LOCUS       BAQ45314.1               333 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum Hsp33-like chaperonin protein.
ACCESSION   AP014704-1874
PROTEIN_ID  BAQ45314.1
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         /inference="similar to AA sequence:RefSeq:WP_015933750.1"
                     /locus_tag="Maq22A_c10165"
                     /note="173d0011"
                     /note="becomes active under oxidative stress; four
                     conserved cysteines bind a zinc atom when they are in the
                     reduced state and the enzyme is inactive; oxidative stress
                     results in oxidized cysteines, release of zinc, and
                     binding of Hsp33 to aggregation-prone proteins; forms
                     dimers and higher order oligomers; Derived by automated
                     computational analysis using gene prediction method:
                     Protein Homology."
                     /transl_table=11
BEGIN
        1 MSETTSSQSP EGRDDAILPF AVEPLDVRGR AVRLGPSLDT ILRRHGYPDT VARLLGEATA
       61 LTVLLGSSLK FEGRFQLQTK SDGPVDMVVV DFEAPDRVRA TARFDAGRVA AAGPRADTAQ
      121 LLGHGHLAMT IDQGSVQSRY QGVVALEGQG FEEAAHQYFR QSEQIPTRVR LAVAEQVEGS
      181 GEAWRAGGLL MQFLPHSPER ARLADLPPGD LPEGHTFLDD SASREDDAWV EAKSLVATIE
      241 DHELVDPTVS SERLLYRLFH ERGVRVFEAQ GVHEACRCSR ERVMGMVRNF SAEERRDIVG
      301 EDGRIGITCE FCSRHYDLDP AEVEAEIVGG QPA
//