LOCUS       BAQ44114.1               567 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum lysine--tRNA ligase protein.
ACCESSION   AP014704-620
PROTEIN_ID  BAQ44114.1
SOURCE      Methylobacterium aquaticum
  ORGANISM  Methylobacterium aquaticum
            Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
            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         /EC_number="6.1.1.6"
                     /gene="lysS"
                     /inference="similar to AA sequence:RefSeq:WP_015933518.1"
                     /locus_tag="Maq22A_c03350"
                     /note="149d0005"
                     /note="class I; LysRS1; catalyzes a two-step reaction,
                     first charging a lysine molecule by linking its carboxyl
                     group to the alpha-phosphate of ATP, followed by transfer
                     of the aminoacyl-adenylate to its tRNA; in Methanosarcina
                     barkeri this enzyme charges both tRNA molecules for lysine
                     that exist in this organism (but the tRNALysUUU very
                     poorly) and in the presence of LysRS2 can charge tRNAPyl
                     with lysine; Derived by automated computational analysis
                     using gene prediction method: Protein Homology."
                     /transl_table=11
BEGIN
        1 MPAPFRIDPA LAEAAASASA WPFEEARKLV ARLERTGKGE VLFETGYGPS GLPHIGTFGE
       61 VARTSMVRHA FRTLTNDSVP TRLVAFSDDM DGLRKVPENV PNKALLAENL NKPLTAVPDP
      121 FGTHDSFGAH NNAELRRFLD KFGFEYEFLS ATECYRAGRF DATLLRVLER YDAVMAVMLP
      181 SLRAERSASY SPFLPLHPVT GHVMQVPIDE VKVSSGTIVW RDPATGEAYE TPVTGGHAKL
      241 QWKPDWAMRW VALGVDYEMA GKDLIDSVKL SGQIARVLGA EPPEGFNYEL FLDEKGQKIS
      301 KSKGNGLTID EWLAYGTPES LALFMYNKPR EAKRLHFDVI PRHVDDYLSF LEKFPGQEPK
      361 LKLGNPTWHL HAGTPPEPER VGEGGALPFA MLLNLVAVAN TEDPAVLWGF IRRYAPEASP
      421 ETHPRLDRLV HHAVRYFRDF VRPEKTYRTP SAEEAAALAD LSETLAAQTG STDPEALQAA
      481 VYEVGRRHFP DLSGKSKSPD GRPGVSQTWF TTLYGILLGE ARGPRFGSFV ALYGVEETRA
      541 LIARALSGAL AEEHAAFLES RDTPQAA
//