ID A0A1G1A9D2_9BACT Unreviewed; 1074 AA.
AC A0A1G1A9D2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=A2498_10735 {ECO:0000313|EMBL:OGV67051.1};
OS Lentisphaerae bacterium RIFOXYC12_FULL_60_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798582 {ECO:0000313|EMBL:OGV67051.1, ECO:0000313|Proteomes:UP000178496};
RN [1] {ECO:0000313|EMBL:OGV67051.1, ECO:0000313|Proteomes:UP000178496}
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:OGV67051.1}.
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DR EMBL; MHBQ01000030; OGV67051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1A9D2; -.
DR STRING; 1798582.A2498_10735; -.
DR Proteomes; UP000178496; 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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 5..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 220..271
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 454..514
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 601..660
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 716..764
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 793..845
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 975..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1047..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..733
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 836..863
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1074 AA; 118272 MW; 0502AD3ED12831F8 CRC64;
MDVMRILAVE DNPADFRLLK EHLGEDPAVP FEVVGVQTIR EALDLLPAGD FAAVLLDLNL
PDSTGLAGLD RIVAGAPALP VIVLTGLKDI AMGLQALSRN AQDYLVKDRI DGDTLVRSIR
YAIERGKARE TAHRQNVELE KRAATIEHAR QEWERTFDAV PDLIAILDER HQVLRVNRAM
ARKLGREPDA CRGATCYEVV HGCRAAIETC PHARTMKDGK EHSAEVHEDR LGGDFHITTT
PVMDADGRMV GAVHVARDIT KSKQREADLR RLNRVLNALG HSGQALMRAT GEADFLAEAC
RIIVEDCGHA MVWIGFAEHD EAKTIRPAAS AGFEEGYLDA LKLTWADTER GRGPTGMAIR
TGQVTRCLDI PSDPAFLPWR QDAIKRGYAS SIALPLLADG KALGALCIYS RDPVGFGDDE
VKLLTDLAAD FAQNIVSFRT RAARDRAEQA VRESEERYRS LFNTMAEGFA QHAVICDSEG
KPCDYRFLDI NPAFERLTGL KREQVVGKTV LEIMPETEPV WIERFGRVGL TGEPDHFSHV
SAVIGRHFEV AAYQTAPGRF AVIFTDVTEL KAFQERDKAN AVRLAWGQAA IDTISVMYEG
VALLEDDGTI LSVNPAVERL TGLAGDSLGG RNVEILLPEL LTGSDLATAQ QGLETLRSGE
MPKMTTLTIQ RRGGGFSHVL PSLVRMAVPD GVRPVVVLTL WDVTELHEAA AQLKQSERKY
RELVENANSI IMRILPDHTI TFFNEYAQTF FGFEAGDVVG RNVLGTIAAE VDSEGRDMRA
MLQAIMMHPE QHGSNESENV CKDGRRVWVH WANRAVRDDQ GQVVEILCVG TDITRRRAME
AETRVYQQRL RELAKRLATA EEADRWRISR YIHDTIIQNL SLSIIRLGSI AKPLADARRG
DEVVKLGQIR GLIEQSIGEC RMVMSDLTPA LLYELGLIPA LNDLAQQLET KHRARLVVKG
DGHEPFLSPA LRGLLFQSVR ELVMNALKHA GPCEISVTVS QRENDLVVQV ADDGAGFDPS
RAGASRDRKG GFGLFSIRQR LEGLGGRLEI DSTPGKGTTA TIDVPVGERG EAEG
//
