ID A0A1G0QLW0_9BACT Unreviewed; 1051 AA.
AC A0A1G0QLW0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=A2080_03415 {ECO:0000313|EMBL:OGU48871.1};
OS Ignavibacteria bacterium GWC2_36_12.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798427 {ECO:0000313|EMBL:OGU48871.1, ECO:0000313|Proteomes:UP000178676};
RN [1] {ECO:0000313|EMBL:OGU48871.1, ECO:0000313|Proteomes:UP000178676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGU48871.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGZZ01000167; OGU48871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0QLW0; -.
DR STRING; 1798427.A2080_03415; -.
DR Proteomes; UP000178676; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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 Pfam; PF07494; Reg_prop; 8.
DR Pfam; PF07495; Y_Y_Y; 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; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 859..1051
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 833..860
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1051 AA; 118734 MW; 164A730DEC7D5004 CRC64;
MSLINRAFHQ VVHQLLIATL LYLIYFLVIP QELSAQTPGL SGINVVVNRI STEQGLSNSE
VNAITQDKQG FIWIGTAYGL NRFDGENFTV FVNDPNDLTS LSDSFIWSLY VDREGTLWVG
TQYGLNKFNP ATRTFKRYFH NPENPQSLSS NEIRSFYEDR AGVFWVGTAR GLNRFDRTTE
TWTFFLPTPN DSTRPGDNFV NAILEDRQGN FWIGTGNFLM NGGGLHKFDR SSGTFKHFWY
NPSDQKSLSD NWVTSILEDQ SGTIWVTSDA GDVNKFDKVF GNFTRLKLPV AESTNLNSGT
LSIKCIREDN LGALWIATWG WGLFRYEKRT ETFMQYTFDA ANPGSLSNPA VNMLYIDKAG
LLWAGTSRGG VSTVATKPFL HRHTLGNSLR IGSRVDDLFT DSQGSFWIGA VGIGLLRFDI
LTRRFTNVLP DGTGIKMYED ATEIIWISTL DEVTKYNIKT GTSAVVWSIP SPHGSQEWIS
SILPDKEGFL WVGTNGGSLY RIGRNLKEYS VFTHDTQNPK SITAGPINSM LQDQTGIIWI
GTTEGLSRFN KDTQSFSRFT HDERDSTSLS SNYWCSLLED RSGDLWVGTS DGLNRFNEES
LNFTRFYTAD QRHGRFVNLM LEDNKGRFWY GGGSNIFMFD PAAGSFRSFD ESDGLEHVDV
LGWSLIKLKS GELVFGTANG ILVFNPESVK VSSYVPPIVI TGLKKLNQTI NLATLPELMS
EITFEHEDNV FSIEYAALSY DMPAFNQYAY KLEGFDKDWV YCGNRREATY TNLDPGVYTF
FVKGSNHDGV WNEQGTSITI IISPPWWKTW WFTIFFWVSV AGSIGGTLRY VEKRKLQKKI
ERLERERALE KERVRISQDM HDEVGSSLSE ISILSELLKR DMSKSEEAEI HLRDISDRSA
EVIENIGQII WAINPRNDPL DNLVAHLRLY TADYIRKAGI KYSFKIPDNI PAYHLSAEVR
RNVFLVVKEA LHNIVKHSCA TEVQVRVDFL QNQMIISVKD NGEGFSINQK PGSGNGLINM
QKRIENIGGT FKIESEPGQG TGITITVNFI V
//
