ID   NTRC_AZOBR              Reviewed;         481 AA.
AC   P45671;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 122.
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   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=7553451; DOI=10.1139/m95-093;
RA   Machado H.B., Yates M.G., Funayama S., Rigo L.U., Steffens M.B.R.,
RA   Souza E.M., Pedrosa F.O.;
RT   "The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-
RT   ntrC operon and are negatively regulated.";
RL   Can. J. Microbiol. 41:674-684(1995).
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; Z37984; CAA86065.1; -; Genomic_DNA.
DR   PIR; I39494; I39494.
DR   RefSeq; WP_014197046.1; NZ_WFKD01000007.1.
DR   AlphaFoldDB; P45671; -.
DR   SMR; P45671; -.
DR   GeneID; 56453393; -.
DR   OrthoDB; 123059at2; -.
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; 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; 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..481
FT                   /note="DNA-binding transcriptional regulator NtrC"
FT                   /id="PRO_0000081170"
FT   DOMAIN          5..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          141..369
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        451..470
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         232..241
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   481 AA;  53309 MW;  9F117927E124146E CRC64;
     MSAATILVAD DDRAIRTVLT QALARLGHEV RTTGNASTLW RWVADGQGDL IITDVVMPDE
     NGLDLIPRIK KIRPDLRIIV MSAQNTLITA VKAAERGAFE YLPKPFDLKE LVSVVERALN
     SNTPPAALPA DAGEADEQLP LIGRSPAMQE IYRVLARLMG TDLTVTITGE SGTGKELVAR
     ALHDYGKRRN GPFVAINMAA IPRELIESEL FGHEKGAFTG ATNRSTGRFE QAQGGTLFLD
     EIGDMPLEAQ TRLLRVLQEG EYTTVGGRTP IKTDVRIVAA THRDLRTLIR QGLFREDLFY
     RLCVVPIRLP PLRERTEDVP LLVRHFLNQC SAQGLPVKSI DQPAMDRLKR YRWPGNVREL
     ENLVRRLAAL YSQEVIGLDV VEAELADTTP AAQPVEEPQG EGLSAAVERH LKDYFAAHKD
     GMPSNGLYDR VLREVERPLI SLSLSATRGN QIKAAQLLGL NRNTLRKKIR DLDIQVVRGL
     K