ID A0A086XYY2_9RHOB Unreviewed; 356 AA.
AC A0A086XYY2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CG50_00355 {ECO:0000313|EMBL:KFI27232.1};
OS Paenirhodobacter enshiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paenirhodobacter.
OX NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI27232.1, ECO:0000313|Proteomes:UP000028824};
RN [1] {ECO:0000313|EMBL:KFI27232.1, ECO:0000313|Proteomes:UP000028824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW2-9 {ECO:0000313|EMBL:KFI27232.1,
RC ECO:0000313|Proteomes:UP000028824};
RA Wang D., Wang G.;
RT "Genome of Paenirhodobacter enshiensis DW2-9.";
RL Submitted (MAR-2014) 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:KFI27232.1}.
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DR EMBL; JFZB01000010; KFI27232.1; -; Genomic_DNA.
DR RefSeq; WP_036636838.1; NZ_JFZB01000010.1.
DR AlphaFoldDB; A0A086XYY2; -.
DR STRING; 1105367.CG50_00355; -.
DR eggNOG; COG3852; Bacteria.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000028824; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028824}.
FT DOMAIN 136..353
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 356 AA; 38495 MW; AF6DA72805E2896F CRC64;
MSLPAPGTIW NSLPIPALLI DGDERVIEIN PAAEYFLNLS SKMLKGQSVM ERLAIAAPLE
EIFARVRKNR AATFVNDVDV TTGERAPIQC NIQAAPLGEE PDTVLLLINP REIADRLGRA
SMVKSAARSA IGMAEMLAHE IKNPLAGIAG AAQLLSMNLS GEDLELTDLI VDETRRIVKL
LEQVEQFGNV RPPEKKPVNI HDVLDRARKS ATVGFGSHMT ILEDFDPSLP STLGDADQLT
QVFLNLLKNA AEAAKGRPGT IRIHTFYDYA LRLRRADGKG QALPLQIEII DDGPGIPPDI
AGSLFEPFVS GRENGTGLGL ALVSKIISEH DGWISVDSVP GRTVFRISLP VAPKES
//
