ID   NADR_BACSU              Reviewed;         180 AA.
AC   P39667;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Transcription repressor NadR;
DE   AltName: Full=ORF1;
GN   Name=nadR; Synonyms=niaR, yrxA; OrderedLocusNames=BSU27890;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=8444804; DOI=10.1128/jb.175.5.1423-1432.1993;
RA   Sun D., Setlow P.L.;
RT   "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB
RT   gene and a nifS-like gene, both of which are essential for NAD
RT   biosynthesis.";
RL   J. Bacteriol. 175:1423-1432(1993).
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   SEQUENCE REVISION TO C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   FUNCTION AS A TRANSCRIPTION REPRESSOR, DNA-BINDING, POSSIBLE NICOTINIC
RP   ACID-BINDING, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=16199587; DOI=10.1128/jb.187.20.7155-7160.2005;
RA   Rossolillo P., Marinoni I., Galli E., Colosimo A., Albertini A.M.;
RT   "YrxA is the transcriptional regulator that represses de novo NAD
RT   biosynthesis in Bacillus subtilis.";
RL   J. Bacteriol. 187:7155-7160(2005).
RN   [5]
RP   DNA-BINDING, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=18276644; DOI=10.1093/nar/gkn046;
RA   Rodionov D.A., Li X., Rodionova I.A., Yang C., Sorci L., Dervyn E.,
RA   Martynowski D., Zhang H., Gelfand M.S., Osterman A.L.;
RT   "Transcriptional regulation of NAD metabolism in bacteria: genomic
RT   reconstruction of NiaR (YrxA) regulon.";
RL   Nucleic Acids Res. 36:2032-2046(2008).
CC   -!- FUNCTION: In the presence of nicotinic acid represses transcription of
CC       the nadBCA and nifS-nadR operons. Also binds to DNA upstream of the
CC       niaP gene, probably regulating it as well. May bind nicotinic acid.
CC       {ECO:0000269|PubMed:16199587}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18276644}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype when grown in the absence of
CC       nicotinic acid. {ECO:0000269|PubMed:16199587,
CC       ECO:0000269|PubMed:18276644, ECO:0000269|PubMed:8444804}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; M98822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL009126; CAB14749.2; -; Genomic_DNA.
DR   PIR; A47071; A47071.
DR   RefSeq; NP_390667.2; NC_000964.3.
DR   RefSeq; WP_004398582.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P39667; -.
DR   SMR; P39667; -.
DR   STRING; 224308.BSU27890; -.
DR   PaxDb; P39667; -.
DR   PRIDE; P39667; -.
DR   EnsemblBacteria; CAB14749; CAB14749; BSU_27890.
DR   GeneID; 937515; -.
DR   KEGG; bsu:BSU27890; -.
DR   PATRIC; fig|224308.179.peg.3030; -.
DR   eggNOG; COG1827; Bacteria.
DR   InParanoid; P39667; -.
DR   OMA; HTPEQTK; -.
DR   PhylomeDB; P39667; -.
DR   BioCyc; BSUB:BSU27890-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.1340.20; -; 1.
DR   InterPro; IPR035922; 3H_dom_sf.
DR   InterPro; IPR004173; 3H_domain.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR026043; NadR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR40068; PTHR40068; 1.
DR   Pfam; PF02829; 3H; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   PIRSF; PIRSF037847; NiaR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF75500; SSF75500; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..180
FT                   /note="Transcription repressor NadR"
FT                   /id="PRO_0000049883"
FT   CONFLICT        177..180
FT                   /note="LIKD -> FN (in Ref. 1; M98822)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   180 AA;  19928 MW;  D147AFB02E271C8C CRC64;
     MTEELKLMGA NRRDQLLLWL KESKSPLTGG ELAKKANVSR QVIVQDISLL KAKNVPIIAT
     SQGYVYMDAA AQQHQQAERI IACLHGPERT EEELQLIVDE GVTVKDVKIE HPVYGDLTAA
     IQVGTRKEVS HFIKKINSTN AAYLSQLTDG VHLHTLTAPD EHRIDQACQA LEEAGILIKD