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 03-AUG-2022, entry version 126.
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 O31466; O31466: rtpA; NbExp=2; IntAct=EBI-15753070, EBI-15753070;
CC O31466; 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};
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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 AlphaFoldDB; O31466; -.
DR BMRB; O31466; -.
DR SMR; O31466; -.
DR DIP; DIP-48707N; -.
DR IntAct; O31466; 1.
DR STRING; 224308.BSU02530; -.
DR PaxDb; O31466; -.
DR EnsemblBacteria; CAB12047; CAB12047; BSU_02530.
DR GeneID; 938403; -.
DR KEGG; bsu:BSU02530; -.
DR PATRIC; fig|224308.179.peg.261; -.
DR eggNOG; ENOG502ZS83; Bacteria.
DR OMA; MVIATDD; -.
DR BioCyc; BSUB:BSU02530-MON; -.
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;
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:0007829|PDB:2BX9"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2BX9"
FT TURN 13..17
FT /evidence="ECO:0007829|PDB:2BX9"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2BX9"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:2BX9"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2BX9"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:2BX9"
SQ SEQUENCE 53 AA; 5650 MW; E9956FB4FE0E7A85 CRC64;
MVIATDDLEV ACPKCERAGE IEGTPCPACS GKGVILTAQG YTLLDFIQKH LNK
