ID A0A246FUV7_9PSED Unreviewed; 361 AA.
AC A0A246FUV7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000256|ARBA:ARBA00039567};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000256|ARBA:ARBA00042313};
DE AltName: Full=Nitrogen regulator II {ECO:0000256|ARBA:ARBA00043094};
GN ORFNames=CEC48_23290 {ECO:0000313|EMBL:OWP69367.1};
OS Pseudomonas sp. K2I15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2013577 {ECO:0000313|EMBL:OWP69367.1, ECO:0000313|Proteomes:UP000197956};
RN [1] {ECO:0000313|EMBL:OWP69367.1, ECO:0000313|Proteomes:UP000197956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2I15 {ECO:0000313|EMBL:OWP69367.1,
RC ECO:0000313|Proteomes:UP000197956};
RA Orellana P., Castillo D., Corsini G.;
RT "Draft genome sequence of the Chilean Antartic Pseudomonas sp. strain
RT K2I15.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00037696}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWP69367.1}.
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DR EMBL; NIXO01000047; OWP69367.1; -; Genomic_DNA.
DR RefSeq; WP_003218001.1; NZ_NIXO01000047.1.
DR AlphaFoldDB; A0A246FUV7; -.
DR GeneID; 56074728; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000197956; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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 DNA-templated transcription; IEA:InterPro.
DR CDD; cd16918; HATPase_Glnl-NtrB-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 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 PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF16; SENSORY HISTIDINE KINASE_PHOSPHATASE NTRB; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:OWP69367.1};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:OWP69367.1}.
FT DOMAIN 139..356
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 361 AA; 40055 MW; 08C104B94A5F85A3 CRC64;
MTISDALHRL LLDNLTTATI LLNDELRLEY MNPAAEMLLA ISGQRSHGQF ISELFTESAE
ALSSLRQAVE QAHPFTKREA MLTALTGQTL TVDYAVTPIL SHGATLLLLE VHPRDRLLRI
TKEEAQLSKQ ETSKMLVRGL AHEIKNPLGG IRGAAQLLAR ELPDENLKDY TNVIIEEADR
LRNLVDRMLG SNKLPSLAMT NVHEVLERVC QLVEAESQGC ITLVRDYDPS IPDVLIDREQ
MIQAVLNIVR NAMQAISSQN ELRLGRISLR TRALRQFTIG HVRHRLVTKV EIIDNGPGIP
AELQETIFFP MVSGRPDGTG LGLAITQNII SQHQGLIECE SHPGHTTFSI FLPLEQGAPS
T
//
