ID   FNR_BACSU               Reviewed;         238 AA.
AC   P46908;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Anaerobic regulatory protein;
GN   Name=fnr; OrderedLocusNames=BSU37310;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8846791; DOI=10.1002/j.1460-2075.1995.tb00287.x;
RA   Cruz Ramos H., Boursier L., Moszer I., Kunst F., Danchin A., Glaser P.;
RT   "Anaerobic transcription activation in Bacillus subtilis: identification of
RT   distinct FNR-dependent and -independent regulatory mechanisms.";
RL   EMBO J. 14:5984-5994(1995).
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).
CC   -!- FUNCTION: It is involved in the activation of genes necessary for
CC       anaerobic respiration.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By anaerobiosis.
CC   -!- DOMAIN: The cysteine cluster which is probably involved in the
CC       coordination of the [4Fe-4S] cluster is located at the C-terminal part
CC       of the protein.
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; Z49884; CAA90042.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15759.1; -; Genomic_DNA.
DR   PIR; S60081; S60081.
DR   RefSeq; NP_391612.1; NC_000964.3.
DR   RefSeq; WP_003243241.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P46908; -.
DR   SMR; P46908; -.
DR   STRING; 224308.BSU37310; -.
DR   PaxDb; 224308-BSU37310; -.
DR   EnsemblBacteria; CAB15759; CAB15759; BSU_37310.
DR   GeneID; 937050; -.
DR   KEGG; bsu:BSU37310; -.
DR   PATRIC; fig|224308.179.peg.4042; -.
DR   eggNOG; COG0664; Bacteria.
DR   InParanoid; P46908; -.
DR   OrthoDB; 9810708at2; -.
DR   PhylomeDB; P46908; -.
DR   BioCyc; BSUB:BSU37310-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00092; HTH_CRP; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR012318; HTH_CRP.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR24567:SF79; CAMP-ACTIVATED GLOBAL TRANSCRIPTIONAL REGULATOR CRP; 1.
DR   PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00325; Crp; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00419; HTH_CRP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS00042; HTH_CRP_1; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Activator; Cytoplasm; DNA-binding; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..238
FT                   /note="Anaerobic regulatory protein"
FT                   /id="PRO_0000100173"
FT   DOMAIN          145..219
FT                   /note="HTH crp-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   DNA_BIND        178..197
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   REGION          223..235
FT                   /note="Essential for the oxygen-regulated activity"
FT   BINDING         223
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         227
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         230
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         235
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   238 AA;  27218 MW;  B7079A37EFC7A03B CRC64;
     MNFLSVRPSD SDLISSDLYE LLESISTKRK MEKHTYLFRE GMDAEELYLI QSGLIEIGKL
     TSDGKDLTLR ICQKHDIVGE LTLFTEEPRY MLSAKVLEDG EVLVINKNKL EKELIQNGAL
     TFEFMKWMST HLRKIQSKIR DLLLHGKKGA LYSTLIRLSN SYGVERSDGI LINIVLTNQD
     LAKFCAAARE SVNRMLGDLR KKGVISIDES GKIILHKRDY LRCEIECENC PLEICNID
//