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P19466

- MTRB_BACSU

UniProt

P19466 - MTRB_BACSU

Protein

Transcription attenuation protein MtrB

Gene

mtrB

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

    Required for transcription attenuation control in the trp operon. This trans-acting factor binds to trinucleotide repeats (GAG or UAG) located in the trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan.2 Publications

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. DNA-templated transcription, termination Source: InterPro
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU22770-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription attenuation protein MtrB
    Alternative name(s):
    Trp RNA-binding attenuation protein
    Short name:
    TRAP
    Tryptophan RNA-binding attenuator protein
    Gene namesi
    Name:mtrB
    Ordered Locus Names:BSU22770
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU22770. [Micado]

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7575Transcription attenuation protein MtrBPRO_0000206028Add
    BLAST

    Interactioni

    Subunit structurei

    Oligomer of 11 identical subunits arranged in doughnut-like structure.

    Protein-protein interaction databases

    STRINGi224308.BSU22770.

    Structurei

    Secondary structure

    1
    75
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 168
    Beta strandi19 – 257
    Beta strandi27 – 293
    Beta strandi32 – 387
    Beta strandi43 – 475
    Beta strandi50 – 6516
    Beta strandi68 – 703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WAPX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V1-75[»]
    3ZZQX-ray1.75A/B/C/D/E/F7-71[»]
    4B27X-ray2.72A/B/C/D/E/F1-75[»]
    ProteinModelPortaliP19466.
    SMRiP19466. Positions 8-75.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19466.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MtrB family.Curated

    Phylogenomic databases

    HOGENOMiHOG000245485.
    KOiK06285.
    OMAiFHHTEKL.
    OrthoDBiEOG64V2JJ.

    Family and domain databases

    Gene3Di2.60.40.50. 1 hit.
    HAMAPiMF_00798. Trp_attenuator.
    InterProiIPR000824. MtrB.
    IPR016031. Trp_RNA-bd_attenuator-like_dom.
    IPR023558. Trp_RNA-bd_attenuator_dom.
    [Graphical view]
    PfamiPF02081. TrpBP. 1 hit.
    [Graphical view]
    PRINTSiPR00687. TRPRNAAP.
    SUPFAMiSSF51219. SSF51219. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P19466-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQKHSSDFV VIKAVEDGVN VIGLTRGTDT KFHHSEKLDK GEVIIAQFTE   50
    HTSAIKVRGE ALIQTAYGEM KSEKK 75
    Length:75
    Mass (Da):8,328
    Last modified:February 1, 1991 - v1
    Checksum:i34C173A8D15A4B31
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37320 Genomic DNA. Translation: AAA22616.1.
    M80245 Genomic DNA. Translation: AAA20853.1.
    AL009126 Genomic DNA. Translation: CAB14193.1.
    PIRiB38256.
    RefSeqiNP_390158.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14193; CAB14193; BSU22770.
    GeneIDi938996.
    KEGGibsu:BSU22770.
    PATRICi18976365. VBIBacSub10457_2373.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37320 Genomic DNA. Translation: AAA22616.1 .
    M80245 Genomic DNA. Translation: AAA20853.1 .
    AL009126 Genomic DNA. Translation: CAB14193.1 .
    PIRi B38256.
    RefSeqi NP_390158.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WAP X-ray 1.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V 1-75 [» ]
    3ZZQ X-ray 1.75 A/B/C/D/E/F 7-71 [» ]
    4B27 X-ray 2.72 A/B/C/D/E/F 1-75 [» ]
    ProteinModelPortali P19466.
    SMRi P19466. Positions 8-75.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU22770.

    Chemistry

    DrugBanki DB00150. L-Tryptophan.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14193 ; CAB14193 ; BSU22770 .
    GeneIDi 938996.
    KEGGi bsu:BSU22770.
    PATRICi 18976365. VBIBacSub10457_2373.

    Organism-specific databases

    GenoListi BSU22770. [Micado ]

    Phylogenomic databases

    HOGENOMi HOG000245485.
    KOi K06285.
    OMAi FHHTEKL.
    OrthoDBi EOG64V2JJ.

    Enzyme and pathway databases

    BioCyci BSUB:BSU22770-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P19466.

    Family and domain databases

    Gene3Di 2.60.40.50. 1 hit.
    HAMAPi MF_00798. Trp_attenuator.
    InterProi IPR000824. MtrB.
    IPR016031. Trp_RNA-bd_attenuator-like_dom.
    IPR023558. Trp_RNA-bd_attenuator_dom.
    [Graphical view ]
    Pfami PF02081. TrpBP. 1 hit.
    [Graphical view ]
    PRINTSi PR00687. TRPRNAAP.
    SUPFAMi SSF51219. SSF51219. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The mtr locus is a two-gene operon required for transcription attenuation in the trp operon of Bacillus subtilis."
      Gollnick P., Ishino S., Kuroda M.I., Henner D.J., Yanofsky C.
      Proc. Natl. Acad. Sci. U.S.A. 87:8726-8730(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis."
      Babitzke P., Gollnick P., Yanofsky C.
      J. Bacteriol. 174:2059-2064(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Role of Bacillus subtilis RNase J1 endonuclease and 5'-exonuclease activities in trp leader RNA turnover."
      Deikus G., Condon C., Bechhofer D.H.
      J. Biol. Chem. 283:17158-17167(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    6. "11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis."
      Antson A.A., Brzozowski A.M., Dodson E.J., Dauter Z., Wilson K.S., Kurecki T., Otridge J., Gollnick P.
      J. Mol. Biol. 244:1-5(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

    Entry informationi

    Entry nameiMTRB_BACSU
    AccessioniPrimary (citable) accession number: P19466
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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