NTRC_SALTY
ID NTRC_SALTY Reviewed; 469 AA.
AC P41789;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
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=glnG; Synonyms=ntrC; OrderedLocusNames=STM4005;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7602583; DOI=10.1006/jmbi.1995.0330;
RA Flashner Y., Weiss D.S., Keener J., Kustu S.G.;
RT "Constitutive forms of the enhancer-binding protein NtrC: evidence that
RT essential oligomerization determinants lie in the central activation
RT domain.";
RL J. Mol. Biol. 249:700-713(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP STRUCTURE BY NMR OF 1-124.
RX PubMed=7827089; DOI=10.1021/bi00004a036;
RA Volkman B.F., Nohaile M.J., Amy N.K., Kustu S., Wemmer D.E.;
RT "Three-dimensional solution structure of the N-terminal receiver domain of
RT NTRC.";
RL Biochemistry 34:1413-1424(1995).
RN [4]
RP STRUCTURE BY NMR OF 379-469.
RX PubMed=10512705; DOI=10.1006/jmbi.1999.3140;
RA Pelton J.G., Kustu S., Wemmer D.E.;
RT "Solution structure of the DNA-binding domain of NtrC with three alanine
RT substitutions.";
RL J. Mol. Biol. 292:1095-1110(1999).
RN [5]
RP STRUCTURE BY NMR OF 1-124.
RX PubMed=10622255; DOI=10.1038/47273;
RA Kern D., Volkman B.F., Luginbuhl P., Nohaile M.J., Kustu S., Wemmer D.E.;
RT "Structure of a transiently phosphorylated switch in bacterial signal
RT transduction.";
RL Nature 402:894-898(1999).
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; X85104; CAA59425.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22844.1; -; Genomic_DNA.
DR PIR; S53024; S53024.
DR RefSeq; NP_462885.1; NC_003197.2.
DR RefSeq; WP_001188783.1; NC_003197.2.
DR PDB; 1DC7; NMR; -; A=1-124.
DR PDB; 1DC8; NMR; -; A=1-124.
DR PDB; 1J56; NMR; -; A=1-124.
DR PDB; 1KRW; NMR; -; A=1-124.
DR PDB; 1KRX; NMR; -; A=1-124.
DR PDB; 1NTC; NMR; -; A/B=380-469.
DR PDB; 1NTR; NMR; -; A=1-124.
DR PDBsum; 1DC7; -.
DR PDBsum; 1DC8; -.
DR PDBsum; 1J56; -.
DR PDBsum; 1KRW; -.
DR PDBsum; 1KRX; -.
DR PDBsum; 1NTC; -.
DR PDBsum; 1NTR; -.
DR AlphaFoldDB; P41789; -.
DR BMRB; P41789; -.
DR SMR; P41789; -.
DR STRING; 99287.STM4005; -.
DR DrugBank; DB01857; Phosphoaspartate.
DR PaxDb; P41789; -.
DR EnsemblBacteria; AAL22844; AAL22844; STM4005.
DR GeneID; 1255531; -.
DR KEGG; stm:STM4005; -.
DR PATRIC; fig|99287.12.peg.4221; -.
DR HOGENOM; CLU_000445_0_6_6; -.
DR OMA; DWTGNIR; -.
DR PhylomeDB; P41789; -.
DR BioCyc; SENT99287:STM4005-MON; -.
DR EvolutionaryTrace; P41789; -.
DR Proteomes; UP000001014; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Cytoplasm; DNA-binding;
KW Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..469
FT /note="DNA-binding transcriptional regulator NtrC"
FT /id="PRO_0000081167"
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 140..369
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 445..464
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"
FT CONFLICT 150
FT /note="V -> L (in Ref. 1; CAA59425)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1DC7"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1DC7"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1DC8"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1J56"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1DC7"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1DC8"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1J56"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1KRW"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:1DC7"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1NTC"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:1NTC"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1NTC"
FT HELIX 421..440
FT /evidence="ECO:0007829|PDB:1NTC"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:1NTC"
FT HELIX 447..451
FT /evidence="ECO:0007829|PDB:1NTC"
FT HELIX 456..468
FT /evidence="ECO:0007829|PDB:1NTC"
SQ SEQUENCE 469 AA; 52271 MW; 25D3100A2D707E05 CRC64;
MQRGIVWVVD DDSSIRWVLE RALAGAGLTC TTFENGNEVL AALASKTPDV LLSDIRMPGM
DGLALLKQIK QRHPMLPVII MTAHSDLDAA VSAYQQGAFD YLPKPFDIDE AVALVERAIS
HYQEQQQPRN IEVNGPTTDM IGEAPAMQDV FRIIGRLSRS SISVLINGES GTGKELVAHA
LHRHSPRAKA PFIALNMAAI PKDLIESELF GHEKGAFTGA NTIRQGRFEQ ADGGTLFLDE
IGDMPLDVQT RLLRVLADGQ FYRVGGYAPV KVDVRIIAAT HQNLERRVQE GKFREDLFHR
LNVIRIHLPP LRERREDIPR LARHFLQVAA RELGVEAKLL HPETETALTR LAWPGNVRQL
ENTCRWLTVM AAGQEVLIQD LPGELFEAST PDSPSHLPPD SWATLLAQWA DRALRSGHQN
LLSEAQPELE RTLLTTALRH TQGHKQEAAR LLGWGRNTLT RKLKELGME
