M48_Ste24p_like"
                     /note="M48 Ste24 endopeptidase-like, integral membrane
                     metallopeptidase; cd07328"
                     /db_xref="CDD:320687"
     Site            order(298..299,302,366,370,439)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320687"
     Site            order(298,302,366,439)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320687"
ORIGIN      
        1 mshdtlrvrl laflflipla lyawsavqaf rvdstlrdeq fmrdwsasvr ndpdaagaip
       61 rhlfrpaygv eghlhqfaed aeairrdhpw lalrgwlaai gklcalasal vaaallarle
      121 ydgrrsmrsq ayllghlapa wrrlgrlvpl hagllvaala sqllyealws yshwhshgfv
      181 allfslplwl lflggllmlr rlrgellple epvlhllgre ldrvaapglw qwlgqiadra
      241 gaplpdhvvt giehcyfvtq akvllaprgi plegrtlyip ltyasvmsea esaaiighel
      301 ghfaagdtah gaslsllqrq vrlridriaa pevghvgllg kpglwaalyf ldrferaylh
      361 wnrrqelaad kvgarvagar vfaiallrtc alaglierll aspqtrnlvh altdhlrgns
      421 leldeqdsar rlehpfdshp ptyqriadls laldddllrq arrivsaddt qwlnrlldag
      481 hgesr