MNTR_ALKHC
ID MNTR_ALKHC Reviewed; 139 AA.
AC Q9K943;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=BH2807;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06526.1; -; Genomic_DNA.
DR PIR; G84000; G84000.
DR RefSeq; WP_010898955.1; NC_002570.2.
DR PDB; 6KTA; X-ray; 2.30 A; A/B=1-139.
DR PDB; 6KTB; X-ray; 2.50 A; A/B=1-139.
DR PDBsum; 6KTA; -.
DR PDBsum; 6KTB; -.
DR AlphaFoldDB; Q9K943; -.
DR SMR; Q9K943; -.
DR STRING; 272558.10175428; -.
DR EnsemblBacteria; BAB06526; BAB06526; BAB06526.
DR KEGG; bha:BH2807; -.
DR eggNOG; COG1321; Bacteria.
DR HOGENOM; CLU_069532_3_0_9; -.
DR OMA; SWDAIDR; -.
DR OrthoDB; 2047422at2; -.
DR Proteomes; UP000001258; 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 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Manganese; Metal-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..139
FT /note="HTH-type transcriptional regulator MntR"
FT /id="PRO_0000201117"
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"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:6KTA"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:6KTA"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6KTA"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6KTA"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6KTA"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6KTA"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:6KTA"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6KTA"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6KTA"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:6KTA"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:6KTA"
SQ SEQUENCE 139 AA; 16359 MW; 3DA9B784923B4A45 CRC64;
MPTPSMEDYL ERIYLLIEEK GYARVSDIAE ALEVHPSSVT KMVQKLDKSD YLVYERYRGL
ILTAKGKKIG KRLVYRHDLL EDFLKMIGVD SDHIYEDVEG IEHHLSWDAI DRIGDLVQYF
QEDPSRLNDL REVQKKNEE
