ID   BTR_BACSU               Reviewed;         529 AA.
AC   P40408;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=HTH-type transcriptional activator Btr;
DE   AltName: Full=Bacillibactin transport regulator;
GN   Name=btr; Synonyms=ybbB, yzbC; OrderedLocusNames=BSU01640;
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=BD99 / MS94;
RX   PubMed=8011666; DOI=10.1016/0005-2728(94)90131-7;
RA   Quirk P.G., Guffanti A.A., Clejan S., Cheng J., Krulwich T.A.;
RT   "Isolation of Tn917 insertional mutants of Bacillus subtilis that are
RT   resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL   Biochim. Biophys. Acta 1186:27-34(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
RA   Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
RT   "Sequence and analysis of a 31 kb segment of the Bacillus subtilis
RT   chromosome in the area of the rrnH and rrnG operons.";
RL   Microbiology 143:2763-2767(1997).
RN   [3]
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   [4]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=12354229; DOI=10.1046/j.1365-2958.2002.03113.x;
RA   Baichoo N., Wang T., Ye R., Helmann J.D.;
RT   "Global analysis of the Bacillus subtilis Fur regulon and the iron
RT   starvation stimulon.";
RL   Mol. Microbiol. 45:1613-1629(2002).
RN   [5]
RP   FUNCTION, DNA-BINDING, AND INTERACTION WITH BACILLIBACTIN.
RC   STRAIN=168 / CU1065;
RX   PubMed=17725565; DOI=10.1111/j.1365-2958.2007.05905.x;
RA   Gaballa A., Helmann J.D.;
RT   "Substrate induction of siderophore transport in Bacillus subtilis mediated
RT   by a novel one-component regulator.";
RL   Mol. Microbiol. 66:164-173(2007).
CC   -!- FUNCTION: In iron-limited conditions, activates expression of the
CC       feuABCybbA operon, which encodes the bacillibactin uptake system. Acts
CC       by binding directly to a conserved direct repeat element upstream of
CC       the feuA promoter. Activity is increased in the presence of
CC       bacillibactin. {ECO:0000269|PubMed:17725565}.
CC   -!- SUBUNIT: Binds with high affinity to both apo-bacillibactin and iron-
CC       bacillibactin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Repressed by Fur in the presence of iron.
CC       {ECO:0000269|PubMed:12354229}.
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DR   EMBL; L19954; AAA64353.1; -; Genomic_DNA.
DR   EMBL; AB002150; BAA19497.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11940.1; -; Genomic_DNA.
DR   PIR; I39841; I39841.
DR   RefSeq; NP_388045.1; NC_000964.3.
DR   RefSeq; WP_003234977.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; P40408; -.
DR   SMR; P40408; -.
DR   IntAct; P40408; 1.
DR   STRING; 224308.BSU01640; -.
DR   PaxDb; P40408; -.
DR   PRIDE; P40408; -.
DR   EnsemblBacteria; CAB11940; CAB11940; BSU_01640.
DR   GeneID; 938888; -.
DR   KEGG; bsu:BSU01640; -.
DR   PATRIC; fig|224308.179.peg.170; -.
DR   eggNOG; COG0614; Bacteria.
DR   eggNOG; COG2207; Bacteria.
DR   OMA; LHPKWTA; -.
DR   BioCyc; BSUB:BSU01640-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF01497; Peripla_BP_2; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS50983; FE_B12_PBP; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..529
FT                   /note="HTH-type transcriptional activator Btr"
FT                   /id="PRO_0000194622"
FT   DOMAIN          268..528
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT   DNA_BIND        182..201
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
SQ   SEQUENCE   529 AA;  60763 MW;  FBC2029040C793D2 CRC64;
     MQNAVIYQPV QIEYLKKTSD LFSEQQLADS FVLIFHLKGN GYISIGTNTN PLQKKTLYVC
     PPNETFGFTP AADGHIDACI IRLLSYIKET GQDIFTPCTE SELAKLKLMN VSHIENLAVR
     LQELAALWNE SSQLSQLKCV IEVQSLIYDL FTASLSDQTD THSAIEKTKH YIETHADTKI
     TLAQLSQMAG ISAKHYSESF KKWTGQSVTE FITKTRITKA KRLMAKSNCK LKEIAHQTGY
     QDEFYFSRIF KKYTGCSPTS YMKKRRKKIA AYGRGTMGHL IPLHHIPFAA ALHPKWTSYY
     YQHYSTDIPV QLSAYRFNEK WEENLYTLSQ AEPDVIVSMD SISPEEQDRL NRIAEVMYLP
     SEESWRTHFL QTASFLKEES EAEKWLADYD QQTTAAKKTL QHVQGLRFLF LRLHKQNFYL
     AHNRSVREVF FGDLGFSSAT TADTPSEQAI SLENIANYQA DCMMLFLFKE PETIAYYQQL
     QQTEAWQNLS AVRDNRVYLL SLDPWNEYSA CGHERIVQQT VSLLSGDCP