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Database: UniProt
Entry: A0A0C5WT17_9GAMM
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ID   A0A0C5WT17_9GAMM        Unreviewed;       508 AA.
AC   A0A0C5WT17;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=H744_2c1506 {ECO:0000313|EMBL:AJR08184.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR08184.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR08184.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR08184.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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; CP005974; AJR08184.1; -; Genomic_DNA.
DR   RefSeq; WP_044622971.1; NZ_CP005974.1.
DR   AlphaFoldDB; A0A0C5WT17; -.
DR   STRING; 658445.H744_2c1506; -.
DR   KEGG; pgb:H744_2c1506; -.
DR   PATRIC; fig|658445.3.peg.3421; -.
DR   HOGENOM; CLU_041023_0_0_6; -.
DR   OrthoDB; 9797605at2; -.
DR   Proteomes; UP000032303; Chromosome 2.
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   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR007895; MASE1.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF05231; MASE1; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:AJR08184.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032303};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          310..508
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   508 AA;  55804 MW;  B90EEC0BCC003658 CRC64;
     MRNFALTTLG GWLLIACAWF CLWAIASYFT LDPELAVFLF PFALRMGIAL HCPKKYWGAV
     YGAEWGLMLA LAPQVGNPLW EAALCASVAS VPLLWGAHGQ YYGSQLRRLC VMGTVIGLTA
     LLNVAISGWF SEHSWMVLLV SITGGLMLVP SCYLIWSYLF QQAWIPLTVD LVSRPVALRV
     RHIFFYAGLF IASIALQLGL PDEMRRFAPF CLAIPIILLA FRYGWQGALL GTLLNSVALI
     AARSTGSDLE VTDLLLSLSA QSLTGILLGM GIQRQRELNQ QLRLQLDRNH SLSRQLVKAE
     ESVRRDVARE LHDEIGQNIT AIRTQASIIQ RVETTPVGAG CAGMIENLSL NIYDTTKGLL
     SRLRPKSLDD MGLADSLEQL IRDLECEALG INAVITWHCN GSDPDTLSDT LSVTLYRLCQ
     EAMNNVVKYA NASQLELTFV LCDDTVDLTV RDNGRGFSVD QVMQMSSSGF GLQGMRERVE
     ALGGTIQIES QIAGANQGTG ITIQMPLL
//
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