LOCUS       BAM58585.1               679 aa    PRT              BCT 07-OCT-2016
DEFINITION  Bacillus subtilis BEST7003 glycyl-tRNA synthetase subunit
            beta protein.
ACCESSION   AP012496-2384
PROTEIN_ID  BAM58585.1
SOURCE      Bacillus subtilis BEST7003
  ORGANISM  Bacillus subtilis BEST7003
            Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
REFERENCE   1  (bases 1 to 4043042)
  AUTHORS   Watanabe,S., Shiwa,Y., Itaya,M. and Yoshikawa,H.
  TITLE     Direct Submission
  JOURNAL   Submitted (02-AUG-2012) to the DDBJ/EMBL/GenBank databases.
            Contact:Hirofumi Yoshikawa
            Tokyo University of Agriculture, Department of Bioscience; 1-1-1
            Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
            URL    :http://nodai.cc-town.net/laboratory/single.php?id=23
REFERENCE   2
  AUTHORS   Watanabe,S., Shiwa,Y., Itaya,M. and Yoshikawa,H.
  TITLE     Complete Sequence of the First Chimera Genome Constructed by
            Cloning the Whole Genome of Synechocystis Strain PCC6803 into the
            Bacillus subtilis 168 Genome
  JOURNAL   J. Bacteriol. 194, 7007 (2012)
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Velevt v. 1.1.02
            Genome Coverage       :: 60x
            Sequencing Technology :: llumina Solexa
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /db_xref="taxon:1204342"
                     /mol_type="genomic DNA"
                     /organism="Bacillus subtilis BEST7003"
                     /strain="BEST7003"
     protein         /gene="glyS"
                     /locus_tag="BEST7003_2384"
                     /note="glycine--tRNA ligase beta chain; glyS;
                     classIIaminoacyl tRNA synthetase; tetramer of
                     alpha(2)beta(2);catalyzes a two-step reaction; first
                     charging a glycinemolecule by linking the carboxyl group
                     to thealpha-phosphate of ATP; second by transfer of
                     theaminoacyl-adenylate to its tRNA"
                     /transl_table=11
BEGIN
        1 MSKQDLLLEI GLEEMPARFL NESMVQLGDK LTGWLKEKNI THGEVKLFNT PRRLAVFVKD
       61 VAEKQDDIKE EAKGPAKKIA LDADGNWTKA AIGFSKGQGA NVEDLYIKEV KGIEYVFVQK
      121 FQAGQETKSL LPELSGLITS LHFPKNMRWG NEDLRYIRPI KWIVALFGQD VIPFSITNVE
      181 SGRTTQGHRF LGHEVSIESP SAYEEQLKGQ HVIADPSVRK QMIQSQLETM AAENNWSIPV
      241 DEDLLDEVNH LVEYPTALYG SFESEFLSIP EEVLVTTMKE HQRYFPVKDK NGDLLPHFIT
      301 VRNGNSHAIE NVARGNEKVL RARLSDASFF YKEDQKLNID ANVKKLENIV FHEELGSLAD
      361 KVRRVTSIAE KLAVRLQADE DTLKHVKRAA EISKFDLVTH MIYEFPELQG IMGEKYARML
      421 GEDEAVAAAV NEHYMPRSAG GETPSTFTGA VVAMADKLDT IASFFSIGVI PTGSQDPYGL
      481 RRQASGIVAI LLDRNWGISF EELLTFVQTD KENELLDFFT QRLKYVLNAE QIRHDVIDAV
      541 LESSELEPYS ALHKAQVLEQ KLGAPGFKET AEALGRVISI SKKGVRGDIQ PDLFENEYEA
      601 KLFDAYQTAK QNLQENFSKK DYEAALASLA ALKEPIDAYF DHTMVIADNE SLKANRLAQM
      661 VSLADEIKSF ANMNALIVK
//