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Database: UniProt
Entry: G1XWR5_9PROT
LinkDB: G1XWR5_9PROT
Original site: G1XWR5_9PROT 
ID   G1XWR5_9PROT            Unreviewed;       783 AA.
AC   G1XWR5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Nitrogen regulation protein {ECO:0000256|PIRNR:PIRNR037532};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR037532};
GN   Name=ntrY {ECO:0000313|EMBL:EGY02290.1};
GN   ORFNames=AZA_87994 {ECO:0000313|EMBL:EGY02290.1};
OS   Nitrospirillum amazonense Y2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Nitrospirillum.
OX   NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY02290.1, ECO:0000313|Proteomes:UP000018435};
RN   [1] {ECO:0000313|EMBL:EGY02290.1, ECO:0000313|Proteomes:UP000018435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX   PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA   Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA   Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT   "Genomic insights into the versatility of the plant growth-promoting
RT   bacterium Azospirillum amazonense.";
RL   BMC Genomics 12:409-409(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085,
CC         ECO:0000256|PIRNR:PIRNR037532};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037532};
CC       Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR037532}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:EGY02290.1}.
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DR   EMBL; AFBX01000105; EGY02290.1; -; Genomic_DNA.
DR   RefSeq; WP_004271809.1; NZ_AFBX01000105.1.
DR   AlphaFoldDB; G1XWR5; -.
DR   PATRIC; fig|1003237.3.peg.734; -.
DR   Proteomes; UP000018435; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR017232; NtrY.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR037532};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR037532};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037532};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037532, ECO:0000256|SAM:Phobius};
KW   Nitrogen fixation {ECO:0000256|PIRNR:PIRNR037532};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037532};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018435};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037532};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR037532, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|PIRNR:PIRNR037532}.
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          342..397
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          535..758
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  85896 MW;  7824927DDD2AE79F CRC64;
     MTEVPPALIT PPSPPVPPQV PPKSDSWWRR LSVWSARLGL GNKLAVALAF AAVLSGFATY
     AALTQQPPFG NSPNTVSLLL TLDGALLLLL LALMARRIVG LWIERRRGLA GSRLHVRLVA
     VFSLLAVLPA IVMAAFSAFF FYLGLQSWFS DRVRTAVNES LVVAQAYLDE HQIAIRNDAS
     WVANDLLAAR QGPLVTLDPL FIYAFLRNES FQRSFTEAVI FDGQGRQYGS YTLGSVFQPD
     VMPKERLERA RKGEVDFEFN EKEKRVTALI RLDPDFDIFL LLGRPVEAKV MEHLNAAQTA
     VREYTELEGQ RFGLQTKMTL IFIIVSLLLL LVAIWAGLNF ANTLITPISA LIIAAERIRT
     GDLTARVPET LPGPEDELTS LSRAFNRMTS QLSSQRSDLV EANRQLDLRR RFTEAVLAGV
     SAGVIGLDEQ GFINLPNQSA AQLLDIPDVH EMMGRDILAV VPELEDLMSA IRRRPSRLVE
     GQVQIRRGNT QRTLLVRVAA DTSGNGIRGF VITFDDVSEL LSAQRKAAWA DVARRIAHEI
     KNPLTPIQLS AERLRRKYLK EIQSDPETFK AMTDTIVRHV DDIGRMVDEF SAFARMPTPV
     MKPQNIQELC RQAVFLQATA QSGIKFDSIL PPEKVEVECD GRQISQALTN LLKNAVEAIE
     GRMEEDAADG HDSPPGHISL KVEALDDHIV LTIADNGRGL PSEGRDRLTE PYVTTRAKGT
     GLGLAIVKKI LEDHGGTLGL DDNPGGGARV TLILPLVQAA APQDAETAAS PVLVAGTSAS
     KGV
//
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