ID A0A0P1H1P2_9RHOB Unreviewed; 455 AA.
AC A0A0P1H1P2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 Name=ntrC {ECO:0000313|EMBL:CUH83149.1};
GN ORFNames=TM5383_00332 {ECO:0000313|EMBL:CUH83149.1};
OS Thalassovita mediterranea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=340021 {ECO:0000313|EMBL:CUH83149.1, ECO:0000313|Proteomes:UP000051681};
RN [1] {ECO:0000313|EMBL:CUH83149.1, ECO:0000313|Proteomes:UP000051681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8383 {ECO:0000313|EMBL:CUH83149.1,
RC ECO:0000313|Proteomes:UP000051681};
RG Swine Surveillance;
RL Submitted (SEP-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}.
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DR EMBL; CYSF01000002; CUH83149.1; -; Genomic_DNA.
DR RefSeq; WP_058317315.1; NZ_FTNX01000008.1.
DR AlphaFoldDB; A0A0P1H1P2; -.
DR STRING; 340021.TM5383_00332; -.
DR OrthoDB; 9802388at2; -.
DR Proteomes; UP000051681; 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:UP000051681};
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 141..341
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT REGION 120..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
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 455 AA; 50214 MW; 9DC7B83C84273C33 CRC64;
MDGTVLVADD DRTIRTVLTQ ALTRAGCKVH ATSSLTTLMR WVGEGKGDVV ISDVVMPDGN
GLEMLPKIAQ DRPGLPVIVI SAQNTIMTAI QAAEAEAYDY LPKPFDLPDL MKRTAKALEQ
NHRSAPAARV DEGERPDELP LVGRTPAMQA LYRLVARVMN TDLPVLIAGE SGTGKSLIAR
AIHDFSDRRT LPFVTITAAD LQDIEGPARV LARVKGGTVL IDEIGDVDAE VQARIVRMID
NPGEHVPRFM ATSQTDLTEA LDRGDIRQDL YYRLSGATLV VPSLRERVED IPLLAEHFLL
RAERDGQPSR RLSDDAVELM RSYSWPGNVR QLEHAVRRLV LTSRADEITR TEVEMVLGNQ
PEMEPVLGGG DTEKLSASVA RHLRRYFDLH GAMLPPAGLY ARILREVELP LIEIALEATG
GNQAKCADLL GINRNTLRKK ITDLDINVTR RRKLM
//
