PURR_BACSU
ID PURR_BACSU Reviewed; 285 AA.
AC P37551;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pur operon repressor;
GN Name=purR; Synonyms=yabI; OrderedLocusNames=BSU00470;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
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 PROTEIN SEQUENCE OF 1-25, AND CHARACTERIZATION.
RX PubMed=7638212; DOI=10.1073/pnas.92.16.7455;
RA Weng M., Nagy P.L., Zalkin H.;
RT "Identification of the Bacillus subtilis pur operon repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7455-7459(1995).
CC -!- FUNCTION: Controls the transcription of the pur operon for purine
CC biosynthetic genes, binds to the control region of the operon. DNA
CC binding is inhibited by 5-phosphoribosyl 1-pyrophosphate.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; D26185; BAA05282.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11823.1; -; Genomic_DNA.
DR PIR; S66076; S66076.
DR RefSeq; NP_387928.1; NC_000964.3.
DR RefSeq; WP_003218342.1; NZ_JNCM01000028.1.
DR PDB; 1O57; X-ray; 2.20 A; A/B/C/D=1-285.
DR PDB; 1P4A; X-ray; 2.22 A; A/B/C/D=1-285.
DR PDBsum; 1O57; -.
DR PDBsum; 1P4A; -.
DR AlphaFoldDB; P37551; -.
DR SMR; P37551; -.
DR STRING; 224308.BSU00470; -.
DR DrugBank; DB03942; Carboxylic PRPP.
DR PaxDb; P37551; -.
DR PRIDE; P37551; -.
DR EnsemblBacteria; CAB11823; CAB11823; BSU_00470.
DR GeneID; 64301868; -.
DR GeneID; 937000; -.
DR KEGG; bsu:BSU00470; -.
DR PATRIC; fig|224308.179.peg.47; -.
DR eggNOG; COG0503; Bacteria.
DR InParanoid; P37551; -.
DR OMA; YMLERPR; -.
DR PhylomeDB; P37551; -.
DR BioCyc; BSUB:BSU00470-MON; -.
DR EvolutionaryTrace; P37551; -.
DR PRO; PR:P37551; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045982; P:negative regulation of purine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR015265; PuR_N.
DR InterPro; IPR010078; PurR_Bsub.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR43864:SF2; PTHR43864:SF2; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF09182; PuR_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01743; purR_Bsub; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..285
FT /note="Pur operon repressor"
FT /id="PRO_0000139699"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 37..53
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1O57"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1O57"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1O57"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1O57"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 198..209
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 225..237
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1O57"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1O57"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1O57"
SQ SEQUENCE 285 AA; 31229 MW; 76B1DB289A3F34FB CRC64;
MKFRRSGRLV DLTNYLLTHP HELIPLTFFS ERYESAKSSI SEDLTIIKQT FEQQGIGTLL
TVPGAAGGVK YIPKMKQAEA EEFVQTLGQS LANPERILPG GYVYLTDILG KPSVLSKVGK
LFASVFAERE IDVVMTVATK GIPLAYAAAS YLNVPVVIVR KDNKVTEGST VSINYVSGSS
NRIQTMSLAK RSMKTGSNVL IIDDFMKAGG TINGMINLLD EFNANVAGIG VLVEAEGVDE
RLVDEYMSLL TLSTINMKEK SIEIQNGNFL RFFKDNLLKN GETES
