Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19466

- MTRB_BACSU

UniProt

P19466 - MTRB_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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]

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 – 168Combined sources
Beta strandi19 – 257Combined sources
Beta strandi27 – 293Combined sources
Beta strandi32 – 387Combined sources
Beta strandi43 – 475Combined sources
Beta strandi50 – 6516Combined sources
Beta strandi68 – 703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MNQKHSSDFV VIKAVEDGVN VIGLTRGTDT KFHHSEKLDK GEVIIAQFTE
60 70
HTSAIKVRGE ALIQTAYGEM KSEKK
Length:75
Mass (Da):8,328
Last modified:February 1, 1991 - v1
Checksum:i34C173A8D15A4B31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 115 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