ID   MTRB_BACSU              Reviewed;          75 AA.
AC   P19466;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 153.
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; OrderedLocusNames=BSU22770;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2123343; DOI=10.1073/pnas.87.22.8726;
RA   Gollnick P., Ishino S., Kuroda M.I., Henner D.J., Yanofsky C.;
RT   "The mtr locus is a two-gene operon required for transcription attenuation
RT   in the trp operon of Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8726-8730(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION.
RX   PubMed=1551827; DOI=10.1128/jb.174.7.2059-2064.1992;
RA   Babitzke P., Gollnick P., Yanofsky C.;
RT   "The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA),
RT   an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of
RT   tryptophan biosynthesis.";
RL   J. Bacteriol. 174:2059-2064(1992).
RN   [4]
RP   FUNCTION.
RX   PubMed=18445592; DOI=10.1074/jbc.m801461200;
RA   Deikus G., Condon C., Bechhofer D.H.;
RT   "Role of Bacillus subtilis RNase J1 endonuclease and 5'-exonuclease
RT   activities in trp leader RNA turnover.";
RL   J. Biol. Chem. 283:17158-17167(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=7715723; DOI=10.1038/374693a0;
RA   Antson A.A., Otridge J., Brzozowski A.M., Dodson E.J., Dodson G.G.,
RA   Wilson K.S., Smith T.M., Yan M., Kurecki T., Gollnick P.;
RT   "The structure of trp RNA-binding attenuation protein.";
RL   Nature 374:693-700(1995).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   PubMed=7525975; DOI=10.1006/jmbi.1994.1698;
RA   Antson A.A., Brzozowski A.M., Dodson E.J., Dauter Z., Wilson K.S.,
RA   Kurecki T., Otridge J., Gollnick P.;
RT   "11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from
RT   Bacillus subtilis determined by X-ray analysis.";
RL   J. Mol. Biol. 244:1-5(1994).
CC   -!- FUNCTION: Required for transcription attenuation control in the trp
CC       operon. This trans-acting factor binds to trinucleotide repeats (GAG or
CC       UAG) located in the trp leader transcript causing transcription
CC       termination. Binds the leader RNA only in presence of L-tryptophan.
CC       {ECO:0000269|PubMed:1551827, ECO:0000269|PubMed:18445592}.
CC   -!- SUBUNIT: Oligomer of 11 identical subunits arranged in doughnut-like
CC       structure.
CC   -!- SIMILARITY: Belongs to the MtrB family. {ECO:0000305}.
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DR   EMBL; M37320; AAA22616.1; -; Genomic_DNA.
DR   EMBL; M80245; AAA20853.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14193.1; -; Genomic_DNA.
DR   PIR; B38256; B38256.
DR   RefSeq; NP_390158.1; NC_000964.3.
DR   RefSeq; WP_003230576.1; NZ_JNCM01000036.1.
DR   PDB; 1WAP; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-75.
DR   PDB; 3ZZQ; X-ray; 1.75 A; A/B/C/D/E/F=7-71.
DR   PDB; 4B27; X-ray; 2.72 A; A/B/C/D/E/F=1-75.
DR   PDBsum; 1WAP; -.
DR   PDBsum; 3ZZQ; -.
DR   PDBsum; 4B27; -.
DR   AlphaFoldDB; P19466; -.
DR   SMR; P19466; -.
DR   STRING; 224308.BSU22770; -.
DR   jPOST; P19466; -.
DR   PaxDb; 224308-BSU22770; -.
DR   EnsemblBacteria; CAB14193; CAB14193; BSU_22770.
DR   GeneID; 83886146; -.
DR   GeneID; 938996; -.
DR   KEGG; bsu:BSU22770; -.
DR   eggNOG; ENOG5032Z9Y; Bacteria.
DR   InParanoid; P19466; -.
DR   OrthoDB; 2111980at2; -.
DR   BioCyc; BSUB:BSU22770-MONOMER; -.
DR   EvolutionaryTrace; P19466; -.
DR   PRO; PR:P19466; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:InterPro.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IDA:CACAO.
DR   GO; GO:0060566; P:positive regulation of termination of DNA-templated transcription; IDA:CACAO.
DR   Gene3D; 2.60.40.50; TRAP-like; 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; TRAP-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..75
FT                   /note="Transcription attenuation protein MtrB"
FT                   /id="PRO_0000206028"
FT   STRAND          9..16
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
FT   STRAND          50..65
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:3ZZQ"
SQ   SEQUENCE   75 AA;  8328 MW;  34C173A8D15A4B31 CRC64;
     MNQKHSSDFV VIKAVEDGVN VIGLTRGTDT KFHHSEKLDK GEVIIAQFTE HTSAIKVRGE
     ALIQTAYGEM KSEKK
//