ID Q2C2M9_9GAMM Unreviewed; 350 AA.
AC Q2C2M9;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=SKA34_00640 {ECO:0000313|EMBL:EAR55311.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR55311.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR55311.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR55311.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR55311.1}.
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DR EMBL; AAOU01000019; EAR55311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2C2M9; -.
DR HOGENOM; CLU_000445_114_39_6; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000005284; 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; 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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 2..46
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 136..350
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 350 AA; 39024 MW; 9FF266A4FDB3409E CRC64;
MTTAFTPIII DNLVTAIILL DEHLTIRYVN PAAEQLLSSS KRRLLGITLP ELLQYSSLDL
DLIAATLYSG QGLADSDLAF VIDEQRHLLA LNASPISWQK ELFVMLELKP IDQQRRISQE
LSQLAQQQAA KELVRGLAHE IKNPLGGLRG AAQLLEKALP DPSYVEYTQM IIEQADRLRN
LVDRLLGPQR PGIRKTDNIH LILEKVRQLI ILENDSNLVI ERDYDPSLPE IDMDTEQLEQ
ALLNIVSNAA HVLKKQQNGG IIKLKTRTAH QALIQGKYTR IAAKIEIIDN GPGIPAEIQD
TLFYPMVTGN ADGTGLGLSI SQNLIDQHNG KIEVISWPGH TNFTIYLPIQ
//
