ID   NREB_STAEQ              Reviewed;         344 AA.
AC   Q5HLK5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=SERP1982;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW52895.1; -; Genomic_DNA.
DR   RefSeq; WP_010959271.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLK5; -.
DR   SMR; Q5HLK5; -.
DR   STRING; 176279.SERP1982; -.
DR   EnsemblBacteria; AAW52895; AAW52895; SERP1982.
DR   KEGG; ser:SERP1982; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_114_0_9; -.
DR   OMA; CEGYSNE; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..344
FT                   /note="Oxygen sensor histidine kinase NreB"
FT                   /id="PRO_0000349340"
FT   DOMAIN          147..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;  39871 MW;  2A18019C5C5716B3 CRC64;
     MLEQTDLSLE QLLKNYYETT NEKIVFVNRQ GKIIAMNDAA KDILTEEDNY NAMTNAICHR
     CEGYSNEYDV QSCKDCFLET TQLQHSNFQV FMKTKDNEIK PFTAMYQNID EQRGISAFTL
     QNVAPQIERQ EKMYQQKMLH RSIQAQENER KRISRELHDS VIQDMLNIDV ELRLLKYKHR
     DKVLAETSQR IEGLLSQLID DIRNMSVELR PSSLDDLGIE AAFKSYFKQF EENYGMHIKY
     DSNIKGMRFD NEIETVVYRV VQEGVFNALK YAEVNEIEVS THSDGKQIVA EVVDRGKGFS
     LDHHPKGSGL GLYGMRERAE LVNGHVNIET HINRGTIITL DIPI