LUTR_BACSU
ID LUTR_BACSU Reviewed; 219 AA.
AC O07007; Q795J5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=HTH-type transcriptional regulator LutR;
DE AltName: Full=L-lactate utilization operon repressor;
GN Name=lutR; Synonyms=yvfI; OrderedLocusNames=BSU34180;
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;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 ROLE IN BACILYSIN BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=18604637; DOI=10.1007/s10482-008-9265-8;
RA Koeroglu T.E., Kurt-Guer G., Uenlue E.C., Yazgan-Karatas A.;
RT "The novel gene yvfI in Bacillus subtilis is essential for bacilysin
RT biosynthesis.";
RL Antonie Van Leeuwenhoek 94:471-479(2008).
RN [4]
RP FUNCTION AS A REPRESSOR OF LACTATE UTILIZATION OPERON, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=3610;
RX PubMed=19201793; DOI=10.1128/jb.01464-08;
RA Chai Y., Kolter R., Losick R.;
RT "A widely conserved gene cluster required for lactate utilization in
RT Bacillus subtilis and its involvement in biofilm formation.";
RL J. Bacteriol. 191:2423-2430(2009).
CC -!- FUNCTION: Negatively regulates the transcription of the lutABC operon,
CC which is required for L-lactate utilization. LutR activity is regulated
CC by lactate, since presence of L-lactate, that probably binds to LutR,
CC leads to derepression of the operon. Also appears to be essential for
CC bacilysin biosynthesis. {ECO:0000269|PubMed:18604637,
CC ECO:0000269|PubMed:19201793}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a derepression of
CC lutABC expression. They are also defective in bacilysin production.
CC {ECO:0000269|PubMed:18604637, ECO:0000269|PubMed:19201793}.
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DR EMBL; Z94043; CAB08003.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15423.2; -; Genomic_DNA.
DR PIR; B70038; B70038.
DR RefSeq; NP_391298.2; NC_000964.3.
DR RefSeq; WP_009968191.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O07007; -.
DR SMR; O07007; -.
DR STRING; 224308.BSU34180; -.
DR PaxDb; O07007; -.
DR PRIDE; O07007; -.
DR EnsemblBacteria; CAB15423; CAB15423; BSU_34180.
DR GeneID; 936332; -.
DR KEGG; bsu:BSU34180; -.
DR PATRIC; fig|224308.179.peg.3705; -.
DR eggNOG; COG2186; Bacteria.
DR InParanoid; O07007; -.
DR OMA; EWPVGSR; -.
DR PhylomeDB; O07007; -.
DR BioCyc; BSUB:BSU34180-MON; -.
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; 1.20.120.530; -; 1.
DR InterPro; IPR011711; GntR_C.
DR InterPro; IPR008920; TF_FadR/GntR_C.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF07729; FCD; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00895; FCD; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48008; SSF48008; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..219
FT /note="HTH-type transcriptional regulator LutR"
FT /id="PRO_0000383956"
FT DOMAIN 1..56
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 16..35
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
SQ SEQUENCE 219 AA; 24317 MW; 40E9DB27C9743146 CRC64;
MIKNGELKPG DKLDSVQALA ESFQVSRSAV REALSALKAM GLVEMKQGEG TYLKEFELNQ
ISQPLSAALL MKKEDVKQLL EVRKLLEIGV ASLAAEKRTE ADLERIQDAL KEMGSIEADG
ELGEKADFAF HLALADASQN ELLKHLMNHV SSLLLETMRE TRKIWLFSKK TSVQRLYEEH
ERIYNAVAAG NGAQAEAAML AHLTNVEDVL SGYFEENVQ