ID GLNR_BACCR Reviewed; 129 AA.
AC P62174; P19083;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=HTH-type transcriptional regulator GlnR {ECO:0000250|UniProtKB:P37582};
GN Name=glnR {ECO:0000250|UniProtKB:P37582}; OrderedLocusNames=BC_3706;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
CC -!- FUNCTION: Transcription repressor during nitrogen excess. On the
CC contrary of the MerR members, which require longer DNA sites for high-
CC affinity binding, GlnR requires a DNA sequence of 17 nucleotides as
CC minimal binding site. {ECO:0000250|UniProtKB:P37582}.
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. Under conditions of nitrogen-limited, GlnR is
CC autoinhibited by its C-terminal region. {ECO:0000250|UniProtKB:P37582}.
CC -!- SUBUNIT: Homodimer under conditions of nitrogen excess. Monomer under
CC conditions of nitrogen-limited. Interacts with feedback-inhibited GlnA
CC in order to stabilizes GlnR-DNA complex.
CC {ECO:0000250|UniProtKB:P37582}.
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}.
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DR EMBL; AE016877; AAP10634.1; -; Genomic_DNA.
DR RefSeq; NP_833433.1; NC_004722.1.
DR RefSeq; WP_000656783.1; NZ_CP034551.1.
DR AlphaFoldDB; P62174; -.
DR SMR; P62174; -.
DR STRING; 226900.BC_3706; -.
DR GeneID; 83637354; -.
DR KEGG; bce:BC3706; -.
DR PATRIC; fig|226900.8.peg.3815; -.
DR HOGENOM; CLU_060077_9_0_9; -.
DR OrthoDB; 9806513at2; -.
DR PRO; PR:P62174; -.
DR Proteomes; UP000001417; 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; cd01105; HTH_GlnR-like; 1.
DR Gene3D; 1.10.1660.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR047057; MerR_fam.
DR PANTHER; PTHR30204:SF65; HTH-TYPE TRANSCRIPTIONAL REGULATOR TNRA; 1.
DR PANTHER; PTHR30204; REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR; 1.
DR Pfam; PF13411; MerR_1; 1.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..129
FT /note="HTH-type transcriptional regulator GlnR"
FT /id="PRO_0000098121"
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
//
