ID   MNTR_BACC1              Reviewed;         142 AA.
AC   Q730Y9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=HTH-type transcriptional regulator MntR {ECO:0000255|HAMAP-Rule:MF_00732};
DE   AltName: Full=Manganese transport regulator {ECO:0000255|HAMAP-Rule:MF_00732};
GN   Name=mntR {ECO:0000255|HAMAP-Rule:MF_00732}; OrderedLocusNames=BCE_4277;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- FUNCTION: Central regulator of manganese homeostasis.
CC       {ECO:0000255|HAMAP-Rule:MF_00732}.
CC   -!- ACTIVITY REGULATION: DNA binding is strongly activated by Mn(2+).
CC       {ECO:0000255|HAMAP-Rule:MF_00732}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00732}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00732}.
CC   -!- SIMILARITY: Belongs to the DtxR/MntR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00732}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017194; AAS43178.1; -; Genomic_DNA.
DR   RefSeq; WP_001143076.1; NC_003909.8.
DR   AlphaFoldDB; Q730Y9; -.
DR   SMR; Q730Y9; -.
DR   EnsemblBacteria; AAS43178; AAS43178; BCE_4277.
DR   GeneID; 59155221; -.
DR   GeneID; 64199555; -.
DR   KEGG; bca:BCE_4277; -.
DR   HOGENOM; CLU_069532_3_0_9; -.
DR   OMA; SWDAIDR; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0030026; P:cellular manganese ion homeostasis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.60.10; -; 1.
DR   HAMAP; MF_00732; HTH_MntR; 1.
DR   InterPro; IPR001367; Fe_dep_repressor.
DR   InterPro; IPR036421; Fe_dep_repressor_sf.
DR   InterPro; IPR022687; HTH_DTXR.
DR   InterPro; IPR022897; HTH_tscrpt_reg_MntR.
DR   InterPro; IPR022689; Iron_dep_repressor.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF02742; Fe_dep_repr_C; 1.
DR   Pfam; PF01325; Fe_dep_repress; 1.
DR   SMART; SM00529; HTH_DTXR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47979; SSF47979; 1.
DR   PROSITE; PS50944; HTH_DTXR; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Manganese; Metal-binding; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..142
FT                   /note="HTH-type transcriptional regulator MntR"
FT                   /id="PRO_0000285038"
FT   DOMAIN          1..63
FT                   /note="HTH dtxR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         8
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         11
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         99
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         99
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00732"
SQ   SEQUENCE   142 AA;  16596 MW;  732464522FB01811 CRC64;
     MPTPSMEDYI EQIYLLIDEK GYARVSDIAE ALSVHPSSVT KMVQKLDKDE YLIYEKYRGL
     VLTSKGKKIG ERLVYRHELL EQFMRIIGVD ESKIYNDVEG IEHHLSWEAI DRIGDLVQYF
     EQDEVRVETL RGVQKANEEK SN