ID A0A433X4S4_9BACL Unreviewed; 359 AA.
AC A0A433X4S4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Sensor histidine kinase {ECO:0000256|PIRNR:PIRNR037431};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR037431};
GN ORFNames=EJP77_15090 {ECO:0000313|EMBL:RUT29052.1};
OS Paenibacillus zeisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496267 {ECO:0000313|EMBL:RUT29052.1, ECO:0000313|Proteomes:UP000272464};
RN [1] {ECO:0000313|EMBL:RUT29052.1, ECO:0000313|Proteomes:UP000272464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-5-3 {ECO:0000313|EMBL:RUT29052.1,
RC ECO:0000313|Proteomes:UP000272464};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) 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:PIRNR037431};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037431};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR037431}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:RUT29052.1}.
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DR EMBL; RZNX01000007; RUT29052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433X4S4; -.
DR OrthoDB; 9795828at2; -.
DR Proteomes; UP000272464; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
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 InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR017202; LiaS/VraS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
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; PIRSF037431; STHK_LiaS; 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 PROSITE; PS50885; HAMP; 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:PIRNR037431};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR037431}; 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:PIRNR037431};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037431};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037431};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000272464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037431};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR037431}.
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..123
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 150..344
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 359 AA; 40476 MW; 3F53CEE1D9CB3718 CRC64;
MRRKKPVNMI SRSMRDGILL SFFLCGAILY LLNTYGYLSP TSSWTKVIQA SLTGGLLLVG
TGAAYGLYQI YSVKRRMDLL RDSLLQWEKG NLSRSVPELG EDEIGRLGEQ LERIGKRWEE
QVNSLQRLST HNAQLAEQAR ISAIVEERQR LARELHDAVS QQLFAISMTA TAVGRTLEKD
FDKAQRQVEL IEEMSSVAQS EMRALLLHLR PVYLEGKALS EGVAELVREL KSKVPMDITL
EMDPDIKLVK GIENHLFRII QEALSNTLRH SKADKMEIRI HQRPEAVKVI LRDNGIGFQM
DEKKQTSYGL STMQERIHEI GGSIQFITSP GAGTRIEITV PLMIEEGGWN ENDGDGDSN
//
