GLTC_BACSU
ID GLTC_BACSU Reviewed; 300 AA.
AC P20668;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transcriptional dual regulator GltC;
DE AltName: Full=HTH-type transcriptional regulator GltC;
GN Name=gltC; OrderedLocusNames=BSU18460;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2548995; DOI=10.1128/jb.171.9.4718-4727.1989;
RA Bohannon D.E., Sonenshein A.L.;
RT "Positive regulation of glutamate biosynthesis in Bacillus subtilis.";
RL J. Bacteriol. 171:4718-4727(1989).
RN [2]
RP SEQUENCE REVISION.
RA Sonenshein A.L.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
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 SEQUENCE REVISION TO 2-3.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-300.
RC STRAIN=168 / SMY;
RA Belitsky B.R., Sonenshein A.L.;
RT "The salt-inducible proHJ operon involved in proline biosynthesis in
RT Bacillus subtilis.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION IN THE GLTAB OPERON EXPRESSION.
RX PubMed=17134717; DOI=10.1016/j.jmb.2006.10.100;
RA Picossi S., Belitsky B.R., Sonenshein A.L.;
RT "Molecular mechanism of the regulation of Bacillus subtilis gltAB
RT expression by GltC.";
RL J. Mol. Biol. 365:1298-1313(2007).
RN [7]
RP INHIBITORY INTERACTION WITH ROCG, ACTIVITY REGULATION, SUBUNIT, AND
RP INDUCTION.
RX PubMed=17608797; DOI=10.1111/j.1365-2958.2007.05816.x;
RA Commichau F.M., Herzberg C., Tripal P., Valerius O., Stulke J.;
RT "A regulatory protein-protein interaction governs glutamate biosynthesis in
RT Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in
RT controlling the transcription factor GltC.";
RL Mol. Microbiol. 65:642-654(2007).
CC -!- FUNCTION: Positive regulator of glutamate biosynthesis (gltAB genes).
CC Negatively regulates its own expression. {ECO:0000269|PubMed:17134717}.
CC -!- ACTIVITY REGULATION: Activated by alpha-ketoglutarate and inhibited by
CC glutamate and by RocG. {ECO:0000269|PubMed:17608797}.
CC -!- SUBUNIT: Interacts with gutamate dehydrogenase RocG.
CC {ECO:0000269|PubMed:17608797}.
CC -!- INTERACTION:
CC P20668; P39633: rocG; NbExp=2; IntAct=EBI-1642006, EBI-1642022;
CC -!- INDUCTION: Induced by glucose, repressed by arginine, less protein
CC accumulates when grown in the presence of glucose and arginine (at
CC protein level). {ECO:0000269|PubMed:17608797}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; M28509; AAA16437.1; -; Unassigned_DNA.
DR EMBL; AL009126; CAB13729.2; -; Genomic_DNA.
DR EMBL; AF006720; AAB62699.1; -; Genomic_DNA.
DR PIR; A69635; A69635.
DR RefSeq; NP_389728.2; NC_000964.3.
DR RefSeq; WP_004399246.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P20668; -.
DR SMR; P20668; -.
DR IntAct; P20668; 1.
DR STRING; 224308.BSU18460; -.
DR PaxDb; P20668; -.
DR PRIDE; P20668; -.
DR EnsemblBacteria; CAB13729; CAB13729; BSU_18460.
DR GeneID; 940104; -.
DR KEGG; bsu:BSU18460; -.
DR PATRIC; fig|224308.179.peg.2013; -.
DR eggNOG; COG0583; Bacteria.
DR InParanoid; P20668; -.
DR OMA; DQALDIC; -.
DR PhylomeDB; P20668; -.
DR BioCyc; BSUB:BSU18460-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW Activator; Amino-acid biosynthesis; DNA-binding; Glutamate biosynthesis;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..300
FT /note="Transcriptional dual regulator GltC"
FT /id="PRO_0000105629"
FT DOMAIN 1..58
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT CONFLICT 2..3
FT /note="EL -> DV (in Ref. 1; AAA16437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 34047 MW; 70BB7CC1EE1A3392 CRC64;
MELRQLRYFM EVAEREHVSE AADHLHVAQS AISRQIANLE EELNVTLFER EGRNIKLTPI
GKEFLIHVKT AMKAIDYAKE QIDEYLDPHR GTVKIGFPTS LASQLLPTVI SAFKEEYPHV
EFLLRQGSYK FLIEAVRNRD IDLALLGPVP TNFSDITGKI LFTEKIYALV PLNHPLAKQK
TVHLIDLRND QFVLFPEGFV LREMAIDTCK QAGFAPLVST EGEDLDAIKG LVSAGMGVTL
LPESTFAETT PRFTVKIPIE FPQVKRTVGI IKPKNRELAP SANDFYEFVI QFFSKLEQYQ
