NTRC_RHIME
ID NTRC_RHIME Reviewed; 484 AA.
AC P10577; Q53315;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
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; OrderedLocusNames=R01459; ORFNames=SMc01043;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2881918; DOI=10.1128/jb.169.4.1423-1432.1987;
RA Szeto W.W., Nixon B.T., Ronson C.W., Ausubel F.M.;
RT "Identification and characterization of the Rhizobium meliloti ntrC gene:
RT R. meliloti has separate regulatory pathways for activation of nitrogen
RT fixation genes in free-living and symbiotic cells.";
RL J. Bacteriol. 169:1423-1432(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 452-484, AND VARIANT NTRC283.
RX PubMed=8478331; DOI=10.1128/jb.175.9.2662-2673.1993;
RA Labes M., Rastogi V., Watson R., Finan T.M.;
RT "Symbiotic nitrogen fixation by a nifA deletion mutant of Rhizobium
RT meliloti: the role of an unusual ntrC allele.";
RL J. Bacteriol. 175:2662-2673(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; M15810; AAA26346.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC46038.1; -; Genomic_DNA.
DR EMBL; S59667; AAB26386.1; -; Genomic_DNA.
DR PIR; A26934; A26934.
DR RefSeq; NP_385565.1; NC_003047.1.
DR RefSeq; WP_003535443.1; NC_003047.1.
DR AlphaFoldDB; P10577; -.
DR SMR; P10577; -.
DR STRING; 266834.SMc01043; -.
DR EnsemblBacteria; CAC46038; CAC46038; SMc01043.
DR GeneID; 61602922; -.
DR KEGG; sme:SMc01043; -.
DR PATRIC; fig|266834.11.peg.2878; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_1_5; -.
DR OMA; DWTGNIR; -.
DR Proteomes; UP000001976; 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 Activator; ATP-binding; Cytoplasm; DNA-binding; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..484
FT /note="DNA-binding transcriptional regulator NtrC"
FT /id="PRO_0000081173"
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 139..367
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 452..471
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 230..239
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 464
FT /note="N->Y: In ntrC283; appears to be constitutively
FT active."
FT CONFLICT 481..483
FT /note="SRS -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53803 MW; 7DCAEDB255DBF242 CRC64;
MTGATILVAD DDAAIRTVLN QALSRAGYDV RITSNAATLW RWIAAGDGDL VVTDVVMPDE
NAFDLLPRIK KARPDLPVLV MSAQNTFMTA IKASEKGAYD YLPKPFDLTE LIGIIGRALA
EPKRRPSKLE DDSQDGMPLV GRSAAMQEIY RVLARLMQTD LTLMITGESG TGKELVARAL
HDYGKRRNGP FVAINMAAIP RDLIESELFG HEKGAFTGAQ TRSTGRFEQA EGGTLFLDEI
GDMPMDAQTR LLRVLQQGEY TTVGGRTPIR SDVRIVAATN KDLKQSINQG LFREDLYYRL
NVVPLRLPPL RDRAEDIPDL VRHFVQQAEK EGLDVKRFDQ EALELMKAHP WPGNVRELEN
LVRRLTALYP QDVITREIIE NELRSEIPDS PIEKAAARSG SLSISQAVEE NMRQYFASFG
DALPPSGLYD RVLAEMEYPL ILAALTATRG NQIKAADLLG LNRNTLRKKI RELGVSVYRS
SRSA
