ID   A1RC89_PAEAT            Unreviewed;       426 AA.
AC   A1RC89;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 133.
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   OrderedLocusNames=AAur_4185 {ECO:0000313|EMBL:ABM07058.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM07058.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM07058.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM07058.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA   Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00107}.
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DR   EMBL; CP000474; ABM07058.1; -; Genomic_DNA.
DR   RefSeq; WP_011776774.1; NC_008711.1.
DR   AlphaFoldDB; A1RC89; -.
DR   STRING; 290340.AAur_4185; -.
DR   KEGG; aau:AAur_4185; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_15_11; -.
DR   OrthoDB; 144293at2; -.
DR   Proteomes; UP000000637; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR050482; Sensor_HK_TwoCompSys.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR017205; Sig_transdc_His_kinase_ChrS.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF62; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   PIRSF; PIRSF037434; STHK_ChrS; 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   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|PROSITE-
KW   ProRule:PRU00107}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00107}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..421
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   426 AA;  45232 MW;  239B92ACFBE5CA27 CRC64;
     MQSPAGAATI LRVLRVSLHV GFAVLLLVAI VRLLTGVGTA GTPSPVALTA GLGLSALLAA
     VYLAGTVLEK RHSSDPSRFN PSKYARWWLA AVMLLWLLLL LVSSDFAWVA FPLFFLQLHL
     LPRGLALPAI AVSTALLVGT LWFHSRGSSD GGLQLSMILG PVFGAVFAVV TGLAYRALFL
     EAENQRTVAD ELRRTRAELA RTQHDAGMLA ERERLAREIH DTLAQGFSSI VLMGRSAEKA
     LESSDVETAR ESLKIVQDTA SANLAEARSF VRGLRSPDLE QSGLVDTLRR LCEKTETEAA
     ARGSALRCRF ELVGAPVELP NTYQTTLLRA AQASLANVWA HAHARAAVVT LSFLGAEVTL
     DVFDDGIGFE PSTAAGTARG DGTGVGLQSL RERLAALDGS LEIESAPGEG TVVAVRMPLP
     VDEGAV
//