MNTR_LISMH
ID MNTR_LISMH Reviewed; 142 AA.
AC B8DDM5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=LMHCC_0679;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/jb.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(2011).
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}.
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DR EMBL; CP001175; ACK39034.1; -; Genomic_DNA.
DR RefSeq; WP_003725831.1; NC_011660.1.
DR AlphaFoldDB; B8DDM5; -.
DR SMR; B8DDM5; -.
DR KEGG; lmh:LMHCC_0679; -.
DR HOGENOM; CLU_069532_3_0_9; -.
DR OMA; SWDAIDR; -.
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_1000190481"
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; 16392 MW; DFFB6F2174CB5E56 CRC64;
MPTPSMEDYI EKIYSLIETK GYARVSDIAD ELFVHPSSVT KMVQKLDKDE YLIYEKYRGL
ILTPKGTQMG KRLLERHALL ESFLSIIGVD PSHIYHDVEG IEHHLSWNSI DRIGDVVQFF
ENHPDALKTL KAMETTKPET KE
