ID   NTRB_PROHU              Reviewed;         348 AA.
AC   P28788;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Proteus hauseri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=183417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC
RC   4175 / NRRL B-3405;
RX   PubMed=8095910; DOI=10.1111/j.1574-6968.1993.tb05952.x;
RA   Steglitz-Moersdorf U., Moersdorf G., Kaltwasser H.;
RT   "Cloning, heterologous expression, and sequencing of the Proteus vulgaris
RT   glnAntrBC operon and implications of nitrogen control on heterologous
RT   urease expression.";
RL   FEMS Microbiol. Lett. 106:157-164(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; X68129; CAA48235.1; -; Genomic_DNA.
DR   PIR; S23900; S23900.
DR   AlphaFoldDB; P28788; -.
DR   SMR; P28788; -.
DR   STRING; 1354271.M997_0111; -.
DR   BRENDA; 2.7.13.3; 14542.
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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 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..348
FT                   /note="Sensory histidine kinase/phosphatase NtrB"
FT                   /id="PRO_0000074826"
FT   DOMAIN          5..78
FT                   /note="PAS"
FT   DOMAIN          136..348
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   348 AA;  38928 MW;  2ED734E6F34A0B35 CRC64;
     METGNLPDNT LILDSLIHSV LVINQEFIIC YANHAALQVL AQSRRKLFET PFTDLFSYHS
     FDAELMQETL ANGQSFTDNE VILVIHNQSH TMSLSAQPIS EQHILLELAP MDSQRRLSQE
     QIQQAQQIAA RELVRGLAHE IKNPLGGLRG AAQLLAKSLP DPALTEYTQV IIEQADRLRT
     LVDRLLGPQH PGKKTHQSIH HVVERVAQLI SLECPENVTL LKDYDPSLPE LSHYPDQIEQ
     VLLNITRNAL QAVEKTGGTI ILRTRTAFQI TLHGERHRLV ARIDVIDTGS GIPPHLQDTL
     FYPMVSGRED GNGLGLSIAR NLVDQHAGKI EFTSWPGNTE FSIYLPIK