ID X6L3A5_9RHOB Unreviewed; 456 AA.
AC X6L3A5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA-binding transcriptional regulator NtrC {ECO:0000256|ARBA:ARBA00019059};
DE AltName: Full=Nitrogen regulation protein NR(I) {ECO:0000256|ARBA:ARBA00029881};
DE AltName: Full=Nitrogen regulator I {ECO:0000256|ARBA:ARBA00031910};
GN ORFNames=P279_05100 {ECO:0000313|EMBL:ETA53100.1};
OS Rhodobacteraceae bacterium PD-2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA53100.1, ECO:0000313|Proteomes:UP000023196};
RN [1] {ECO:0000313|EMBL:ETA53100.1, ECO:0000313|Proteomes:UP000023196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD-2 {ECO:0000313|EMBL:ETA53100.1,
RC ECO:0000313|Proteomes:UP000023196};
RX PubMed=25700405;
RA Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT Prorocentrum donghaiense.";
RL Genome Announc. Announc.3:e01549-14(2015).
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:0000256|ARBA:ARBA00043886}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETA53100.1}.
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DR EMBL; AWRV02000006; ETA53100.1; -; Genomic_DNA.
DR AlphaFoldDB; X6L3A5; -.
DR PATRIC; fig|1169855.3.peg.898; -.
DR HOGENOM; CLU_000445_0_1_5; -.
DR OrthoDB; 9802388at2; -.
DR Proteomes; UP000023196; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR025944; Sigma_54_int_dom_CS.
DR PANTHER; PTHR32071:SF15; DNA-BINDING TRANSCRIPTIONAL REGULATOR NTRC; 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF14532; Sigma54_activ_2; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000023196};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 4..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 142..342
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT REGION 118..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 456 AA; 50245 MW; 2FD3E37482DEFA7B CRC64;
MDGTVLVADD DRTIRTVLTQ ALTRAGCKVH ATSSLTTLMR WVGEGKGDVV ISDVMMPDGN
GLEMLPKIAE DRPGLPVIVI SAQNTIMTAI QAAEAEAYDY LPKPFDLPDL MKRTARALEN
RNKQPRRDEP VVGADEPDEL PLVGKTPAMQ ALYRLVAKVM NTDLPVLITG ESGTGKSLIA
RALHDFSDRR TLPFVTVTGA DLSDLDGPAR VLARVKGGTL LIDEIADIDD EVQGRIVRMK
DVPGEHVPRF LASSQYDPQS LTETGKVRHD LFYRLDGAAI AVPSLRERVE DIPLLAEHFL
LRAERDGAPK RWLSEGAAEL FRVYSWPGNV RQLENAVRRL SLTSRSEEIT RAEVEAVLGN
QPETGPVLRG GDGDKLADSV SRHLRRYFDL HGAMLPPPGL YGRILREVEA PLIEIALEAT
GGNQAKCADL LGINRNTLRK KITDLDIRVT RRRKLM
//
