ID   NTRB_KLEOX              Reviewed;         349 AA.
AC   P06218;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 119.
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   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2999699; DOI=10.1093/nar/13.21.7591;
RA   McFarlane S.A., Merrick M.J.;
RT   "The nucleotide sequence of the nitrogen regulation gene ntrB and the glnA-
RT   ntrBC intergenic region of Klebsiella pneumoniae.";
RL   Nucleic Acids Res. 13:7591-7606(1985).
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; X03146; CAA26923.1; -; Genomic_DNA.
DR   PIR; A24114; A24114.
DR   RefSeq; WP_004127098.1; NZ_QDDU01000034.1.
DR   AlphaFoldDB; P06218; -.
DR   SMR; P06218; -.
DR   STRING; 571.MC52_08310; -.
DR   GeneID; 64339165; -.
DR   GeneID; 66562538; -.
DR   eggNOG; COG3852; Bacteria.
DR   OrthoDB; 1755994at2; -.
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   GO; GO:0046777; P:protein autophosphorylation; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 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..349
FT                   /note="Sensory histidine kinase/phosphatase NtrB"
FT                   /id="PRO_0000074825"
FT   DOMAIN          5..78
FT                   /note="PAS"
FT   DOMAIN          136..349
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         139
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   349 AA;  38409 MW;  2CECDE3BA36395F2 CRC64;
     MATGTLPDAG QILNSLINSI LLVDDDLAVH YANPAAQQLL AQSSRKLFGT PLPELLSYFS
     LNIGLMQESL AAGQGFTDNE VTLVIDGRSH ILSLTAQRLP EGYILLEMAP MDNQRRLSQE
     QLQHAQQIAA RDLVRGLAHE IKNPLGGLRG AAQLLSKALP DPALMEYTKV IIEQADRLRN
     LVDRLLGPQH PGMHVTESIH KVAERVVKLV SMELPDNVKL VRDYDPSLPE LPHDPDQIEQ
     VLLNIVRNAL QALGPEGGEI TLRTRTAFQL TLHGVRYRLA ARIDVEDNGP GIPSHLQDTL
     FYPMVSGREG GTGLGLSIAR SLIDQHSGKI EFTSWPGHTE FSVYLPIRK