TRER_BACSU
ID TRER_BACSU Reviewed; 238 AA.
AC P39796;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=HTH-type transcriptional regulator TreR {ECO:0000303|PubMed:8755887};
DE AltName: Full=Trehalose operon repressor {ECO:0000303|PubMed:8755887};
GN Name=treR; Synonyms=yfxA; OrderedLocusNames=BSU07820;
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=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8917076; DOI=10.1016/0378-1119(96)00120-5;
RA Schoeck F., Dahl M.K.;
RT "Analysis of DNA flanking the treA gene of Bacillus subtilis reveals genes
RT encoding a putative specific enzyme IITre and a potential regulator of the
RT trehalose operon.";
RL Gene 175:59-63(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT region of the Bacillus subtilis chromosome containing genes for trehalose
RT metabolism and acetoin utilization.";
RL Microbiology 142:3057-3065(1996).
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7651129; DOI=10.1111/j.1365-2958.1995.tb02396.x;
RA Helfert C., Gotsche S., Dahl M.K.;
RT "Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a
RT phospho-alpha-(1-1)-glucosidase encoded by the treA gene.";
RL Mol. Microbiol. 16:111-120(1995).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=8755887; DOI=10.1128/jb.178.15.4576-4581.1996;
RA Schoeck F., Dahl M.K.;
RT "Expression of the tre operon of Bacillus subtilis 168 is regulated by the
RT repressor TreR.";
RL J. Bacteriol. 178:4576-4581(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 90-238, AND SUBUNIT.
RX PubMed=17705272; DOI=10.1002/prot.21516;
RA Rezacova P., Krejcirikova V., Borek D., Moy S.F., Joachimiak A.,
RA Otwinowski Z.;
RT "The crystal structure of the effector-binding domain of the trehalose
RT repressor TreR from Bacillus subtilis 168 reveals a unique quarternary
RT assembly.";
RL Proteins 69:679-682(2007).
CC -!- FUNCTION: Repressor for the trePA operon. It is able to bind trehalose-
CC 6-phosphate. {ECO:0000269|PubMed:8755887}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000269|PubMed:17705272}.
CC -!- INDUCTION: Probably induced by trehalose-6-phosphate.
CC {ECO:0000305|PubMed:8755887}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are constitutive in the
CC expression of the trePA operon. {ECO:0000269|PubMed:8755887}.
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DR EMBL; Z54245; CAA91016.1; -; Genomic_DNA.
DR EMBL; D83967; BAA23407.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12611.1; -; Genomic_DNA.
DR EMBL; X80203; CAA56496.1; ALT_FRAME; Genomic_DNA.
DR PIR; JC5038; JC5038.
DR RefSeq; NP_388663.1; NC_000964.3.
DR RefSeq; WP_003233679.1; NZ_JNCM01000032.1.
DR PDB; 2OGG; X-ray; 2.50 A; A=90-238.
DR PDBsum; 2OGG; -.
DR AlphaFoldDB; P39796; -.
DR SMR; P39796; -.
DR STRING; 224308.BSU07820; -.
DR PaxDb; P39796; -.
DR PRIDE; P39796; -.
DR DNASU; 936133; -.
DR EnsemblBacteria; CAB12611; CAB12611; BSU_07820.
DR GeneID; 936133; -.
DR KEGG; bsu:BSU07820; -.
DR PATRIC; fig|224308.179.peg.846; -.
DR eggNOG; COG2188; Bacteria.
DR InParanoid; P39796; -.
DR OMA; HRPDKFR; -.
DR PhylomeDB; P39796; -.
DR BioCyc; BSUB:BSU07820-MON; -.
DR EvolutionaryTrace; P39796; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.1410.10; -; 1.
DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR InterPro; IPR012770; TreR.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR011663; UTRA.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00392; GntR; 1.
DR Pfam; PF07702; UTRA; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SMART; SM00866; UTRA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF64288; SSF64288; 1.
DR TIGRFAMs; TIGR02404; trehalos_R_Bsub; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..238
FT /note="HTH-type transcriptional regulator TreR"
FT /id="PRO_0000050669"
FT DOMAIN 1..71
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 31..50
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:2OGG"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2OGG"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2OGG"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:2OGG"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2OGG"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:2OGG"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:2OGG"
FT STRAND 172..184
FT /evidence="ECO:0007829|PDB:2OGG"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:2OGG"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:2OGG"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:2OGG"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2OGG"
SQ SEQUENCE 238 AA; 27842 MW; 41715DA057CEA600 CRC64;
MKVNKFITIY KDIAQQIEGG RWKAEEILPS EHELTAQYGT SRETVRKALH MLAQNGYIQK
IRGKGSVVLN REKMQFPVSG LVSFKELAQT LGKETKTTVH KFGLEPPSEL IQKQLRANLD
DDIWEVIRSR KIDGEHVILD KDYFFRKHVP HLTKEICENS IYEYIEGELG LSISYAQKEI
VAEPCTDEDR ELLDLRGYDH MVVVRNYVFL EDTSLFQYTE SRHRLDKFRF VDFARRGK
