GenomeNet

Database: UniProt
Entry: A0A1W1V7P4_9DEIO
LinkDB: A0A1W1V7P4_9DEIO
Original site: A0A1W1V7P4_9DEIO 
ID   A0A1W1V7P4_9DEIO        Unreviewed;       582 AA.
AC   A0A1W1V7P4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN00790413_00403 {ECO:0000313|EMBL:SMB89419.1};
OS   Deinococcus hopiensis KR-140.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=695939 {ECO:0000313|EMBL:SMB89419.1, ECO:0000313|Proteomes:UP000192582};
RN   [1] {ECO:0000313|EMBL:SMB89419.1, ECO:0000313|Proteomes:UP000192582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KR-140 {ECO:0000313|EMBL:SMB89419.1,
RC   ECO:0000313|Proteomes:UP000192582};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FWWU01000009; SMB89419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1V7P4; -.
DR   STRING; 695939.SAMN00790413_00403; -.
DR   OrthoDB; 9795828at2; -.
DR   Proteomes; UP000192582; Unassembled WGS sequence.
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   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF65; SENSOR HISTIDINE KINASE COMP; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
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:SMB89419.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192582};
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   TRANSMEM        31..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          385..582
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   582 AA;  62133 MW;  263865C8B425CC1D CRC64;
     MMDPPAALPS PPPPEPSGVP LSDRVRLVRN VLPPLIVLVV AVVEFAIGQL GTATGEQWAH
     LLFYGLVGPA VTFFSVEWIA EGTRARERTE HELRLTYAQL SASHARLSAV QELMRDLTEA
     PDMGAVVEVA ARGAVRATGA VQATLTVPGG LSASASGEVT QAAEADAGRF PLRVPIPGGG
     ALALHFDTPP TPETAALAQA LAAEVATGVE AARQRTLDLM TLYSVDQSIR AERNMRRLLG
     RITRNMAERV RASARAAYLS DQDGTLRLEY AGDLGGEISG SGTLAPAFAA RVAQAGTPLV
     ATREEAAEAF PAEAGPEAAS ALGFPMRDEE GLVGVLVLGD TRPDTFEDAR LPLLALLAGQ
     ATLAVRNARA YLYSEELAIS DERARIAREI HDGVAQSLAF CALKLDIVAR QLHAEPEKAE
     AEVKAATALL REQIREVRRS IFALRPIDLE RYGLLETVRR YVEDFGEQNN LRTVLNVTGD
     IHLAPGDEAV VFRILQESLN NVAKHARARE VTVTLHGGTH VTLRVQDDGQ GFDLAQTTGR
     VSSAGGLGLM QMRERVESRG GQYRVLSAPG HGTVVEAEMP QA
//
DBGET integrated database retrieval system