NREB_STACT
ID NREB_STACT Reviewed; 347 AA.
AC Q7WZY5; B9DL90;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=Sca_1889;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INHIBITION BY ADP,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF CYS-62.
RX PubMed=12426351; DOI=10.1128/jb.184.23.6624-6634.2002;
RA Fedtke I., Kamps A., Krismer B., Goetz F.;
RT "The nitrate reductase and nitrite reductase operons and the narT gene of
RT Staphylococcus carnosus are positively controlled by the novel two-
RT component system NreBC.";
RL J. Bacteriol. 184:6624-6634(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
RN [3]
RP FUNCTION AS AN OXYGEN SENSOR, ACTIVITY REGULATION, AUTOPHOSPHORYLATION,
RP IRON-SULFUR CLUSTER, AND MUTAGENESIS OF CYS-62.
RX PubMed=15101978; DOI=10.1111/j.1365-2958.2004.04024.x;
RA Kamps A., Achebach S., Fedtke I., Unden G., Goetz F.;
RT "Staphylococcal NreB: an O(2)-sensing histidine protein kinase with an
RT O(2)-labile iron-sulphur cluster of the FNR type.";
RL Mol. Microbiol. 52:713-723(2004).
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:0000269|PubMed:12426351, ECO:0000269|PubMed:15101978}.
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 -!- ACTIVITY REGULATION: Activated by cysteine desulfurase, Fe(2+) ions and
CC cysteine and inhibited by oxygen and ADP.
CC {ECO:0000269|PubMed:15101978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: NreB may sense the oxygen concentration directly via the
CC disassembly and reassembly of the FNR-type 4Fe-4S cluster. The iron-
CC sulfur cluster controls the functional state of the kinase domain.
CC Under oxic conditions, the iron-sulfur cluster is destroyed and the
CC autophosphorylation activity of NreB is decreased. However, under
CC anoxic conditions and in the presence of iron ions, the iron-sulfur
CC cluster is formed and NreB is autophosphorylated (Probable).
CC {ECO:0000305}.
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DR EMBL; AF029224; AAP79639.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL28795.1; -; Genomic_DNA.
DR RefSeq; WP_015901131.1; NC_012121.1.
DR AlphaFoldDB; Q7WZY5; -.
DR SMR; Q7WZY5; -.
DR STRING; 396513.SCA_1889; -.
DR GeneID; 60544397; -.
DR KEGG; sca:SCA_1889; -.
DR eggNOG; COG4585; Bacteria.
DR HOGENOM; CLU_000445_114_0_9; -.
DR OMA; CEGYSNE; -.
DR OrthoDB; 1755994at2; -.
DR BioCyc; SCAR396513:SCA_RS09585-MON; -.
DR Proteomes; UP000000444; 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 1: Evidence at protein level;
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..347
FT /note="Oxygen sensor histidine kinase NreB"
FT /id="PRO_0000349338"
FT DOMAIN 153..347
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 159
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 62
FT /note="C->S: Impaired in nitrate and nitrite reduction and
FT also exhibits a growth defect. Inhibits incorporation of
FT the iron-sulfur cluster."
FT /evidence="ECO:0000269|PubMed:12426351,
FT ECO:0000269|PubMed:15101978"
SQ SEQUENCE 347 AA; 39953 MW; 197FC822E3B5AB58 CRC64;
MKSISNRDKL QDLLTQYYLN TNEKMVFLNS TGEVIALNEA AEEVFADDND YSQMTNAVCR
RCEGYSNEYD IMSCENCFLE ALEIGKGSFQ VFIRTKDNKI QPYTASYELI DHEKGIYAFT
LHNVSPQIQR QERMYQRKMM QKTISAQENE RKRISRELHD GIVQELINVD VELRLLKYQQ
DKDELIDNSK RIEGIMSRLI DDVRNLSVEL RPSSLDDLGL DAAFRSYFKQ FEKNYGIHVN
YHTNFSAQRF DNEIETVVYR VVQEALFNAL KYAQVDIVEV SLQLNENNII AEVSDRGVGF
KRGDDPKGTG LGLFGMNERA ELVNGTVNID SQINRGTIVT LEVPITD
