ID A0A1M4M5X7_9FIRM Unreviewed; 388 AA.
AC A0A1M4M5X7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Oxygen sensor histidine kinase NreB {ECO:0000256|ARBA:ARBA00017322};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Nitrogen regulation protein B {ECO:0000256|ARBA:ARBA00030800};
GN Name=degS {ECO:0000313|EMBL:SCG83116.1};
GN ORFNames=DW1_1545 {ECO:0000313|EMBL:SCG83116.1};
OS Proteiniborus sp. DW1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG83116.1, ECO:0000313|Proteomes:UP000185208};
RN [1] {ECO:0000313|EMBL:SCG83116.1, ECO:0000313|Proteomes:UP000185208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW1 {ECO:0000313|EMBL:SCG83116.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; FMDO01000030; SCG83116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M4M5X7; -.
DR STRING; 1889883.DW1_1545; -.
DR Proteomes; UP000185208; 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: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 InterPro; IPR008595; DegS.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR InterPro; IPR016381; Sig_transdc_His_kinase_DegS.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF55; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE DEGS; 1.
DR Pfam; PF05384; DegS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR PIRSF; PIRSF003169; STHK_DegS; 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; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:0000313|EMBL:SCG83116.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000185208};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCG83116.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 200..382
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 26..81
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 388 AA; 44718 MW; 57D7ABB03DC1FD57 CRC64;
MSKSKLDLKK MNEIIEKTIV TIESGRQEIF EIAEDARKEC ERIKQELTSI NHKVSLTILE
VDELKREEKR AKIRLMMVSK DFNQYSEEDI RLAYEEANNI RIKHLLKKRE EKDLIVRRTD
LELNFKRTNE ILKRAEKLVA HVGVAMDFLK GNLNDIYETI GDMSKKQLLG IKIIEAQEEE
RMRVSREIHD GPAQSMANVV LKAELCEKLL SIDINQSRTE LQKLKDIVRT SLKDIRKIIY
DLRPMSLDDL GLVPTIQRYI DRYIEETGIN VELMVLNKQP DIDSVIEIAC FRIIQEALNN
ILKHSKAQDV LIKIDQTHDK LYIVVKDNGI GFDMNGRKFK SGESGFGLIG MKERAELLNG
KLDIVSTLGA GTKIALTIPL ERKDGLYE
//
