ID   NTRB_AZOBR              Reviewed;         400 AA.
AC   P45670;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 108.
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};
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=7553451; DOI=10.1139/m95-093;
RA   Machado H.B., Yates M.G., Funayama S., Rigo L.U., Steffens M.B.R.,
RA   Souza E.M., Pedrosa F.O.;
RT   "The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-
RT   ntrC operon and are negatively regulated.";
RL   Can. J. Microbiol. 41:674-684(1995).
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; Z37984; CAA86064.1; -; Genomic_DNA.
DR   PIR; I39493; I39493.
DR   RefSeq; WP_035675954.1; NZ_WFKD01000007.1.
DR   AlphaFoldDB; P45670; -.
DR   SMR; P45670; -.
DR   GeneID; 56453394; -.
DR   OrthoDB; 1755994at2; -.
DR   BRENDA; 2.7.13.3; 611.
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.
DR   PROSITE; PS50112; PAS; 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..400
FT                   /note="Sensory histidine kinase/phosphatase NtrB"
FT                   /id="PRO_0000074828"
FT   DOMAIN          29..99
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          163..381
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   400 AA;  43406 MW;  28AC58224489D218 CRC64;
     MARASAAAPL PRRPARPRAP SSSYRPVRPC IDPSVMLNAL PDPVLVVDGS GDIRYVNLEA
     QEFFGLSAAM MEGMPLAELL PPNSPVSQLI EQVQQGRHRA SQEGVVIDTP RIGPHHVTVR
     VTALGEPADH VLLTVNERTL ARKIDNSLTH RNAARSVTAM ASMLGHEVKN PLSGIRGAAQ
     LLEENCSESD RVLTRLICDE ADRIVALVNR MEVFSDQRPL ERDAVNIHTV LEHVRKVAQS
     GFARNIRFIE RYDPSLPPVY GNRDQLIQIF LNLIKNAAEA APESGGEIIL STSYQHGVRM
     ALPGGDTRLH LPLLVSVQDN GDGIPDDLRS NLFDAFITTK VNGTGLGLAL VAKIVGDHGG
     VIEFDSQPRR TVFKVSLPMF DEAQMSGDPA PARGIRGAIG