ID   TNRA_PRIMW              Reviewed;         108 AA.
AC   G2RUZ1;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=HTH-type transcriptional regulator TnrA {ECO:0000250|UniProtKB:Q45666};
DE   AltName: Full=Transcriptional nitrogen regulatory protein A {ECO:0000250|UniProtKB:Q45666};
DE            Short=TnrA {ECO:0000250|UniProtKB:Q45666};
GN   Name=tnrA {ECO:0000250|UniProtKB:Q45666};
GN   ORFNames=BMWSH_3277 {ECO:0000312|EMBL:AEN90159.1};
OS   Priestia megaterium (strain WSH-002) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1006007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSH-002;
RX   PubMed=22038958; DOI=10.1128/jb.06066-11;
RA   Liu L., Li Y., Zhang J., Zou W., Zhou Z., Liu J., Li X., Wang L., Chen J.;
RT   "Complete genome sequence of the industrial strain Bacillus megaterium WSH-
RT   002.";
RL   J. Bacteriol. 193:6389-6390(2011).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 6-90, AND 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 regulator that actives the transcription of
CC       genes required for nitrogen assimilation during nitrogen limitation. On
CC       the contrary of the MerR members, which require longer DNA sites for
CC       high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides
CC       as minimal binding site. {ECO:0000250|UniProtKB:Q45666}.
CC   -!- ACTIVITY REGULATION: Under conditions of nitrogen excess, the DNA-
CC       binding activity is inhibited by the formation of a stable complex with
CC       feedback-inhibited GlnA. {ECO:0000250|UniProtKB:Q45666}.
CC   -!- SUBUNIT: Homodimer (PubMed:25691471). Under conditions of nitrogen
CC       excess, TnrA forms a stable complex with feedback-inhibited GlnA (By
CC       similarity). {ECO:0000250|UniProtKB:Q45666,
CC       ECO:0000269|PubMed:25691471}.
CC   -!- INDUCTION: Under conditions of nitrogen excess, repressed by GlnR.
CC       Under conditions of nitrogen-limited growth, it positively regulates
CC       its own expression. {ECO:0000250|UniProtKB:Q45666}.
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:Q45666}.
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DR   EMBL; CP003017; AEN90159.1; -; Genomic_DNA.
DR   RefSeq; WP_013082852.1; NC_017138.1.
DR   PDB; 4R22; X-ray; 2.60 A; B=7-88.
DR   PDB; 4R24; X-ray; 2.25 A; B=6-90.
DR   PDBsum; 4R22; -.
DR   PDBsum; 4R24; -.
DR   AlphaFoldDB; G2RUZ1; -.
DR   SMR; G2RUZ1; -.
DR   GeneID; 48012544; -.
DR   GeneID; 64148942; -.
DR   KEGG; bmh:BMWSH_3277; -.
DR   PATRIC; fig|1006007.3.peg.3356; -.
DR   HOGENOM; CLU_060077_9_2_9; -.
DR   Proteomes; UP000001283; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043562; P:cellular response to nitrogen levels; ISS:UniProtKB.
DR   GO; GO:0090294; P:nitrogen catabolite activation of transcription; ISS:UniProtKB.
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; PS50937; HTH_MERR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..108
FT                   /note="HTH-type transcriptional regulator TnrA"
FT                   /id="PRO_0000439001"
FT   DOMAIN          13..81
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   DNA_BIND        16..35
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   HELIX           7..10
FT                   /evidence="ECO:0007829|PDB:4R24"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:4R22"
FT   HELIX           16..23
FT                   /evidence="ECO:0007829|PDB:4R24"
FT   HELIX           27..35
FT                   /evidence="ECO:0007829|PDB:4R24"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:4R24"
FT   HELIX           53..67
FT                   /evidence="ECO:0007829|PDB:4R24"
FT   HELIX           72..89
FT                   /evidence="ECO:0007829|PDB:4R24"
SQ   SEQUENCE   108 AA;  12717 MW;  5566ACB6924F49B3 CRC64;
     MSTNEASYRD KKVMSIGIVK ELTGLSERQI RYYEKRSLLF PDRTNTGIRK YSFSDVERLM
     DIADRIEEGV QTSEIRTELA KKDEARKMKE VKNQMLQGQL NAHFKRKL