ID   NTRC_BRASR              Reviewed;         480 AA.
AC   P10576;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=DNA-binding transcriptional regulator NtrC {ECO:0000250|UniProtKB:P0AFB8};
DE   AltName: Full=Nitrogen regulation protein NR(I) {ECO:0000250|UniProtKB:P0AFB8};
DE   AltName: Full=Nitrogen regulator I {ECO:0000250|UniProtKB:P0AFB8};
DE            Short=NRI {ECO:0000250|UniProtKB:P0AFB8};
GN   Name=ntrC;
OS   Bradyrhizobium sp. (strain RP501 Parasponia).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=378;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3020561; DOI=10.1073/pnas.83.20.7850;
RA   Nixon B.T., Ronson C.W., Ausubel F.M.;
RT   "Two-component regulatory systems responsive to environmental stimuli share
RT   strongly conserved domains with the nitrogen assimilation regulatory genes
RT   ntrB and ntrC.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:7850-7854(1986).
CC   -!- FUNCTION: Member of the two-component regulatory system NtrB/NtrC,
CC       which controls expression of the nitrogen-regulated (ntr) genes in
CC       response to nitrogen limitation. Phosphorylated NtrC binds directly to
CC       DNA and stimulates the formation of open promoter-sigma54-RNA
CC       polymerase complexes. {ECO:0000250|UniProtKB:P0AFB8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AFB8}.
CC   -!- PTM: Phosphorylated and dephosphorylated by NtrB.
CC       {ECO:0000250|UniProtKB:P0AFB8}.
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DR   EMBL; M14227; AAA26239.1; -; Genomic_DNA.
DR   AlphaFoldDB; P10576; -.
DR   SMR; P10576; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   InterPro; IPR010114; Transcript_reg_NtrC.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01818; ntrC; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Cytoplasm; DNA-binding; Nitrogen fixation;
KW   Nucleotide-binding; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..480
FT                   /note="DNA-binding transcriptional regulator NtrC"
FT                   /id="PRO_0000081171"
FT   DOMAIN          5..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          140..368
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        450..469
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         231..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   480 AA;  52894 MW;  6544F2CB898C9F05 CRC64;
     MPAGSILVAD DDTAIRTVLN QALSRAGYEV RLTGNAATLW RWVSQGEGDL VITDVVMPDE
     NAFDLLPRIK KMRPNLPVIV MSAQNTFMTA IRPSERGAYE YLPKPFDLKE LITIVGRALA
     EPKERVSSPA DDGEFDSIPL VGRSPAMQEI YRVLARLMQT DLTVMISGES GTGKELVARA
     LHDYGRRRNG PFVAVNMAAI PRDLIESELF GHERGAFTGA NTRASGRFEQ AEGGTLFLDE
     IGDMPMEAQT RLLRVLQQGE YTTVGGRTPI KTDVRIVAAS NKDLRILIQQ GLFREDLFFR
     LNVVPLRVPP LRERIEDLPD LIRHFFSLAE KDGLPPKKLD AQALERLKQH RWPGNVRELE
     NLARRLAALY PQDVITASVI DGELAPPAVT SGSTATVGVD NLGGAVEAYL SSHFSGFPNG
     VPPPGLYHRI LKEIEIPLLT AALAATRGNQ IRAADLLGLN RNTLRKKIRD LDIQVYRSGG