MTRB_GEOSE
ID MTRB_GEOSE Reviewed; 74 AA.
AC Q9X6J6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Transcription attenuation protein MtrB;
DE AltName: Full=Trp RNA-binding attenuation protein;
DE Short=TRAP;
DE AltName: Full=Tryptophan RNA-binding attenuator protein;
GN Name=mtrB;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.5
RP ANGSTROMS).
RC STRAIN=ATCC 12980 / NCA 26;
RX PubMed=10369778; DOI=10.1006/jmbi.1999.2834;
RA Chen X.-P., Antson A.A., Yang M., Baumann C., Dodson E.J., Dodson G.G.,
RA Gollnick P.;
RT "Regulatory features of the trp operon and the crystal structure of the trp
RT RNA-binding attenuation protein from Bacillus stearothermophilus.";
RL J. Mol. Biol. 289:1003-1016(1999).
CC -!- FUNCTION: Required for transcription attenuation control in the Trp
CC operon. This trans-acting factor seems to recognize a 10 bases
CC nucleotide sequence in the Trp leader transcript causing transcription
CC termination. Binds the leader RNA only in presence of L-tryptophan.
CC -!- SUBUNIT: Oligomer of 11 identical subunits arranged in doughnut-like
CC structure.
CC -!- INTERACTION:
CC Q9X6J6; Q9X6J6: mtrB; NbExp=4; IntAct=EBI-15582912, EBI-15582912;
CC Q9X6J6; O31466: rtpA; Xeno; NbExp=3; IntAct=EBI-15582912, EBI-15753070;
CC -!- SIMILARITY: Belongs to the MtrB family. {ECO:0000305}.
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DR EMBL; AF139535; AAD33793.1; -; Genomic_DNA.
DR RefSeq; WP_033013997.1; NZ_RCTK01000002.1.
DR PDB; 1C9S; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 1GTF; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 1GTN; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 1QAW; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K=1-74.
DR PDB; 1UTD; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 2EXS; X-ray; 2.00 A; A/B/C=2-74.
DR PDB; 2EXT; X-ray; 1.80 A; A/B/C=2-74.
DR PDB; 2ZCZ; X-ray; 1.80 A; A/B/C/D/E/F=1-74.
DR PDB; 2ZD0; X-ray; 2.50 A; A/B/C=1-74.
DR PDB; 2ZP8; X-ray; 3.20 A; A/B/C/D=1-74.
DR PDB; 2ZP9; X-ray; 3.20 A; A/B/F/G/K/L=1-74.
DR PDB; 3AQD; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 3ZZS; X-ray; 1.49 A; A/B/C/D/E/F/G/H/I=5-69.
DR PDB; 4V4F; X-ray; 1.90 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT/BU/BV=1-74.
DR PDB; 5EEU; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EEV; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EEW; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EEX; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EEY; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EEZ; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EF0; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EF1; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EF2; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 5EF3; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-74.
DR PDB; 6RVV; EM; 3.70 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/CA/CB/CC/CD/CE/CF/CG/CH=1-74.
DR PDB; 6RVW; EM; 3.70 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/CA/CB/CC/CD/CE/CF/CG/CH=1-74.
DR PDBsum; 1C9S; -.
DR PDBsum; 1GTF; -.
DR PDBsum; 1GTN; -.
DR PDBsum; 1QAW; -.
DR PDBsum; 1UTD; -.
DR PDBsum; 2EXS; -.
DR PDBsum; 2EXT; -.
DR PDBsum; 2ZCZ; -.
DR PDBsum; 2ZD0; -.
DR PDBsum; 2ZP8; -.
DR PDBsum; 2ZP9; -.
DR PDBsum; 3AQD; -.
DR PDBsum; 3ZZS; -.
DR PDBsum; 4V4F; -.
DR PDBsum; 5EEU; -.
DR PDBsum; 5EEV; -.
DR PDBsum; 5EEW; -.
DR PDBsum; 5EEX; -.
DR PDBsum; 5EEY; -.
DR PDBsum; 5EEZ; -.
DR PDBsum; 5EF0; -.
DR PDBsum; 5EF1; -.
DR PDBsum; 5EF2; -.
DR PDBsum; 5EF3; -.
DR PDBsum; 6RVV; -.
DR PDBsum; 6RVW; -.
DR AlphaFoldDB; Q9X6J6; -.
DR BMRB; Q9X6J6; -.
DR SMR; Q9X6J6; -.
DR DIP; DIP-29104N; -.
DR IntAct; Q9X6J6; 1.
DR GeneID; 58572467; -.
DR EvolutionaryTrace; Q9X6J6; -.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.60.40.50; -; 1.
DR HAMAP; MF_00798; Trp_attenuator; 1.
DR InterPro; IPR000824; MtrB.
DR InterPro; IPR016031; Trp_RNA-bd_attenuator-like_dom.
DR InterPro; IPR023558; Trp_RNA-bd_attenuator_dom.
DR Pfam; PF02081; TrpBP; 1.
DR PRINTS; PR00687; TRPRNAAP.
DR SUPFAM; SSF51219; SSF51219; 1.
PE 1: Evidence at protein level;
KW 3D-structure; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..74
FT /note="Transcription attenuation protein MtrB"
FT /id="PRO_0000206027"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:3ZZS"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:3ZZS"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3ZZS"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:3ZZS"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3ZZS"
FT STRAND 48..63
FT /evidence="ECO:0007829|PDB:3ZZS"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3ZZS"
SQ SEQUENCE 74 AA; 8242 MW; B3E22117331531CE CRC64;
MYTNSDFVVI KALEDGVNVI GLTRGADTRF HHSEKLDKGE VLIAQFTEHT SAIKVRGKAY
IQTRHGVIES EGKK
