MULTISPECIES: serine/threonine-protein kinase [Pseudomonas].

LOCUS       WP_003114615             329 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_003114615
VERSION     WP_003114615.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
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 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..329
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35986
     Region          50..316
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(50,74..75,110,115,120..123,137)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(57..58,60..63,65,84,86,118,136..139,143,145,183,185,
                     187..188,190,199..200,203,220,226..228)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(57..58,60..63,65,84,86,118,136..139,143,185,
                     187..188,190,199..200)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(61,143,145,183,185,187,203,220,226..228)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(199..207,216..220,226..228)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mneplsslel lpeeegganl tyfafaapta sapdlpavlp gplpdvlsgr yrlermlgag
       61 gmgtvyrard llheqfgdpa plvalkllne svaespdasa llysefaltr rlrhpnvvrl
      121 ftfdvdtacq rayivmelmp glpldrllce rpeglpwsel saiarplldv layvheqgvl
      181 hgdlkpsnvm lgeegvrlfd fglgqaqagi ldglpqlsrg ridawtpgya apellegapl
      241 spaadlyala cvlyeladgr hpfrrlpsnq areqglerql raprhlprrc wpalrtalsl
      301 dperrcigvr elqealgarr swlagvlar