M4 family metallopeptidase [Vibrio coralliilyticus].

LOCUS       WP_019276696             667 aa            linear   BCT 21-JAN-2025
ACCESSION   WP_019276696
VERSION     WP_019276696.1
KEYWORDS    RefSeq.
SOURCE      Vibrio coralliilyticus
  ORGANISM  Vibrio coralliilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Vibrio coralliilyticus"
                     /db_xref="taxon:190893"
     Protein         1..667
                     /product="M4 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=74019
     Region          1..604
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrnvnllmlf pmafasqaan vvdysqvdls qvlnppttra fsapnqplay qdasrvkags
       61 qtllrkqqlh ygvpvygqsl vaqvstqgkv tpvdgkvltg idadigstlp mlnakqaiel
      121 akgnsqgfas qairdpnael miwqdeqqia rlvykvdfiq mngmgpsrpi tlvdaksgdv
      181 ldrwegiafi eaegpggnrk sgryyfgpkt qyggfevnqy cqmdspnvvt lnmnnqqygg
      241 qvhqfdcnvn nyrsvngaya pmndahyfgq rvfdmymdwl ntrpiqqklt mrvhygsnyg
      301 nafwdgrqmt fgdgnqsmyp latwdviahe vshgfteqns gleyrgmsgg mnesfsdvaa
      361 aalsqyvhgs fnwkmgehvm kysdamryfi qpskdgvsid hinqyyngid vhhssgvfnk
      421 afyhlatssn wdikkafiay atanqlywrp nsdfqqgaeg vckaahelgy dtsavnnafa
      481 qvgiqvtqca sgqpdpeptp npdivslqin ipsaiesagn deqhfvlkna paediwvqty
      541 ngygnvdmyv ainrpaslsd hdcastnrdn neycgfsgvg dadvyvmvtg arsssdayvg
      601 vsayleeptp epqdlcanle ewspyyyypq gtevqsygnr fvatqtnwga dpysyywyws
      661 fegsclq