ID A0A074LTT3_9BACL Unreviewed; 382 AA.
AC A0A074LTT3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase DegS {ECO:0000256|PIRNR:PIRNR003169};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003169};
DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR003169};
GN ORFNames=EL26_06160 {ECO:0000313|EMBL:KEO84045.1};
OS Tumebacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO84045.1, ECO:0000313|Proteomes:UP000027931};
RN [1] {ECO:0000313|EMBL:KEO84045.1, ECO:0000313|Proteomes:UP000027931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GST4 {ECO:0000313|EMBL:KEO84045.1,
RC ECO:0000313|Proteomes:UP000027931};
RX PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT bacterium isolated from cassava wastewater.";
RL Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
CC -!- FUNCTION: Member of the two-component regulatory system DegS/DegU,
CC which plays an important role in the transition growth phase.
CC {ECO:0000256|PIRNR:PIRNR003169}.
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 ECO:0000256|PIRNR:PIRNR003169};
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 ECO:0000256|PIRNR:PIRNR003169}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEO84045.1}.
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DR EMBL; JMIR01000006; KEO84045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074LTT3; -.
DR STRING; 1157490.EL26_06160; -.
DR eggNOG; COG4585; Bacteria.
DR Proteomes; UP000027931; Unassembled WGS sequence.
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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
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; IPR008595; DegS.
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; IPR016381; Sig_transdc_His_kinase_DegS.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF55; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE DEGS; 1.
DR Pfam; PF05384; DegS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR PIRSF; PIRSF003169; STHK_DegS; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR003169};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR003169};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR003169};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003169};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR003169};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR003169};
KW Reference proteome {ECO:0000313|Proteomes:UP000027931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR003169}.
FT DOMAIN 182..381
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 46..80
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 110..144
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 206..233
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 382 AA; 43738 MW; 3BF4AD2280E1BA2B CRC64;
MPIEFDAKML DTAVNATLRA IEDGKNQVFE IAESARKEEQ AMREDALGIQ RQVAETIREV
ERLERAYTLA RHKLVEVSRD FDRHSESEIK QAYDDAHKVQ TQVLVTRERE QQLRARRDDL
DRRLRNLEQT IARAEALITQ LGVAFSYLSG DLSQIGNVLK NVEQRRFLGI RVIQAQEEER
KRVAREIHDG PAQTMANVVL RAEICEKMLD RDVEKVRSEL RELKDSVRAS LSEVRQIIFD
LRPMALDDLG LAPTLRRYMA DFQDKYKIAT ELKVFGREKR FNNSLEVAVF RSIQEALNNI
WKHAKASTAT VRLELTEKQV NVHIEDNGIG FDVSEATSGP EGGHFGLLGI KERIQLLEGR
LEIKSNRGKG TKVILSLPIT DE
//
