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Database: UniProt
Entry: C6BGU3_RALP1
LinkDB: C6BGU3_RALP1
Original site: C6BGU3_RALP1 
ID   C6BGU3_RALP1            Unreviewed;       399 AA.
AC   C6BGU3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000256|ARBA:ARBA00039567};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000256|ARBA:ARBA00042313};
DE   AltName: Full=Nitrogen regulator II {ECO:0000256|ARBA:ARBA00043094};
GN   OrderedLocusNames=Rpic12D_1181 {ECO:0000313|EMBL:ACS62473.1};
OS   Ralstonia pickettii (strain 12D).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=428406 {ECO:0000313|EMBL:ACS62473.1};
RN   [1] {ECO:0000313|EMBL:ACS62473.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12D {ECO:0000313|EMBL:ACS62473.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Marsh T., Richardson P.;
RT   "Complete sequence chromosome 1 of Ralstonia pickettii 12D.";
RL   Submitted (JUN-2009) 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. Under conditions of nitrogen
CC       limitation, NtrB autophosphorylates and transfers the phosphoryl group
CC       to NtrC. In the presence of nitrogen, acts as a phosphatase that
CC       dephosphorylates and inactivates NtrC. {ECO:0000256|ARBA:ARBA00037696}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CP001644; ACS62473.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6BGU3; -.
DR   STRING; 428406.Rpic12D_1181; -.
DR   KEGG; rpf:Rpic12D_1181; -.
DR   HOGENOM; CLU_000445_114_39_4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; 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; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF16; SENSORY HISTIDINE KINASE_PHOSPHATASE NTRB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kinase {ECO:0000313|EMBL:ACS62473.1};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:ACS62473.1}.
FT   DOMAIN          182..399
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   399 AA;  44157 MW;  682CDC48B2DE6D44 CRC64;
     MRRLIRKAAR RDEQEQTTPS APSASAAREA AAGEPIDGPP PIPFSHGAPP LFPGLDAAPN
     PILFVRHPAL TIFYANPAAE AALAVSRRQL VEMSLYELFA DPSELAEMIA TVAARQFDAK
     RRDVSLDRLG HEPLHAHAVV GALDFAPASV LLELLPNEQK IRSEREERLL DLTSANKELI
     RNLAHEIKNP LGGIRGAAQL LEFELPERSL REYTQVIIKE SDRLQTLVDR LLEPHRHPHI
     VGDVNIHEVL ERVRSVVLAE FPQGLHIVRD YDASLPEFRG DKEQLIQAVL NIVHNAAHAL
     GARIAQGDGE IILRTRVARK VTIAKRLYKL ALDLHVVDNG PGIPDDIRER IFFPLVSGRE
     GGSGLGLTLA QTFVQQHDGL IECESRPGQT DFRILVPLH
//
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