ID ARAR_BACSU Reviewed; 362 AA. AC P96711; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2002, sequence version 3. DT 27-MAR-2024, entry version 147. DE RecName: Full=Arabinose metabolism transcriptional repressor; GN Name=araR; Synonyms=araC, yvbS; OrderedLocusNames=BSU33970; 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=9045819; DOI=10.1128/jb.179.5.1598-1608.1997; RA Sa-Nogueira I.M.G., Mota L.J.; RT "Negative regulation of L-arabinose metabolism in Bacillus subtilis: RT characterization of the araR (araC) gene."; RL J. Bacteriol. 179:1598-1608(1997). 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 PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION. RX PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x; RA Mota L.J., Tavares P., Sa-Nogueira I.M.G.; RT "Mode of action of AraR, the key regulator of L-arabinose metabolism in RT Bacillus subtilis."; RL Mol. Microbiol. 33:476-489(1999). RN [4] RP CHARACTERIZATION. RC STRAIN=168; RX PubMed=11418559; DOI=10.1128/jb.183.14.4190-4201.2001; RA Mota L.J., Sarmento L.M., Sa-Nogueira I.M.G.; RT "Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: RT crucial roles of operators, cooperativity, and DNA looping."; RL J. Bacteriol. 183:4190-4201(2001). CC -!- FUNCTION: Transcriptional repressor of the arabinose utilization genes. CC Also regulates its own expression. Binds to two sequences within the CC promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one CC sequence in the araR promoter. CC -!- ACTIVITY REGULATION: Binding to DNA is inhibited by L-arabinose. CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; X98354; CAA66999.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15402.2; -; Genomic_DNA. DR PIR; D69588; D69588. DR RefSeq; NP_391277.1; NC_000964.3. DR RefSeq; WP_003243070.1; NZ_JNCM01000033.1. DR PDB; 3TB6; X-ray; 2.21 A; A/B=71-362. DR PDB; 4EGY; X-ray; 2.30 A; A/B=1-68. DR PDB; 4EGZ; X-ray; 2.30 A; A/B=1-68. DR PDB; 4H0E; X-ray; 1.97 A; A/B=1-68. DR PDB; 5D4R; X-ray; 2.07 A; A/B=1-68. DR PDB; 5D4S; X-ray; 1.97 A; A/B=1-68. DR PDBsum; 3TB6; -. DR PDBsum; 4EGY; -. DR PDBsum; 4EGZ; -. DR PDBsum; 4H0E; -. DR PDBsum; 5D4R; -. DR PDBsum; 5D4S; -. DR AlphaFoldDB; P96711; -. DR SMR; P96711; -. DR STRING; 224308.BSU33970; -. DR PaxDb; 224308-BSU33970; -. DR EnsemblBacteria; CAB15402; CAB15402; BSU_33970. DR GeneID; 938635; -. DR KEGG; bsu:BSU33970; -. DR PATRIC; fig|224308.179.peg.3683; -. DR eggNOG; COG1609; Bacteria. DR InParanoid; P96711; -. DR OrthoDB; 9813468at2; -. DR BioCyc; BSUB:BSU33970-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd01541; PBP1_AraR; 1. DR CDD; cd07377; WHTH_GntR; 1. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR033532; AraR_ligand_bind_dom. DR InterPro; IPR046335; LacI/GalR-like_sensor. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR30146:SF147; ARABINOSE METABOLISM TRANSCRIPTIONAL REPRESSOR; 1. DR PANTHER; PTHR30146; LACI-RELATED TRANSCRIPTIONAL REPRESSOR; 1. DR Pfam; PF00392; GntR; 1. DR Pfam; PF13377; Peripla_BP_3; 1. DR PRINTS; PR00035; HTHGNTR. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding; KW Reference proteome; Repressor; Transcription; Transcription regulation. FT CHAIN 1..362 FT /note="Arabinose metabolism transcriptional repressor" FT /id="PRO_0000050620" FT DOMAIN 1..70 FT /note="HTH gntR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307" FT DNA_BIND 30..49 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307" FT HELIX 4..15 FT /evidence="ECO:0007829|PDB:5D4S" FT TURN 16..19 FT /evidence="ECO:0007829|PDB:5D4S" FT HELIX 30..37 FT /evidence="ECO:0007829|PDB:5D4S" FT HELIX 41..53 FT /evidence="ECO:0007829|PDB:5D4S" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:5D4S" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:5D4S" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:5D4S" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 94..107 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 153..161 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 185..198 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 203..212 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 213..228 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 249..260 FT /evidence="ECO:0007829|PDB:3TB6" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 274..286 FT /evidence="ECO:0007829|PDB:3TB6" FT TURN 291..294 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 314..317 FT /evidence="ECO:0007829|PDB:3TB6" FT HELIX 321..335 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:3TB6" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:3TB6" SQ SEQUENCE 362 AA; 40488 MW; 679DC8FEE69FB421 CRC64; MLPKYAQVKE EISSWINQGK ILPDQKIPTE NELMQQFGVS RHTIRKAIGD LVSQGLLYSV QGGGTFVASR SAKSALHSNK TIGVLTTYIS DYIFPSIIRG IESYLSEQGY SMLLTSTNNN PDNERRGLEN LLSQHIDGLI VEPTKSALQT PNIGYYLNLE KNGIPFAMIN ASYAELAAPS FTLDDVKGGM MAAEHLLSLG HTHMMGIFKA DDTQGVKRMN GFIQAHRERE LFPSPDMIVT FTTEEKESKL LEKVKATLEK NSKHMPTAIL CYNDEIALKV IDMLREMDLK VPEDMSIVGY DDSHFAQISE VKLTSVKHPK SVLGKAAAKY VIDCLEHKKP KQEDVIFEPE LIIRQSARKL NE //