ID   NTRX_AZOC5              Reviewed;         454 AA.
AC   Q04849; A8IBK2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Nitrogen assimilation regulatory protein NtrX;
GN   Name=ntrX; OrderedLocusNames=AZC_3083;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1661370; DOI=10.1007/bf00293830;
RA   Pawlowski K., Klosse U., de Bruijn F.J.;
RT   "Characterization of a novel Azorhizobium caulinodans ORS571 two-component
RT   regulatory system, NtrY/NtrX, involved in nitrogen fixation and
RT   metabolism.";
RL   Mol. Gen. Genet. 231:124-138(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system NtrY/NtrX
CC       involved in the activation of nitrogen assimilatory genes such as GlnA.
CC       NtrX is probably phosphorylated by NtrY and interacts with sigma-54.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X63841; CAA45331.1; -; Genomic_DNA.
DR   EMBL; AP009384; BAF89081.1; -; Genomic_DNA.
DR   PIR; S18625; S18625.
DR   RefSeq; WP_012171607.1; NC_009937.1.
DR   AlphaFoldDB; Q04849; -.
DR   SMR; Q04849; -.
DR   STRING; 438753.AZC_3083; -.
DR   EnsemblBacteria; BAF89081; BAF89081; AZC_3083.
DR   KEGG; azc:AZC_3083; -.
DR   eggNOG; COG2204; Bacteria.
DR   HOGENOM; CLU_000445_0_6_5; -.
DR   OMA; PTNSRVM; -.
DR   OrthoDB; 123059at2; -.
DR   Proteomes; UP000000270; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
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; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
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   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; DNA-binding; Nitrogen fixation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..454
FT                   /note="Nitrogen assimilation regulatory protein NtrX"
FT                   /id="PRO_0000081164"
FT   DOMAIN          4..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          141..367
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        430..449
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         229..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   454 AA;  50220 MW;  9612731C6AEEBFB1 CRC64;
     MAHDILIVDD EPDISGLVAG ILEDEGYSAR TARDADGALA EIAARRPNLI FLDIWLQGSR
     LDGLELLDII KREHPEVPVV MISGHGNIET AVAAIKRGAY DFIEKPFNAD RLVVITERAL
     ETLRLRREVR ELKQLTQPHT MVGRSSVIQQ LRATVDRVGP TNSRILIVGP SGSGKELTAR
     MIHAASARAQ GPFVVINAAA ITPERLEYEL FGVEEGEGRE RHRGALEEAH GGTLFLDEIA
     DMPRETQNRV LRVLVEQTFS RIGSSEKVRV DVRIISSTGR HLEEEIAAGR FREDLYHRLS
     VVPIRVPPLA ERREDIPDLV DFFIDLISQT TGLQRRKVGE DAMAVLQSHD WPGNVRQLRN
     NVERLLILAG GDPDAEVTAS MLPPDVGALV PTLPNGNGGE HLMGLPLREA REVFEREYLA
     AQINRFGGNI SRTAEFVGME RSALHRKLKA LGVG