ID PUCR_BACSU Reviewed; 531 AA. AC O32138; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Purine catabolism regulatory protein; GN Name=pucR; Synonyms=yunI; OrderedLocusNames=BSU32420; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; 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 FUNCTION. RC STRAIN=168; RX PubMed=11344136; DOI=10.1128/jb.183.11.3293-3302.2001; RA Schultz A.C., Nygaard P., Saxild H.H.; RT "Functional analysis of 14 genes that constitute the purine catabolic RT pathway in Bacillus subtilis and evidence for a novel regulon controlled by RT the PucR transcription activator."; RL J. Bacteriol. 183:3293-3302(2001). RN [3] RP FUNCTION. RC STRAIN=168; RX PubMed=12029039; DOI=10.1128/jb.184.12.3232-3241.2002; RA Beier L., Nygaard P., Jarmer H., Saxild H.H.; RT "Transcription analysis of the Bacillus subtilis PucR regulon and RT identification of a cis-acting sequence required for PucR-regulated RT expression of genes involved in purine catabolism."; RL J. Bacteriol. 184:3232-3241(2002). CC -!- FUNCTION: Activates the expression of pucFG, pucH, pucI, pucJKLM and CC guaD, while it represses pucABCDE and its own expression. CC {ECO:0000269|PubMed:11344136, ECO:0000269|PubMed:12029039}. CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus CC ammonia) and is induced during limiting-nitrogen conditions CC (glutamate). Expression slightly decreases when allantoin is added CC during limiting-nitrogen conditions. CC -!- SIMILARITY: Belongs to the CdaR family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL009126; CAB15232.1; -; Genomic_DNA. DR PIR; D70016; D70016. DR RefSeq; NP_391122.1; NC_000964.3. DR RefSeq; WP_003244351.1; NZ_JNCM01000033.1. DR AlphaFoldDB; O32138; -. DR SMR; O32138; -. DR STRING; 224308.BSU32420; -. DR PaxDb; 224308-BSU32420; -. DR EnsemblBacteria; CAB15232; CAB15232; BSU_32420. DR GeneID; 937221; -. DR KEGG; bsu:BSU32420; -. DR PATRIC; fig|224308.179.peg.3509; -. DR eggNOG; COG2508; Bacteria. DR InParanoid; O32138; -. DR OrthoDB; 142218at2; -. DR PhylomeDB; O32138; -. DR BioCyc; BSUB:BSU32420-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.2840; PucR C-terminal helix-turn-helix domain; 1. DR InterPro; IPR041522; CdaR_GGDEF. DR InterPro; IPR025736; PucR_C-HTH_dom. DR InterPro; IPR042070; PucR_C-HTH_sf. DR InterPro; IPR012914; PucR_dom. DR PANTHER; PTHR33744; CARBOHYDRATE DIACID REGULATOR; 1. DR PANTHER; PTHR33744:SF15; CARBOHYDRATE DIACID REGULATOR; 1. DR Pfam; PF17853; GGDEF_2; 1. DR Pfam; PF13556; HTH_30; 1. DR Pfam; PF07905; PucR; 1. PE 2: Evidence at transcript level; KW Activator; DNA-binding; Purine metabolism; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..531 FT /note="Purine catabolism regulatory protein" FT /id="PRO_0000165945" SQ SEQUENCE 531 AA; 60514 MW; CC2DA7F96247452F CRC64; MNILDVMKIP AFENANLIAG KAGGEREVQH VNMMDAPDIV DFLHKNELLV TTAYHLKDHP HQLSELIRQM AKRGCAGLGI KTKRYLEDIP KEIIELADSY AFPIIELPEH IRLGDIVNAT LSHILDMRSN ELQQAIYAHK KFTNHIMSGK GLQSLLKKVS DILQLPVLLL DQHAKMLSAS HQISVETEKL KGTLNTVSGP FFTCFSTISD QKTYSVLPIY NHEKNCGYLL IPDMVQAGDK GLILTIEQAA NVISFELLKE NALKQFSRRA RNEFFNNFIE RTFSSDDEIK NRAKEFKLRW DQKYMCIAGK LDRNDESISF TENQLASDSV FEFLEGELSA FPFPPHFFMK GNVGIILIEA TDSWSEMHAS VISFLEQFQT QVSAQFKRTV SFGISNICQK LIDVPDAFTE ASDALQSGHL SRSTAFIQVY HAKDVPELLR LLPVEDLKKF YNSTLQSLAE KQQEDQSLLH TLSVYLETHC QISETAKRLY VHRNTVIYRL EKCEELLGKS LKDPETTMRL RLALRMQRLI S //