(data stored in ACNUC7421 zone)

SWISSPROT: RTPA_BACSU

ID   RTPA_BACSU              Reviewed;          53 AA.
AC   O31466;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Tryptophan RNA-binding attenuator protein inhibitory protein;
DE   AltName: Full=Anti-TRAP protein;
DE            Short=AT;
GN   Name=rtpA; Synonyms=yczA; OrderedLocusNames=BSU02530;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   CHARACTERIZATION, AND MASS SPECTROMETRY.
RX   PubMed=11557884; DOI=10.1126/science.1062187;
RA   Valbuzzi A., Yanofsky C.;
RT   "Inhibition of the B. subtilis regulatory protein TRAP by the TRAP-
RT   inhibitory protein, AT.";
RL   Science 293:2057-2059(2001).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=11786553; DOI=10.1074/jbc.m111813200;
RA   Valbuzzi A., Gollnick P., Babitzke P., Yanofsky C.;
RT   "The anti-trp RNA-binding attenuation protein (Anti-TRAP), AT, recognizes
RT   the tryptophan-activated RNA binding domain of the TRAP regulatory
RT   protein.";
RL   J. Biol. Chem. 277:10608-10613(2002).
CC   -!- FUNCTION: By forming a complex with tryptophan-activated TRAP, and
CC       masking its RNA binding site, it inhibits TRAP's RNA binding ability,
CC       thereby abolishing TRAP regulation of gene expression, leading to
CC       antitermination and increased trp operon expression. AT acts by
CC       competing with messenger RNA for the RNA binding domain of TRAP.
CC   -!- SUBUNIT: Homopentamer or homohexamer.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-15753070, EBI-15753070;
CC       Q9X6J6:mtrB (xeno); NbExp=3; IntAct=EBI-15753070, EBI-15582912;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By uncharged Trp tRNA, via the T-box transcription
CC       antitermination mechanism.
CC   -!- MASS SPECTROMETRY: Mass=5648; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11557884};
DR   EMBL; AL009126; CAB12047.1; -; Genomic_DNA.
DR   PIR; H69766; H69766.
DR   RefSeq; NP_388135.1; NC_000964.3.
DR   RefSeq; WP_003234807.1; NZ_JNCM01000030.1.
DR   PDB; 2BX9; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-53.
DR   PDB; 2KO8; NMR; -; A/B/C=1-53.
DR   PDB; 2ZP8; X-ray; 3.20 A; E/F/G/H/I/J=1-53.
DR   PDB; 2ZP9; X-ray; 3.20 A; C/D/E/H/I/J/M/N/O=1-53.
DR   PDBsum; 2BX9; -.
DR   PDBsum; 2KO8; -.
DR   PDBsum; 2ZP8; -.
DR   PDBsum; 2ZP9; -.
DR   SMR; O31466; -.
DR   DIP; DIP-48707N; -.
DR   IntAct; O31466; 1.
DR   STRING; 224308.BSU02530; -.
DR   PaxDb; O31466; -.
DR   PRIDE; O31466; -.
DR   EnsemblBacteria; CAB12047; CAB12047; BSU02530.
DR   GeneID; 938403; -.
DR   KEGG; bsu:BSU02530; -.
DR   PATRIC; fig|224308.179.peg.261; -.
DR   HOGENOM; HOG000008724; -.
DR   OMA; MVIATDD; -.
DR   BioCyc; BSUB:BSU02530-MONOMER; -.
DR   EvolutionaryTrace; O31466; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   InterPro; IPR031538; Anti-TRAP.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   Pfam; PF15777; Anti-TRAP; 1.
DR   SUPFAM; SSF57938; SSF57938; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31466.
DR   SWISS-2DPAGE; O31466.
KW   3D-structure; Cytoplasm; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..53
FT                   /note="Tryptophan RNA-binding attenuator protein inhibitory
FT                   protein"
FT                   /id="PRO_0000097522"
FT   REPEAT          12..19
FT                   /note="CXXCXGXG motif"
FT   REPEAT          26..33
FT                   /note="CXXCXGXG motif"
FT   HELIX           5..8
FT                   /evidence="ECO:0000244|PDB:2BX9"
FT   STRAND          9..11
FT                   /evidence="ECO:0000244|PDB:2BX9"
FT   TURN            13..17
FT                   /evidence="ECO:0000244|PDB:2BX9"
FT   STRAND          18..21
FT                   /evidence="ECO:0000244|PDB:2BX9"
FT   TURN            27..31
FT                   /evidence="ECO:0000244|PDB:2BX9"
FT   STRAND          32..36
FT                   /evidence="ECO:0000244|PDB:2BX9"
FT   HELIX           38..50
FT                   /evidence="ECO:0000244|PDB:2BX9"
SQ   SEQUENCE   53 AA;  5650 MW;  E9956FB4FE0E7A85 CRC64;
     MVIATDDLEV ACPKCERAGE IEGTPCPACS GKGVILTAQG YTLLDFIQKH LNK
//

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