ID A0A1H5XK47_9SPHI Unreviewed; 743 AA.
AC A0A1H5XK47;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05421877_10531 {ECO:0000313|EMBL:SEG12119.1};
OS Sphingobacterium lactis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=797291 {ECO:0000313|EMBL:SEG12119.1, ECO:0000313|Proteomes:UP000236731};
RN [1] {ECO:0000313|Proteomes:UP000236731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22361 {ECO:0000313|Proteomes:UP000236731};
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; FNUT01000005; SEG12119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5XK47; -.
DR OrthoDB; 9778366at2; -.
DR Proteomes; UP000236731; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; IPR011990; TPR-like_helical_dom_sf.
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 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.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:SEG12119.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Signal {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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..743
FT /note="Oxygen sensor histidine kinase NreB"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009289546"
FT TRANSMEM 488..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 550..741
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 388..422
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 446..480
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 743 AA; 85616 MW; 1398489350382376 CRC64;
MVKKLFIFFF SLCSLYPIAH GQDMLQKLQS EYQGSKLQDP ERFYRSGRYA QALFFNQQED
MAFHILKQEV QRASTLSESK YAAYLNTVLA INKMIAEEPA VAKQYITKAR NLANRTSDLE
IKGYVAYGHG WLLARQQQEG EAVKSLLEAL GHLDKAPKSK TLGGRKSAVY KELTAIYANW
NEFALQEKYS KLSLDLAREQ QDPMAIFDGY MLLGYLYEQQ YLTQTTELSY RNSAETYYLK
ALDTYLQNEG EMPIPSNLSF VANNLAHLYF KHFPRTYREK AISFAELARQ KGEETKQYNL
VASSYGIMAE MELQDGNAAK AKEYLLASLI AMNKSTVQDQ QILMSIYESL AKASEEEGDY
KEAIQYYKRY VETFSAFYDQ EKLNLSKRLE AQYEKDKQEQ QMATLTLESE KKEQQIRLME
ALGLQQRQEL ENMTLIRANQ SKELELSKLH TERQAQEIQL NKLEAKNKEQ QIDLFQKELN
LKDKLNTYYI ALLLAFLLLL GLVLYAYRQR SKHLRQQIDL KNLELAQERQ DVKIATLTAL
LDGQEQERAR IARDLHDGLG GLLSGTKLHL SQLNEQLLQQ NKMKMEKGIT QLDMAVDELR
RVAHNLTPDL LQKFGLFEAL QEYARRMSNE TLEIDVQFLY FKTPLPAESE LLLYRIIQEL
VNNAIKHANP TQVIIQLVEE DNAYLVTVED DGTGFDYLRQ QGNSAGLLNI QSRVEFLKGV
LHVQSDPGKG SSFEITFPKS TTI
//
