ID G2FQ47_9FIRM Unreviewed; 534 AA.
AC G2FQ47;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DOT_1850 {ECO:0000313|EMBL:EGW40209.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW40209.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW40209.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW40209.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EGW40209.1}.
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DR EMBL; AGAF01000085; EGW40209.1; -; Genomic_DNA.
DR AlphaFoldDB; G2FQ47; -.
DR PATRIC; fig|913865.3.peg.1675; -.
DR eggNOG; COG3852; Bacteria.
DR Proteomes; UP000004928; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:EGW40209.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EGW40209.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..532
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 534 AA; 59797 MW; C4B4BE72D0ECBF41 CRC64;
MNFIREKRLA KVLLIMLILV PVVTMGYLLL FDQLNEQRQE MINKNMQIAR LTANYVDDYL
SSYKQTLKGV AFRVPLIDND RNELTKLLRD ISLAHSEASL FYVANAKGQL LAKYPNDHAD
KNIVDRDFFT AAMQKKVFIG GPYVGRVTGI DIISITAPFY QDGKVSGIVG VSIPLDELQN
KLSVIQIGHS GYATRFTKDG NFLWHPKLEE LKKTMELDKT PLFKAALAAK TGEGSIGPSP
GEEPPEQHSF VTLTEAPWVI VIVQPLQEFN NQMNQIMWRN IFIIILLIMF IIVILRYFNL
LKDRIAAEHI QKAEKLALVG QLAAGVAHEI RNPLTSIKGF VQLIQSKKSE PIPEFYLETI
MQEIDRINDI VGEMVVLAKP VPVQFAEINL RNLINDILNL IGPQAVLKDI QLELIASEDL
LAIRGEPNQL KQVFINLIKN SIESIVDGGF VKIHLTNRGN SVVEVKVQDN GPGVPRENLE
KLGTPFFTTK ETGTGLGLMV TYGIIRNHKG EINVLSEVGH GTTFSINFPV LTIE
//
