ID A0A117S4T2_9SPHN Unreviewed; 472 AA.
AC A0A117S4T2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=APF82_03490 {ECO:0000313|EMBL:KUO52096.1};
OS Sphingomonadales bacterium BRH_c42.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO52096.1, ECO:0000313|Proteomes:UP000054281};
RN [1] {ECO:0000313|EMBL:KUO52096.1, ECO:0000313|Proteomes:UP000054281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO52096.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO52096.1}.
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DR EMBL; LOEX01000118; KUO52096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117S4T2; -.
DR Proteomes; UP000054281; 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; IPR025943; Sigma_54_int_dom_ATP-bd_2.
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; PF00158; Sigma54_activat; 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; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
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 139..367
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT REGION 116..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
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 472 AA; 51241 MW; 008CB02699B52097 CRC64;
MSGKILLVED DQAIATVITA ALEDEGMLVH RCDSIAARDR LLAGQRFDTM LTDVMLADGD
GIATLAAVRT IDPNMPVIVL SAQNTLDTAV RASETQAFEY FPKPFDLEEL VRATRQAAGR
RSEDRGDAPE ADEHAGLPMV GRSQAMQGVY RMIARVLRND LTVLVTGESG TGKELVAEAI
HQLGARKSGP FVAVNAAAIP SELIESELFG HEKGAFTGAI NQAIGKFEQA NGGTLFLDEI
GDMPAEAQTR LLRALQSGTI RRVGGRQEIS VNARIIAATN RNLAPMIAAG TFREDLFYRL
NVVPIELPPL RQRREDIGVL AQHFLVKAAE DGLSRHAITS DAVRALEQRS WPGNVRELRN
VIYRLALMAR DDTIDAASVR DILGDSDSVG KPGKADGFRA ALDQWLALTP VQKGALYRNA
LAAFEKPLFE HALAQTSGNQ LRAAHVLGIN RNTLRKRIVE LGIDPDRFGH AI
//
