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MNTR_BACCR
ID   MNTR_BACCR              Reviewed;         142 AA.
AC   Q818P5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=BC_4204;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP11119.1; -; Genomic_DNA.
DR   RefSeq; NP_833918.1; NC_004722.1.
DR   RefSeq; WP_001143085.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q818P5; -.
DR   SMR; Q818P5; -.
DR   STRING; 226900.BC_4204; -.
DR   EnsemblBacteria; AAP11119; AAP11119; BC_4204.
DR   GeneID; 67508842; -.
DR   KEGG; bce:BC4204; -.
DR   PATRIC; fig|226900.8.peg.4343; -.
DR   HOGENOM; CLU_069532_3_0_9; -.
DR   OMA; SWDAIDR; -.
DR   Proteomes; UP000001417; 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;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..142
FT                   /note="HTH-type transcriptional regulator MntR"
FT                   /id="PRO_0000201116"
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;  FFC0CD6FBE001EDB CRC64;
     MPTPSMEDYI EQIYLLIDEK GYARVSDIAE ALSVHPSSVT KMVQKLDKDE YLIYEKYRGL
     VLTTKGKKIG ERLVYRHDLL EQFMRIIGVD ESKIYNDVEG IEHHLSWEAI DRIGDLVQYF
     EQDTVRVETL RGVQRANEEK SN
 
 
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