NTRC_KLEPN
ID NTRC_KLEPN Reviewed; 469 AA.
AC P03029;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3011408; DOI=10.1002/j.1460-2075.1986.tb04230.x;
RA Drummond M., Whitty P., Wootton J.;
RT "Sequence and domain relationships of ntrC and nifA from Klebsiella
RT pneumoniae: homologies to other regulatory proteins.";
RL EMBO J. 5:441-447(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989799; DOI=10.1093/nar/13.12.4539;
RA Buikema W.J., Szeto W.W., Lemley P.V., Orme-Johnson W.H., Ausubel F.M.;
RT "Nitrogen fixation specific regulatory genes of Klebsiella pneumoniae and
RT Rhizobium meliloti share homology with the general nitrogen regulatory gene
RT ntrC of K. pneumoniae.";
RL Nucleic Acids Res. 13:4539-4555(1985).
RN [3]
RP MUTAGENESIS OF SER-170.
RX PubMed=2041769; DOI=10.1093/nar/19.9.2281;
RA Austin S., Kundrot C., Dixon R.;
RT "Influence of a mutation in the putative nucleotide binding site of the
RT nitrogen regulatory protein NTRC on its positive control function.";
RL Nucleic Acids Res. 19:2281-2287(1991).
RN [4]
RP ATPASE ACTIVITY.
RX PubMed=1534752; DOI=10.1002/j.1460-2075.1992.tb05281.x;
RA Austin S., Dixon R.;
RT "The prokaryotic enhancer binding protein NTRC has an ATPase activity which
RT is phosphorylation and DNA dependent.";
RL EMBO J. 11:2219-2228(1992).
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; X02617; CAA26473.1; -; Genomic_DNA.
DR PIR; B91060; RGKBCP.
DR AlphaFoldDB; P03029; -.
DR SMR; P03029; -.
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; IMP:CACAO.
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 Activator; ATP-binding; Cytoplasm; DNA-binding; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..469
FT /note="DNA-binding transcriptional regulator NtrC"
FT /id="PRO_0000081168"
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 MUTAGEN 170
FT /note="S->A: Prevents transcriptional activation at sigma
FT 54-dependent promoters both in vivo and in vitro."
FT /evidence="ECO:0000269|PubMed:2041769"
FT CONFLICT 144
FT /note="A -> R (in Ref. 2; CAA26473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52344 MW; 7F41DDBD50F62F18 CRC64;
MQRGIAWIVD DDSSIRWVLE RALTGAGLSC TTFESGNEVL DALTTKTPDV LLSDIRMPGM
DGLALLKQIK QRHPMLPVII MTAHSDLDAA VSAYQQGAFD YLPKPFDIDE AVALVDRAIS
HYQEQQQPRN APINSPTADI IGEAPAMQDV FRIIGRLSRS SISVLINGES GTGKELVAHA
LHRHSPRAKA PFIALNMAAI PKDLIESELF GHEKGAFTGA NTVRQGRFEQ ADGGTLFLDE
IGDMPLDVQT RLLRVLADGQ FYRVGGYAPV KVDVRIIAAT HQNLELRVQE GKFREDLFHR
LNVIRVHLPP LRERREDIPR LARHFLQIAA RELGVEAKQL HPETEMALTR LAWPGNVRQL
ENTCRWLTVM AAGQEVLTQD LPSELFETAI PDNPTQMLPD SWATLLGQWA DRALRSGHQN
LLSEAQPEME RTLLTTALRH TQGHKQEAAR LLGWGRNTLT RKLKELGME
