PUCR_BACSU
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 03-AUG-2022, entry version 115.
DE RecName: Full=Purine catabolism regulatory protein;
GN Name=pucR; Synonyms=yunI; OrderedLocusNames=BSU32420;
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 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}.
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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 STRING; 224308.BSU32420; -.
DR PaxDb; O32138; -.
DR PRIDE; O32138; -.
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 OMA; CQISETA; -.
DR PhylomeDB; O32138; -.
DR BioCyc; BSUB:BSU32420-MON; -.
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; -; 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 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
