ID A0LPI6_SYNFM Unreviewed; 650 AA.
AC A0LPI6;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
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 OrderedLocusNames=Sfum_3668 {ECO:0000313|EMBL:ABK19338.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK19338.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK19338.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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; CP000478; ABK19338.1; -; Genomic_DNA.
DR RefSeq; WP_011700463.1; NC_008554.1.
DR AlphaFoldDB; A0LPI6; -.
DR STRING; 335543.Sfum_3668; -.
DR KEGG; sfu:Sfum_3668; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4585; Bacteria.
DR HOGENOM; CLU_000445_114_71_7; -.
DR InParanoid; A0LPI6; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 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; 3.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
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:ABK19338.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 49..87
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 115..182
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 183..253
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 255..307
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 308..352
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 377..430
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 559..650
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..448
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73071 MW; 15073F490173FF44 CRC64;
MSDERDGNKT QAVCSPPLKS RQAREEITDD AGGRPLRDRP HITRRNLDII EFLPDATFVI
DREGKVIAWN RAIEEMTGVR KKDILGRGDF AYAVPFYGER RPIVIDLVMG ADSKFERKYQ
YVKKQGETYF AEAYAPNAYR GKGAYLWGKA SPLYDGKGNW VGAIQSIRDI TDKRLADQAL
ARSERQFRML VETMNEGLCV RDANDRVLYA NDKMCRLLGY VREELVGMQV SALFDSANLL
ILQREMEKRR NREGSLYEIQ MKSRDGRNIP VLVSGRPMFG EQGDYRGTIS TMTDITTIKE
AETKLRESEQ KYRMIFENSP LGIFHFDADC VITTANENIF RIWGTTAEKL VGFNLNTSLK
NKKMKAAVIA CMSGKSAHYE GSYLSVTGGK ISNLKANYGP ILSADGKVIG GIGIIEDISE
RKQTEAALQE SERQLHLLSS QLLAAQEQER KRIARELHDG IGSSLSTIKF SLEATLRRMR
QGSQSYESLQ NVIVLTQHAI DESRRIMTDL RPPILDDFGI LTTMDWFCAQ FRKAYTHLRV
DKEIEVVEED IPEALKIVIF RVLQEALHNT AKYSQASRVK IGLRKTPGTL ELKIGDNGIG
FDRTSASRRS DSSSGLGLPS MKERTELSGG TFSVESTEGA GTTLCATWPL
//
