ID A0A0M0GP40_9BACI Unreviewed; 138 AA.
AC A0A0M0GP40;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=HTH-type transcriptional regulator MntR {ECO:0000256|HAMAP-Rule:MF_00732};
DE AltName: Full=Manganese transport regulator {ECO:0000256|HAMAP-Rule:MF_00732};
GN Name=mntR {ECO:0000256|HAMAP-Rule:MF_00732,
GN ECO:0000313|EMBL:TYS56525.1};
GN ORFNames=AF331_03595 {ECO:0000313|EMBL:KON91604.1}, FZC83_02845
GN {ECO:0000313|EMBL:TYS56525.1};
OS Rossellomorea marisflavi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON91604.1, ECO:0000313|Proteomes:UP000037405};
RN [1] {ECO:0000313|Proteomes:UP000037405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14235 jcm11544.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KON91604.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 11544 {ECO:0000313|EMBL:KON91604.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TYS56525.1, ECO:0000313|Proteomes:UP000322997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH108_3D {ECO:0000313|EMBL:TYS56525.1,
RC ECO:0000313|Proteomes:UP000322997};
RA Olmedo-Alvarez G.;
RT "Bacillus genomes from the desert of Cuatro Cienegas, Coahuila.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Central regulator of manganese homeostasis.
CC {ECO:0000256|HAMAP-Rule:MF_00732}.
CC -!- ACTIVITY REGULATION: DNA binding is strongly activated by Mn(2+).
CC {ECO:0000256|HAMAP-Rule:MF_00732}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00732}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00732}.
CC -!- SIMILARITY: Belongs to the DtxR/MntR family.
CC {ECO:0000256|ARBA:ARBA00007871, ECO:0000256|HAMAP-Rule:MF_00732}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KON91604.1}.
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DR EMBL; LGUE01000001; KON91604.1; -; Genomic_DNA.
DR EMBL; VTEQ01000001; TYS56525.1; -; Genomic_DNA.
DR RefSeq; WP_053426793.1; NZ_VTEQ01000001.1.
DR AlphaFoldDB; A0A0M0GP40; -.
DR STRING; 189381.GCA_900166615_03580; -.
DR GeneID; 42291012; -.
DR PATRIC; fig|189381.12.peg.822; -.
DR OrthoDB; 9791355at2; -.
DR Proteomes; UP000037405; Unassembled WGS sequence.
DR Proteomes; UP000322997; Unassembled WGS sequence.
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:intracellular manganese ion homeostasis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.60.10; Iron dependent repressor, metal binding and dimerisation domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR33238; IRON (METAL) DEPENDENT REPRESSOR, DTXR FAMILY; 1.
DR PANTHER; PTHR33238:SF7; TRANSCRIPTIONAL REGULATOR MNTR; 1.
DR Pfam; PF02742; Fe_dep_repr_C; 1.
DR Pfam; PF01325; Fe_dep_repress; 1.
DR SMART; SM00529; HTH_DTXR; 1.
DR SUPFAM; SSF47979; Iron-dependent repressor protein, dimerization domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50944; HTH_DTXR; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_00732};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00732};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00732};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00732};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00732}; Reference proteome {ECO:0000313|Proteomes:UP000037405};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_00732};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00732};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00732}.
FT DOMAIN 1..63
FT /note="HTH dtxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50944"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00732"
SQ SEQUENCE 138 AA; 16274 MW; 29F501C7EEDD2945 CRC64;
MPTPSMEDYI EQIYLLIENK GYARVSDIAE ALSVHPSSVT KMVQKLDKDD YLVYEKYRGL
VLTPKGNKVG KRLVYRHELL EQFLTVIGVK DEHIYEDVEG IEHHLSWDSI DRIGDLVQYF
EEDKKRVEEL RFIQNRSE
//