ID   NTRY_AZOBR              Reviewed;         777 AA.
AC   P45675;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Nitrogen regulation protein NtrY homolog;
DE            EC=2.7.13.3;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RA   Ishida M.L.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-300.
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=7553451; DOI=10.1139/m95-093;
RA   Machado H.B., Yates M.G., Funayama S., Rigo L.U., Steffens M.B.R.,
RA   Souza E.M., Pedrosa F.O.;
RT   "The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-
RT   ntrC operon and are negatively regulated.";
RL   Can. J. Microbiol. 41:674-684(1995).
CC   -!- FUNCTION: Member of the two-component regulatory system NtrY/NtrX
CC       involved in nitrogen level control. Probably activates NtrX by
CC       phosphorylation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; Z37984; CAA86066.2; -; Genomic_DNA.
DR   PIR; I39495; I39495.
DR   AlphaFoldDB; P45675; -.
DR   PRIDE; P45675; -.
DR   BRENDA; 2.7.13.3; 611.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR017232; NtrY.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nitrogen fixation;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..777
FT                   /note="Nitrogen regulation protein NtrY homolog"
FT                   /id="PRO_0000074834"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          327..380
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          392..465
FT                   /note="PAS"
FT   DOMAIN          523..745
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          745..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  84353 MW;  23C524D2F0631D76 CRC64;
     MSPTPPETVT PLWQQFLRWA ARVGLAKRLA FALSLAALVA GFATYTALTE SAPFGETNPR
     TVTWLLTLDL ALLLLLGVLI ARRIVYLWIG RRRGLAGSQM HVRLVAVFSL LAVAPAIIMA
     IFSTVFFYVG VQSWFSERVR TAVNESLAVA SAYLHEHQQN IRADALAMAN DLNQEAARLA
     SDPERFEQVV ATQAMLRALS EAIVFNGTTG AIVARSGYTF ALEFDPIPDD KLATARRGEV
     AMIVSENDDR VRALVRLDRF ADTYLYVGRM VEPRVLSHMA SAEGAVREFG ALESQRGSLQ
     ITFTLIFLCV ALLLLLAAVW AGLIFATRLV RPISALIGAA DRVRAGDLTV RVTERPAEDD
     LALLSRAFNR MTTEIESQRH ALLSANRLID SRRRFTETVL SGVSAGRDGL DAEGRITLSK
     FSAARLLGVK DAESLIGMRL AELVPEMGGL LHEAPGRPGL VVQDQIKIRR DGTTPLTLLV
     RISTEGRGSG MMRGYVVTFD EHHRTWSPAQ RKAAWARRRP IAASPTRVKN PLTPIQLSAE
     PCAASTLKEI TSDTEVFTMC TDTIVRQVDD IRRMVDEFSA FARMPQPVMK PCNLNDLVRQ
     AVFLQSSAHA GKIKFDMALP QGPLTVPCDS RQISQALTNL LQNAADAIEG RPPPAEGTEL
     PPGHVAIRVE ADAERIAMII EDNGKGLPTE ERDRLTEPYV TTRAKGTGLG LAIVKKIMED
     HGGVLTLEDR EGGGARVGLV IPQHIPPASG TAAGDAPGGV GTPAETGEEK RHAAHGA