GLNR_BACSU
ID GLNR_BACSU Reviewed; 135 AA.
AC P37582;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=HTH-type transcriptional regulator GlnR {ECO:0000303|PubMed:2573733};
GN Name=glnR {ECO:0000303|PubMed:2573733}; OrderedLocusNames=BSU17450;
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=2906311; DOI=10.1016/0378-1119(88)90042-x;
RA Strauch M.A., Aronson A.I., Brown S.W., Schreier H.J., Sonenshein A.L.;
RT "Sequence of the Bacillus subtilis glutamine synthetase gene region.";
RL Gene 71:257-265(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DNA-BINDING.
RX PubMed=2573733; DOI=10.1016/0022-2836(89)90290-8;
RA Schreier H.J., Brown S.W., Hirschi K.D., Nomellini J.F., Sonenshein A.L.;
RT "Regulation of Bacillus subtilis glutamine synthetase gene expression by
RT the product of the glnR gene.";
RL J. Mol. Biol. 210:51-63(1989).
RN [3]
RP ERRATUM OF PUBMED:2573733.
RA Schreier H.J., Brown S.W., Hirschi K.D., Nomellini J.F., Sonenshein A.L.;
RL J. Mol. Biol. 226:571-571(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DNA-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=1677938;
RA Nakano Y., Kimura K.;
RT "Purification and characterization of a repressor for the Bacillus cereus
RT glnRA operon.";
RL J. Biochem. 109:223-228(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.;
RT "Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of
RT spoVJ.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=8799114; DOI=10.1073/pnas.93.17.8841;
RA Wray L.V. Jr., Ferson A.E., Rohrer K., Fisher S.H.;
RT "TnrA, a transcription factor required for global nitrogen regulation in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8841-8845(1996).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=10231480; DOI=10.1046/j.1365-2958.1999.01333.x;
RA Fisher S.H.;
RT "Regulation of nitrogen metabolism in Bacillus subtilis: vive la
RT difference!";
RL Mol. Microbiol. 32:223-232(1999).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=18331450; DOI=10.1111/j.1365-2958.2008.06162.x;
RA Wray L.V. Jr., Fisher S.H.;
RT "Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain
RT required for the interaction with glutamine synthetase.";
RL Mol. Microbiol. 68:277-285(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 1-84, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=25691471; DOI=10.1101/gad.254714.114;
RA Schumacher M.A., Chinnam N.B., Cuthbert B., Tonthat N.K., Whitfill T.;
RT "Structures of regulatory machinery reveal novel molecular mechanisms
RT controlling B. subtilis nitrogen homeostasis.";
RL Genes Dev. 29:451-464(2015).
CC -!- FUNCTION: Transcription repressor that represses many genes including
CC ureABC and tnrA, during nitrogen excess (PubMed:2573733,
CC PubMed:1677938, PubMed:10231480, PubMed:18331450). On the contrary of
CC the MerR members, which require longer DNA sites for high-affinity
CC binding, GlnR requires a DNA sequence of 17 nucleotides as minimal
CC binding site (PubMed:10231480, PubMed:25691471).
CC {ECO:0000269|PubMed:10231480, ECO:0000269|PubMed:1677938,
CC ECO:0000269|PubMed:18331450, ECO:0000269|PubMed:25691471,
CC ECO:0000269|PubMed:2573733}.
CC -!- ACTIVITY REGULATION: Under conditions of nitrogen excess, the DNA
CC binding activity of GlnR is activated by a transient interaction with
CC feedback-inhibited GlnA (PubMed:18331450). Under conditions of
CC nitrogen-limited, GlnR is autoinhibited by its C-terminal region
CC (PubMed:25691471). {ECO:0000269|PubMed:18331450,
CC ECO:0000269|PubMed:25691471}.
CC -!- SUBUNIT: Homodimer under conditions of nitrogen excess (PubMed:1677938,
CC PubMed:18331450, PubMed:25691471). Monomer under conditions of
CC nitrogen-limited (PubMed:25691471). Interacts with feedback-inhibited
CC GlnA in order to stabilizes GlnR-DNA complex (PubMed:1677938,
CC PubMed:18331450, PubMed:25691471). {ECO:0000269|PubMed:1677938,
CC ECO:0000269|PubMed:18331450, ECO:0000269|PubMed:25691471}.
CC -!- INTERACTION:
CC P37582; P12425: glnA; NbExp=3; IntAct=EBI-6402856, EBI-6402863;
CC P37582; P37582: glnR; NbExp=2; IntAct=EBI-6402856, EBI-6402856;
CC -!- INDUCTION: Under conditions of nitrogen-limited growth, repressed by
CC TnrA. {ECO:0000269|PubMed:10231480, ECO:0000269|PubMed:2573733,
CC ECO:0000269|PubMed:8799114}.
CC -!- DISRUPTION PHENOTYPE: In vivo, this mutant constitutively represses
CC glnR expression. In vitro, this mutant binds DNA more tightly than
CC wild-type and this binding is not activated by feedback-inhibited GlnA.
CC {ECO:0000269|PubMed:18331450}.
CC -!- MISCELLANEOUS: The amino acid sequences of the N-terminal DNA binding
CC domains of TnrA and GlnR are highly similar, and both proteins bind to
CC DNA sequences with a common consensus sequence. In contrast, the C-
CC terminal signal transduction domains of TnrA and GlnR have no homology.
CC {ECO:0000305|PubMed:18331450}.
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DR EMBL; M22811; AAA83375.1; -; Genomic_DNA.
DR EMBL; D00854; BAA00729.1; -; Genomic_DNA.
DR EMBL; U66480; AAB41079.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13629.1; -; Genomic_DNA.
DR PIR; JT0393; JT0393.
DR RefSeq; NP_389627.1; NC_000964.3.
DR RefSeq; WP_003238341.1; NZ_JNCM01000035.1.
DR PDB; 4R4E; X-ray; 2.57 A; A/B=1-84.
DR PDBsum; 4R4E; -.
DR AlphaFoldDB; P37582; -.
DR SMR; P37582; -.
DR DIP; DIP-29671N; -.
DR IntAct; P37582; 1.
DR STRING; 224308.BSU17450; -.
DR PaxDb; P37582; -.
DR PRIDE; P37582; -.
DR EnsemblBacteria; CAB13629; CAB13629; BSU_17450.
DR GeneID; 940070; -.
DR KEGG; bsu:BSU17450; -.
DR PATRIC; fig|224308.179.peg.1893; -.
DR eggNOG; COG0789; Bacteria.
DR InParanoid; P37582; -.
DR OMA; SIVMQLT; -.
DR PhylomeDB; P37582; -.
DR BioCyc; BSUB:BSU17450-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR Pfam; PF13411; MerR_1; 1.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..135
FT /note="HTH-type transcriptional regulator GlnR"
FT /id="PRO_0000098122"
FT DOMAIN 11..79
FT /note="HTH merR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT DNA_BIND 14..33
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 96
FT /note="M -> V (in strain: PCI 219)"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:4R4E"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:4R4E"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:4R4E"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4R4E"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:4R4E"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:4R4E"
SQ SEQUENCE 135 AA; 15832 MW; 5FF14F3BB2B1F1D7 CRC64;
MSDNIRRSMP LFPIGIVMQL TELSARQIRY YEENGLIFPA RSEGNRRLFS FHDVDKLLEI
KHLIEQGVNM AGIKQILAKA EAEPEQKQNE KTKKPMKHDL SDDELRQLLK NELMQAGRFQ
RGNTFRQGDM SRFFH
