ID A0A150LWQ4_9BACI Unreviewed; 348 AA.
AC A0A150LWQ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Sensor histidine kinase {ECO:0000256|PIRNR:PIRNR037431};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR037431};
GN ORFNames=B4135_2597 {ECO:0000313|EMBL:KYD16685.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD16685.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD16685.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD16685.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:PIRNR037431};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037431};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR037431}.
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:KYD16685.1}.
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DR EMBL; LQYT01000061; KYD16685.1; -; Genomic_DNA.
DR RefSeq; WP_061569233.1; NZ_LQYT01000061.1.
DR AlphaFoldDB; A0A150LWQ4; -.
DR STRING; 301148.B4135_2597; -.
DR PATRIC; fig|301148.3.peg.4171; -.
DR OrthoDB; 9795828at2; -.
DR Proteomes; UP000075683; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR017202; LiaS/VraS.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
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 PIRSF; PIRSF037431; STHK_LiaS; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037431};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR037431};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037431};
KW Membrane {ECO:0000256|PIRNR:PIRNR037431, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037431};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037431};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR037431}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..341
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 109..144
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 348 AA; 39621 MW; 59C6F73547D09EC3 CRC64;
MNLFFRQLAA GFAVILPLVA AISTILFAAY PLDDWSLLWK REVFDIPFLM FLPLFSIGAA
FLAAVGSTLY WRKQFKTIED YLLAVEHGHV PSKKDKKFLQ EVADILSGIE QVQKQLQEQT
KISQKLAKEK AEELDKRMQE LVFEERQRLA RELHDSVSQQ LFAASMLLSA IIEGGRDPEE
NRRQLKLVEK TIQQAQLEMR ALLLHLRPAA LKGKSLKKGI EELLVELSQK VPIQIRWKVE
DLQINHKGVE DHLFRILQEA VSNTLRHSKA SAMEVLLVER DGFIILRVTD DGEGFDVDKV
KTASYGLQNM RERAREIGGT WKMVSSPGMG TKLEVRVPIV HLGGEKDD
//
