ID   NTRB_VIBAL              Reviewed;         350 AA.
AC   P19906;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 111.
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   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2574025; DOI=10.1007/bf00425484;
RA   Maharaj R., Rumbak E., Jones W.A., Robb S.M., Robb F.T., Woods D.R.;
RT   "Nucleotide sequence of the Vibrio alginolyticus glnA region.";
RL   Arch. Microbiol. 152:542-549(1989).
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; L08499; AAA27524.1; ALT_TERM; Genomic_DNA.
DR   PIR; JL0114; JL0114.
DR   AlphaFoldDB; P19906; -.
DR   SMR; P19906; -.
DR   STRING; 663.BAU10_15720; -.
DR   eggNOG; COG3852; Bacteria.
DR   BRENDA; 2.7.13.3; 6624.
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: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   TIGRFAMs; TIGR00229; sensory_box; 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..350
FT                   /note="Sensory histidine kinase/phosphatase NtrB"
FT                   /id="PRO_0000074827"
FT   DOMAIN          4..67
FT                   /note="PAS"
FT   DOMAIN          136..350
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         330
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   350 AA;  39002 MW;  7386B4D689601D13 CRC64;
     MDTSLPSAIL NNMVTATLIL DDGLAIRYAN PAAELLFSQS AKRIVEQSLS QLIQHASLDL
     ALLTQPLQSG QSITDSDVTF VVDGRPLMLE VTVSPITWQK QLMLLVEMRK IDQQRRLSQE
     LNQHAQQQAA KLLVRGLAHE IKNPLGGLRG AAQLLEKMLP DPSLTEYTHI IIEQADRLRA
     LVDRLLGPQK PGKKTQENLH QILEKVRQLV ELESQRSIVI ERDYDPSLPE ILMDADQIEQ
     AMLNIVSNAA QILSHQEHGK ITIRTRTVHQ ANIHGKRCKL AARVEITDNG PGIPPELQDT
     LFYPMVSGRE GGTGLGLSIS QNLIDQHNGK IDVESWPGHT TFTIYLPILR