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P54512

- MNTR_BACSU

UniProt

P54512 - MNTR_BACSU

Protein

Transcriptional regulator MntR

Gene

mntR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Central regulator of manganese homeostasis. In the presence of manganese, it mediates repression of the manganese transporter MntH; under low manganese conditions, it activates the transcription of the mntABCD operon.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-HAMAP
    2. manganese ion binding Source: UniProtKB-HAMAP
    3. sequence-specific DNA binding transcription factor activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cellular manganese ion homeostasis Source: UniProtKB-HAMAP
    2. positive regulation of transcription, DNA-templated Source: UniProtKB-HAMAP
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Manganese

    Enzyme and pathway databases

    BioCyciBSUB:BSU24520-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional regulator MntR
    Alternative name(s):
    Manganese transport regulator
    Gene namesi
    Name:mntR
    Synonyms:yqhN
    Ordered Locus Names:BSU24520
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU24520. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 142142Transcriptional regulator MntRPRO_0000201118Add
    BLAST

    Proteomic databases

    PaxDbiP54512.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    STRINGi224308.BSU24520.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2017
    Helixi25 – 328
    Helixi36 – 4813
    Beta strandi51 – 555
    Turni56 – 583
    Beta strandi59 – 624
    Helixi64 – 8623
    Helixi91 – 10111
    Helixi102 – 1043
    Helixi107 – 12115
    Helixi124 – 13411
    Helixi139 – 1413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ON1X-ray1.75A/B1-142[»]
    1ON2X-ray1.61A/B1-142[»]
    2EV0X-ray1.65A/B1-142[»]
    2EV5X-ray2.00A/B1-142[»]
    2EV6X-ray1.70A/B1-142[»]
    2F5CX-ray2.40A1-142[»]
    2F5DX-ray1.90A/B1-142[»]
    2F5EX-ray2.20A/B1-142[»]
    2F5FX-ray2.40A/B1-142[»]
    2HYFX-ray2.80A/B/C/D1-142[»]
    2HYGX-ray2.80D1-142[»]
    3R60X-ray1.80A/B2-142[»]
    3R61X-ray1.90A/B2-142[»]
    4HV5X-ray1.90A/B2-142[»]
    4HV6X-ray2.30A/B2-142[»]
    4HX4X-ray1.65A/B2-142[»]
    4HX7X-ray1.90A/B2-142[»]
    4HX8X-ray2.00A/B2-142[»]
    ProteinModelPortaliP54512.
    SMRiP54512. Positions 4-140.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54512.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6363HTH dtxR-typeAdd
    BLAST

    Domaini

    It contains an N-terminal DNA-binding domain and a metal-binding domain.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1321.
    HOGENOMiHOG000040349.
    OrthoDBiEOG6M9F3P.
    PhylomeDBiP54512.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.60.10. 1 hit.
    HAMAPiMF_00732. HTH_MntR.
    InterProiIPR001367. Fe_dep_repressor.
    IPR022689. Fe_dep_repressor_HTH_DtxR.
    IPR022687. Fe_dep_repressor_HTH_DtxR_N.
    IPR022897. Tscrpt_reg_MntR.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF02742. Fe_dep_repr_C. 1 hit.
    PF01325. Fe_dep_repress. 1 hit.
    [Graphical view]
    SMARTiSM00529. HTH_DTXR. 1 hit.
    [Graphical view]
    SUPFAMiSSF47979. SSF47979. 1 hit.
    PROSITEiPS50944. HTH_DTXR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54512-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTPSMEDYI EQIYMLIEEK GYARVSDIAE ALAVHPSSVT KMVQKLDKDE    50
    YLIYEKYRGL VLTSKGKKIG KRLVYRHELL EQFLRIIGVD EEKIYNDVEG 100
    IEHHLSWNSI DRIGDLVQYF EEDDARKKDL KSIQKKTEHH NQ 142
    Length:142
    Mass (Da):16,759
    Last modified:July 7, 2009 - v2
    Checksum:i653BD8E0F4AB9F2C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811E → D in BAA12551. (PubMed:8969508)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84432 Genomic DNA. Translation: BAA12551.1.
    AL009126 Genomic DNA. Translation: CAB14383.2.
    PIRiE69959.
    RefSeqiNP_390332.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14383; CAB14383; BSU24520.
    GeneIDi938554.
    KEGGibsu:BSU24520.
    PATRICi18976738. VBIBacSub10457_2559.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84432 Genomic DNA. Translation: BAA12551.1 .
    AL009126 Genomic DNA. Translation: CAB14383.2 .
    PIRi E69959.
    RefSeqi NP_390332.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ON1 X-ray 1.75 A/B 1-142 [» ]
    1ON2 X-ray 1.61 A/B 1-142 [» ]
    2EV0 X-ray 1.65 A/B 1-142 [» ]
    2EV5 X-ray 2.00 A/B 1-142 [» ]
    2EV6 X-ray 1.70 A/B 1-142 [» ]
    2F5C X-ray 2.40 A 1-142 [» ]
    2F5D X-ray 1.90 A/B 1-142 [» ]
    2F5E X-ray 2.20 A/B 1-142 [» ]
    2F5F X-ray 2.40 A/B 1-142 [» ]
    2HYF X-ray 2.80 A/B/C/D 1-142 [» ]
    2HYG X-ray 2.80 D 1-142 [» ]
    3R60 X-ray 1.80 A/B 2-142 [» ]
    3R61 X-ray 1.90 A/B 2-142 [» ]
    4HV5 X-ray 1.90 A/B 2-142 [» ]
    4HV6 X-ray 2.30 A/B 2-142 [» ]
    4HX4 X-ray 1.65 A/B 2-142 [» ]
    4HX7 X-ray 1.90 A/B 2-142 [» ]
    4HX8 X-ray 2.00 A/B 2-142 [» ]
    ProteinModelPortali P54512.
    SMRi P54512. Positions 4-140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU24520.

    Proteomic databases

    PaxDbi P54512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14383 ; CAB14383 ; BSU24520 .
    GeneIDi 938554.
    KEGGi bsu:BSU24520.
    PATRICi 18976738. VBIBacSub10457_2559.

    Organism-specific databases

    GenoListi BSU24520. [Micado ]

    Phylogenomic databases

    eggNOGi COG1321.
    HOGENOMi HOG000040349.
    OrthoDBi EOG6M9F3P.
    PhylomeDBi P54512.

    Enzyme and pathway databases

    BioCyci BSUB:BSU24520-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P54512.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.60.10. 1 hit.
    HAMAPi MF_00732. HTH_MntR.
    InterProi IPR001367. Fe_dep_repressor.
    IPR022689. Fe_dep_repressor_HTH_DtxR.
    IPR022687. Fe_dep_repressor_HTH_DtxR_N.
    IPR022897. Tscrpt_reg_MntR.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF02742. Fe_dep_repr_C. 1 hit.
    PF01325. Fe_dep_repress. 1 hit.
    [Graphical view ]
    SMARTi SM00529. HTH_DTXR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47979. SSF47979. 1 hit.
    PROSITEi PS50944. HTH_DTXR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 81.
    4. "Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins."
      Que Q., Helmann J.D.
      Mol. Microbiol. 35:1454-1468(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: 168.

    Entry informationi

    Entry nameiMNTR_BACSU
    AccessioniPrimary (citable) accession number: P54512
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3