LOCUS       BAQ43857.1               454 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum response regulator PleD protein.
ACCESSION   AP014704-345
PROTEIN_ID  BAQ43857.1
SOURCE      Methylobacterium aquaticum
  ORGANISM  Methylobacterium aquaticum
            Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
            Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (bases 1 to 5348274)
  AUTHORS   Tani,A. and Ogura,Y.
  TITLE     Direct Submission
  JOURNAL   Submitted (21-JAN-2015) to the DDBJ/EMBL/GenBank databases.
            Contact:Akio Tani
            Okayama University, Institute of Plant Science and Resources; Chuo
            2-20-1, Kurashiki, Okayama 710-0046, Japan
REFERENCE   2
  AUTHORS   Tani,A., Ogura,Y., Hayashi,T. and Kimbara,K.
  TITLE     Complete Genome Sequence of Methylobacterium aquaticum Strain 22A,
            Isolated from Racomitrium japonicum Moss
  JOURNAL   Genome Announc 3, e00266-15 (2015)
  REMARK    Publication Status: Online-Only
            DOI:10.1128/genomeA.00266-15
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.7
            Genome Coverage       :: 47x
            Sequencing Technology :: 454 GS FLX; ABI 3730; Illumina PE
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /culture_collection="NBRC:FERM BP-11078"
                     /db_xref="taxon:270351"
                     /mol_type="genomic DNA"
                     /organism="Methylobacterium aquaticum"
                     /strain="MA-22A"
     protein         /gene="pleD"
                     /inference="similar to AA sequence:RefSeq:WP_012336306.1"
                     /locus_tag="Maq22A_c01810"
                     /note="1d0008"
                     /note="involved in swarmer-to-stalked cell differentiation
                     in Caulobacter crescentus; catalyzes the condensation of
                     two GTP molecules to form the secondary messenger cyclic
                     di-GMP (c-di-GMP); upon phosphorylation of domain D1 the
                     protein dimerizes; presumably this allows the two
                     GTP-bound GGDEF (diguanylate cyclase) domains to catalyze
                     the condensation reaction; allosterically inhibited by
                     c-di-GMP; Derived by automated computational analysis
                     using gene prediction method: Protein Homology."
                     /transl_table=11
BEGIN
        1 MSARVLIVDD LFPNIKLLET KLTLEYFDVV SAMNGPDALA ICEKGLCDIV LLDVMMPGMD
       61 GFEVCRRIKA TPTTAHLPVV MVTALDQPSD RLRGLDAGAD DFLTKPIDDT ALMARVRSLV
      121 RLKAVTDELR SRAMASRVGD PLAAAAAETG HNANVLIVED RRSAADRLSA ALGQYHCVET
      181 VATPQEALER VKAGEYDVVL VSLDLQDHDG LRLCSQLRSL DRTRTVPVVM LADAGDRARI
      241 MRGLDLGVHD YLVRPIDRNE LVARVRTQVK RKRFSHSLRE SVQASMDLAV TDGLTGLHNR
      301 RYLDSYLAGL FSEPSLRDRP VSLLILDIDR FKSINDRFGH DAGDEVLKEF ATRIRSQTRG
      361 IDVVARFGGE EIVVVVPDTA LEAARQVAER IRERIEAAPF VVQRGTCSID VTVSIGVAAR
      421 QAGDGEPGAL LKRADLALYE AKQTGRNRVV AAAA
//