MULTISPECIES: copper-sensing transcriptional repressor CsoR

LOCUS       WP_003723408              97 aa            linear   BCT 11-MAY-2020
            [Listeria].
ACCESSION   WP_003723408
VERSION     WP_003723408.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Corbett,D., Schuler,S., Glenn,S., Andrew,P.W., Cavet,J.S. and
            Roberts,I.S.
  TITLE     The combined actions of the copper-responsive repressor CsoR and
            copper-metallochaperone CopZ modulate CopA-mediated copper efflux
            in the intracellular pathogen Listeria monocytogenes
  JOURNAL   Mol. Microbiol. 81 (2), 457-472 (2011)
   PUBMED   21564342
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  :: BlastRule
            Evidence Accession :: NBR011917
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     gene            1..97
                     /gene="csoR"
     Protein         1..97
                     /product="copper-sensing transcriptional repressor CsoR"
                     /calculated_mol_wt=10931
     Region          13..96
                     /region_name="CsoR-like_DUF156"
                     /note="Transcriptional regulators CsoR (copper-sensitive
                     operon repressor), RcnR, and FrmR, and related domains;
                     this domain superfamily was previously known as DUF156;
                     cl00846"
                     /db_xref="CDD:445134"
     Site            order(15,18..19,22..23,26,29..30,32..33,36..39,41..43,
                     45..47,49..50,52..53,56..57,60..61,63..65,67..69,72,
                     80..81,83..92)
                     /site_type="other"
                     /note="putative homotetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:197392"
     Site            order(15,18..19,22..23,26,29..30,32..33,36..39,41..43,
                     45..47,49..50,52..53,56..57,60,63,67,86,89..92)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:197392"
     Site            order(41,67,86)
                     /site_type="other"
                     /note="putative allosteric switch controlling residues"
                     /db_xref="CDD:197392"
     Site            order(42,67,71)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197392"
     Site            order(61,64..65,68..69,71..72,80..81,83..85,87..88)
                     /site_type="other"
                     /note="putative homodimer-homodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:197392"
ORIGIN      
        1 mkhdqpivpr kedetkllqn rlrriegqir giaqmveddr yctdilvqis aankalknvg
       61 lqvlehhtah cvvdaaknge ddvmedllka irqfskt