ID   GLNR_BACCE              Reviewed;         129 AA.
AC   P62173; P19083;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=HTH-type transcriptional regulator GlnR {ECO:0000303|PubMed:1677938};
GN   Name=glnR {ECO:0000303|PubMed:1677938};
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 3131;
RX   PubMed=2572584; DOI=10.1093/oxfordjournals.jbchem.a122834;
RA   Nakano Y., Kato C., Tanaka E., Kimura K., Horikoshi K.;
RT   "Nucleotide sequence of the glutamine synthetase gene (glnA) and its
RT   upstream region from Bacillus cereus.";
RL   J. Biochem. 106:209-215(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-5, FUNCTION, ACTIVITY REGULATION, DNA-BINDING, AND
RP   SUBUNIT.
RC   STRAIN=NBRC 3131;
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).
CC   -!- FUNCTION: Transcription repressor during nitrogen excess
CC       (PubMed:1677938). On the contrary of the MerR members, which require
CC       longer DNA sites for high-affinity binding, GlnR requires a DNA
CC       sequence of 17 nucleotides as minimal binding site (By similarity).
CC       {ECO:0000250|UniProtKB:P37582, ECO:0000269|PubMed:1677938}.
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 (Probable). Under conditions of nitrogen-
CC       limited, GlnR is autoinhibited by its C-terminal region (By
CC       similarity). {ECO:0000250|UniProtKB:P37582,
CC       ECO:0000305|PubMed:1677938}.
CC   -!- SUBUNIT: Homodimer under conditions of nitrogen excess
CC       (PubMed:1677938). Monomer under conditions of nitrogen-limited (By
CC       similarity). Interacts with feedback-inhibited GlnA in order to
CC       stabilizes GlnR-DNA complex (By similarity).
CC       {ECO:0000250|UniProtKB:P37582, ECO:0000269|PubMed:1677938}.
CC   -!- INDUCTION: Under conditions of nitrogen-limited growth, repressed by
CC       TnrA. {ECO:0000250|UniProtKB:P37582}.
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:0000250|UniProtKB:P37582}.
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; D00513; BAA00402.1; -; Genomic_DNA.
DR   PIR; JU0076; JU0076.
DR   RefSeq; WP_000656783.1; NZ_WBPP01000016.1.
DR   AlphaFoldDB; P62173; -.
DR   SMR; P62173; -.
DR   STRING; 1396.DJ87_1225; -.
DR   GeneID; 59155801; -.
DR   GeneID; 64202245; -.
DR   GeneID; 67508342; -.
DR   eggNOG; COG0789; Bacteria.
DR   OMA; SIVMQLT; -.
DR   OrthoDB; 1661714at2; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   Direct protein sequencing; DNA-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..129
FT                   /note="HTH-type transcriptional regulator GlnR"
FT                   /id="PRO_0000098120"
FT   DOMAIN          10..78
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   DNA_BIND        13..32
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
SQ   SEQUENCE   129 AA;  15173 MW;  BA363083892C6802 CRC64;
     MKEDRRSAPL FPIGIVMDLT QLSARQIRYY EEHNLVSPTR TKGNRRLFSF NDVDKLLEIK
     DLLDQGLNMA GIKQVLLMKE NQTEAVKVKE ETKEISKTEL RKILRDELQH TGRFNRTSLR
     QGDISRFFH