NREB_STAES
ID NREB_STAES Reviewed; 344 AA.
AC Q8CR97;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SE_1970;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05611.1; -; Genomic_DNA.
DR RefSeq; NP_765525.1; NC_004461.1.
DR RefSeq; WP_002456059.1; NZ_WBME01000017.1.
DR AlphaFoldDB; Q8CR97; -.
DR SMR; Q8CR97; -.
DR STRING; 176280.SE_1970; -.
DR EnsemblBacteria; AAO05611; AAO05611; SE_1970.
DR GeneID; 50017936; -.
DR KEGG; sep:SE_1970; -.
DR PATRIC; fig|176280.10.peg.1923; -.
DR eggNOG; COG4585; Bacteria.
DR HOGENOM; CLU_000445_114_0_9; -.
DR OMA; CEGYSNE; -.
DR Proteomes; UP000001411; 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_0000349339"
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; 2F1D0199595716B3 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 THSDGKQLVA EVVDRGKGFS
LDHHPKGSGL GLYGMRERAE LVNGHVNIET HINRGTIITL DIPI
