MULTISPECIES: formaldehyde-responsive transcriptional repressor

LOCUS       WP_001141271              91 aa            linear   BCT 28-MAY-2024
            FrmR [Pseudomonadota].
ACCESSION   WP_001141271
VERSION     WP_001141271.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Osman,D., Piergentili,C., Chen,J., Sayer,L.N., Uson,I.,
            Huggins,T.G., Robinson,N.J. and Pohl,E.
  TITLE     The Effectors and Sensory Sites of Formaldehyde-responsive
            Regulator FrmR and Metal-sensing Variant
  JOURNAL   J. Biol. Chem. 291 (37), 19502-19516 (2016)
   PUBMED   27474740
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Chen,N.H., Djoko,K.Y., Veyrier,F.J. and McEwan,A.G.
  TITLE     Formaldehyde Stress Responses in Bacterial Pathogens
  JOURNAL   Front Microbiol 7, 257 (2016)
   PUBMED   26973631
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  :: HMM
            Evidence Accession :: NF008464.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11352
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     gene            1..91
                     /gene="frmR"
     Protein         1..91
                     /product="formaldehyde-responsive transcriptional
                     repressor FrmR"
                     /calculated_mol_wt=10187
     Region          1..91
                     /region_name="PRK11352"
                     /note="formaldehyde-responsive transcriptional repressor
                     FrmR"
                     /db_xref="CDD:183095"
     Site            order(3,35,60,64)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197388"
     Site            order(8,11..12,15..16,19,22..23,25..26,29..32,34..36,
                     38..40,42..43,45..46,49..50,53..54,56..58,60..62,65,
                     75..76,78..87)
                     /site_type="other"
                     /note="putative homotetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:197388"
     Site            order(8,11..12,15..16,19,22..23,25..26,29..32,34..36,
                     38..40,42..43,45..46,49..50,53,56,60,81,84..87)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:197388"
     Site            order(54,57..58,61..62,64..65,75..76,78..80,82..83)
                     /site_type="other"
                     /note="putative homodimer-homodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:197388"
     Site            order(60,81)
                     /site_type="other"
                     /note="putative allosteric switch controlling residues"
                     /db_xref="CDD:197388"
ORIGIN      
        1 mpstpeekkk vltrvrrirg qidalersle gdaecrailq qiaavrgaan glmaevlesh
       61 iretfdrndc ysrevsqsvd dtielvrayl k