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Database: UniProt
Entry: A0A1H1X3D3_9PSED
LinkDB: A0A1H1X3D3_9PSED
Original site: A0A1H1X3D3_9PSED 
ID   A0A1H1X3D3_9PSED        Unreviewed;       805 AA.
AC   A0A1H1X3D3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=SAMN05216221_3275 {ECO:0000313|EMBL:SDT03126.1};
OS   Pseudomonas oryzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1392877 {ECO:0000313|EMBL:SDT03126.1, ECO:0000313|Proteomes:UP000243359};
RN   [1] {ECO:0000313|Proteomes:UP000243359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32247 {ECO:0000313|Proteomes:UP000243359};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; LT629751; SDT03126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1X3D3; -.
DR   STRING; 1392877.SAMN05216221_3275; -.
DR   OrthoDB; 9797605at2; -.
DR   Proteomes; UP000243359; Chromosome i.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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; cd00130; PAS; 2.
DR   CDD; cd01007; PBP2_BvgS_HisK_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; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:SDT03126.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243359};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..805
FT                   /note="Oxygen sensor histidine kinase NreB"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009265117"
FT   TRANSMEM        278..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          335..372
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          401..451
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          452..529
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          532..583
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          605..799
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   805 AA;  89784 MW;  95EDCC9456954CB0 CRC64;
     MSVRPSPLRH LIALILLGLA LLAGRSAAAE GVVADAGQWQ TGPAPLQVGV VLQAPYAELD
     RRQRQDLLVG AHVELMEALA EQLGVGLRWH TFADQDALET AVRHGEIELA PGLQQTPSGL
     RLWRYSDPYL RIPHLIVGER SSAAAVRLDR LSRQQPVAVR DDSPVQRFLR SSHSGLEVLS
     ASSERQALRL VLAGEASYAV IDEAQYARLL GEAEFAPLQV LGDVGYPLLL RVAVRRDLDA
     LAARIDQGLR ALPEERLEQL QRRWLQPPVA GLGETAGFWR SLALLLGLLL AALLVATWWL
     RRESSELEQR LAAARHDLWL RESAEQALRL TQFSIDHSTV GILWVNWDSH VRYANHAAEQ
     LLGYRPGELV ERPLRELEPQ LDMDRWLALW KNARAADEVA LGFETRCRRA DGSWLPTDVS
     ISFLRFRDTE YLLVYLTDVT ERRRARAALE ESEARLKGIA GNVPGLLFRL ERAAPGAEVH
     ISFIGEGSAG LVGYPAATLL EPERGIRSLV HPDDRDGYWS SQQAALAADD DWHWQGRLLT
     RDGTPIWVDI KATARRLEAG RVVWDGMVWD ISEIKHTELA LAESRAQLRE LAAHMESVRE
     EEKARIAREV HDELGQMLTV LKLEISMCQL AHGEQDAELR ERLQNMSKLI AQLFQQVRDV
     ATALRPPILD AGIASAIEWQ ARRFEARTQI PCLVEVPEQL PPLGEAKATG LFRVLQEALT
     NIMRHARAHS VEVRLSREAD ELQLSISDDG VGFDPAHTRS GSFGLVGMRE RVAMLGGRLR
     LDSTPGQGTT LYVRIPLAQE EKETA
//
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