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Database: UniProt
Entry: A0A1A9F5J8_9GAMM
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ID   A0A1A9F5J8_9GAMM        Unreviewed;       449 AA.
AC   A0A1A9F5J8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=A8C75_06625 {ECO:0000313|EMBL:ANG65131.1};
OS   Marinobacterium aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG65131.1, ECO:0000313|Proteomes:UP000078070};
RN   [1] {ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA   Baek K., Yang S.-J.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANG65131.1, ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|EMBL:ANG65131.1,
RC   ECO:0000313|Proteomes:UP000078070};
RX   PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA   Bae S.S., Jung J., Chung D., Baek K.;
RT   "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT   isolated from estuary sediment.";
RL   Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP015839; ANG65131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9F5J8; -.
DR   STRING; 1821621.A8C75_06625; -.
DR   KEGG; mars:A8C75_06625; -.
DR   OrthoDB; 9797605at2; -.
DR   Proteomes; UP000078070; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR033480; sCache_2.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR017171; Sig_transdc_His_kinase_MctS.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF59; NITROGEN REGULATION PROTEIN B; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   PIRSF; PIRSF037314; STHK_MctS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01049; Cache_2; 1.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:0000313|EMBL:ANG65131.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078070};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        203..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..449
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   449 AA;  50017 MW;  5185DE2EC6A49C14 CRC64;
     MSLKAKLLLL AILPLLLVSS LVTMVSLQQA RNLSEQEIRI FEDNLLSTKQ RELQNYVSLA
     LTSIDHIVAN ADVHDEAAKI EVMRILSDLT FGDDGYFFVY DRNGKVLVHP ILTDLVGQDL
     YDMQDARGDY VIRSLLQRAR EGGGFHRYLW QKPSRGESEE KLGYVVSLPK WGWMLGTGLY
     IDDITEEVAK IRSEVTRNIR NTFFTVLLIV AAAVAVIIVI GIALNLHESR LADGRLRSLA
     HKSIQLQVSQ RRGFARELHD GINQLMVSVK FRIESALNKL SKAGDSASAT ADLHHAMAVL
     NEAIQEVRRV SHNLRPSILD DLGLEPALRN LLDEFKLRTG ILVDLRLSLP AARLNDDIET
     TLYRVVQEAL TNIEKHADAS HLLVRSWYSS GLLWLELKDN GCGFDPDDLS PQAGIGLRNI
     RDRLELLGGE LALESAPGEG ARLCIGLPA
//
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