ID   NTRC_PROHU              Reviewed;         473 AA.
AC   P28787;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 127.
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   Proteus hauseri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=183417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC
RC   4175 / NRRL B-3405;
RX   PubMed=8095910; DOI=10.1111/j.1574-6968.1993.tb05952.x;
RA   Steglitz-Moersdorf U., Moersdorf G., Kaltwasser H.;
RT   "Cloning, heterologous expression, and sequencing of the Proteus vulgaris
RT   glnAntrBC operon and implications of nitrogen control on heterologous
RT   urease expression.";
RL   FEMS Microbiol. Lett. 106:157-164(1993).
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; X68129; CAA48236.1; -; Genomic_DNA.
DR   PIR; S23901; S23901.
DR   RefSeq; WP_064718178.1; NZ_PGWU01000008.1.
DR   AlphaFoldDB; P28787; -.
DR   SMR; P28787; -.
DR   STRING; 1354271.M997_0112; -.
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; 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; 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..473
FT                   /note="DNA-binding transcriptional regulator NtrC"
FT                   /id="PRO_0000081169"
FT   DOMAIN          5..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          141..370
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        447..466
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   473 AA;  53524 MW;  9F2A1A69426CE2C8 CRC64;
     MQKGNVWVVD DDSSIRWVLE RAITREGMLC RAFEHANDVL KALNSEQPDV LLSDIRMPDM
     DGLSLLKIIK EQYPTLPVII MTAHSDLDAA VNAYQQGAFD YLPKPFDIDE TLALIERAIT
     HYREQKQPNN AENILQSVSD MIGEAPAMQE VYRIIGRLSR SSISVLINGE SGTGKELVAH
     ALHRHSPRAL APFIALNMAA IPKDLIESEL FGHEKGAFTG ASQVRQGRFE QANGGSLFLD
     EIGDMPLDIQ TRLLRVLAEG QFYRVGGYAP VKVDVRIIAA THQDLEKRVN EGDFREDLYH
     RLNVIRIQLP PLRDRTEDIP SLARYFLQKT AKELGVETKS LHEQSLKTMM EYVWSGNVRQ
     LENVCRWLTV MTASQEIMPQ DLPSEIRLAD EKAKNINRLT SQHWSQHLSL WADEALGEGK
     ENILNDALPQ FERTLLLSAL AYTQGHKQDA ARLLGWGRNT LTRKLKELGI EDY