ID A0A431VM12_9PROT Unreviewed; 395 AA.
AC A0A431VM12;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EJ903_02895 {ECO:0000313|EMBL:RTR23498.1};
OS Azospirillum griseum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2496639 {ECO:0000313|EMBL:RTR23498.1, ECO:0000313|Proteomes:UP000277007};
RN [1] {ECO:0000313|EMBL:RTR23498.1, ECO:0000313|Proteomes:UP000277007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-25-5w-1 {ECO:0000313|EMBL:RTR23498.1,
RC ECO:0000313|Proteomes:UP000277007};
RA Yang Y.;
RL Submitted (DEC-2018) 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:RTR23498.1}.
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DR EMBL; RXMA01000002; RTR23498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A431VM12; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000277007; 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:UP000277007}.
FT DOMAIN 159..377
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 43160 MW; 59715600F48FBA8B CRC64;
MDPLPTDDPP PRGRSRSRSS AARPTSIDPS VVLNALPDPV LVIDGANEIR FVNLEAQEFF
DLSFNSMAGM ALTELLPPDS PVLGLIAQVR RGSRRVSQEG VVIDTPRIGP HHVTVQVATM
GEPSDHLLLT VHERSIARKI DNSLTHRHAA RSVTAMAAML AHEVKNPLSG IRGAAQLLEE
NAHEQDRVLT RLICDEADRI VALVNRMEVF SDERPLERAD VNIHTVLEHV RTIAQSGFAR
KIRFIERYDP SLPPVYGNRD QLVQVFLNLI KNAAEAAPET GGEITLSTSY QQGVRMALPG
GDTRLHLPLL VSVQDNGDGI PEDLRSNLFD PFVTSKVNGT GLGLALVAKL IGDHGGTIEF
DSQPRRTVFK VSLPMYDDSQ MSQGVSMVRG GRGSR
//
