ID A0A0M9DJH1_9BACI Unreviewed; 344 AA.
AC A0A0M9DJH1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Sensor histidine kinase {ECO:0000256|PIRNR:PIRNR037432};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR037432};
GN ORFNames=ADM90_12200 {ECO:0000313|EMBL:KOY81686.1};
OS Lysinibacillus macroides.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY81686.1, ECO:0000313|Proteomes:UP000037977};
RN [1] {ECO:0000313|EMBL:KOY81686.1, ECO:0000313|Proteomes:UP000037977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 54 {ECO:0000313|EMBL:KOY81686.1,
RC ECO:0000313|Proteomes:UP000037977};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the two-component regulatory system NreB/NreC
CC involved in the control of dissimilatory nitrate/nitrite reduction in
CC response to oxygen. NreB functions as a direct oxygen sensor histidine
CC kinase which is autophosphorylated, in the absence of oxygen, probably
CC at the conserved histidine residue, and transfers its phosphate group
CC probably to a conserved aspartate residue of NreC. NreB/NreC activates
CC the expression of the nitrate (narGHJI) and nitrite (nir) reductase
CC operons, as well as the putative nitrate transporter gene narT.
CC {ECO:0000256|ARBA:ARBA00024827}.
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 ECO:0000256|PIRNR:PIRNR037432};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- PTM: Autophosphorylated. {ECO:0000256|PIRSR:PIRSR037432-51}.
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:KOY81686.1}.
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DR EMBL; LGCI01000008; KOY81686.1; -; Genomic_DNA.
DR RefSeq; WP_053995278.1; NZ_LGCI01000008.1.
DR AlphaFoldDB; A0A0M9DJH1; -.
DR STRING; 33935.ADM90_12200; -.
DR PATRIC; fig|33935.3.peg.3280; -.
DR OrthoDB; 9760839at2; -.
DR Proteomes; UP000037977; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR InterPro; IPR017203; Sig_transdc_His_kinase_NreB.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR PIRSF; PIRSF037432; STHK_NreB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037432};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037432};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR037432-51};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037432};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR037432}.
FT DOMAIN 146..340
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 176..203
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 152
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037432-51"
SQ SEQUENCE 344 AA; 39376 MW; FEF71DF4848D63CE CRC64;
MQSNSENEYL KQIYHHMKDG IILMKENREI IMINPAGQNL TGWHKGGFVP YCSYCTEQAG
THHKPSCYLI ANKDVLGLLS KMPTYRGDKI DVEMSVAAIY VNKETSQTEY MLVLRDHETH
KQVREAAISK KMIRALIEAK EEEHKRLAQE LHDGVGQSLF SVSLALQAIE SFVQQNDKLI
DYIDEVREEL QKVMNDVKSY AYQLRPQSLD QLGLEPTIRY LIDLLQRKVP NLEIQMNTQG
LGRCDPAVEI NLYRIIQEAL HNITKYAQAT LVVIDLIKDN THIYMTIKDN GIGFDRNSIQ
SEGLGLKHIE ERVDQLGGTC KIISNLARGT TIEIVIPRWR PKND
//
