ID   NTRB_RHILP              Reviewed;         383 AA.
AC   P41503;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000250|UniProtKB:P0AFB5};
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AFB5};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:P0AFB5};
DE   AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000250|UniProtKB:P0AFB5};
DE   AltName: Full=Nitrogen regulator II {ECO:0000250|UniProtKB:P0AFB5};
DE            Short=NRII {ECO:0000250|UniProtKB:P0AFB5};
GN   Name=ntrB;
OS   Rhizobium leguminosarum bv. phaseoli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE-3;
RX   PubMed=8412703; DOI=10.1111/j.1365-2958.1993.tb01717.x;
RA   Patriarca E.J., Riccio A., Tate R., Colonna-Romano S., Iaccarino M.,
RA   Defez R.;
RT   "The ntrBC genes of Rhizobium leguminosarum are part of a complex operon
RT   subject to negative regulation.";
RL   Mol. Microbiol. 9:569-577(1993).
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:0000250|UniProtKB:P0AFB5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P0AFB5};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AFB5}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P0AFB5}.
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DR   EMBL; X71436; CAA50568.1; -; Genomic_DNA.
DR   PIR; S36202; S36202.
DR   AlphaFoldDB; P41503; -.
DR   SMR; P41503; -.
DR   BRENDA; 2.7.13.3; 5343.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; 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   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Kinase; Nitrogen fixation;
KW   Nucleotide-binding; Phosphoprotein; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..383
FT                   /note="Sensory histidine kinase/phosphatase NtrB"
FT                   /id="PRO_0000074830"
FT   DOMAIN          147..366
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         150
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   383 AA;  41194 MW;  21C5AF53207BD2D4 CRC64;
     MTKDTTSPPD QAGGTVAMAV LNAIQNPVVM VDESGFIAFA NWEAEAFFGA AFASGALPDL
     DIHSFGSPLL ALVDQVRTQG SPVNEYRVDL SSPRLGQDKL VDLYVAPVLS EPGGVVIVFQ
     ERSMADKIDR QLTHRAAARS VTGLASSLAH EIKNPLSGNR GAAQLLEQSV IDDDRALTRL
     ICDETDRIVS LVDRMEVFSD ERPVRRMPVN IHSVLDHVKR LAQSGFARNI RITESYDPSL
     PAVYANRDQL VQVFLNLVKN AAEAVGDRPD GEIMLTTAYR PGIRLSVAGT REKISLPLEF
     CVHDNGPGVP ADLLPHLFDP FITTKTNGSG LGLALVAKII GDHGGIIECD SQNSRTTFRV
     LMPASKDASL EDASSASSTG PSR