ID   NREB_STAAM              Reviewed;         344 AA.
AC   Q931F6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Oxygen sensor histidine kinase NreB;
DE            EC=2.7.13.3;
DE   AltName: Full=Nitrogen regulation protein B;
GN   Name=nreB; OrderedLocusNames=SAV2392;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR   EMBL; BA000017; BAB58554.1; -; Genomic_DNA.
DR   RefSeq; WP_000606545.1; NC_002758.2.
DR   AlphaFoldDB; Q931F6; -.
DR   SMR; Q931F6; -.
DR   PaxDb; Q931F6; -.
DR   EnsemblBacteria; BAB58554; BAB58554; SAV2392.
DR   KEGG; sav:SAV2392; -.
DR   HOGENOM; CLU_000445_114_0_9; -.
DR   OMA; CEGYSNE; -.
DR   PhylomeDB; Q931F6; -.
DR   BioCyc; SAUR158878:SAV_RS13025-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of 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:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
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; IPR017203; Sig_transdc_His_kinase_NreB.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   PIRSF; PIRSF037432; STHK_NreB; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..344
FT                   /note="Oxygen sensor histidine kinase NreB"
FT                   /id="PRO_0000349331"
FT   DOMAIN          152..344
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         61
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         158
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   344 AA;  39101 MW;  D51BA10149F3D90C CRC64;
     MINEDSIQLD TLLKKYYEHS IEKIVFADDN GKIIAMNDAA KDILSEEDNY SAVANAICHR
     CEGYTNAYDV QSCKDCFLES MQVQATNFQV FMKTKDQKVM PFTATYQLID QDRGIHAFTL
     QNVSSQIEQQ EKLHQQHMMR KTISAQENER KRISRELHDS VIQEMLNVDV QLRLLKYQED
     TTKLLEDAEN IEYIVAKLID DIRNMSVELR PASLDDLGLE AAFKSYFKQF EENYGIKIIY
     TSNIKNTRFD SDIETVVYRV VQEAILNALK YADVNEINVG IRQTGRHLVA EVIDAGNGFD
     PSSKPKGSGL GLYGMNERAE LVSGSVNIET KIGEGTNVTL NIPI