ID A0A0Q3TK32_9BACI Unreviewed; 543 AA.
AC A0A0Q3TK32;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AN964_13180 {ECO:0000313|EMBL:KQL54352.1};
OS Heyndrickxia shackletonii.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Heyndrickxia.
OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL54352.1, ECO:0000313|Proteomes:UP000051888};
RN [1] {ECO:0000313|EMBL:KQL54352.1, ECO:0000313|Proteomes:UP000051888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL54352.1,
RC ECO:0000313|Proteomes:UP000051888};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KQL54352.1}.
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DR EMBL; LJJC01000004; KQL54352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3TK32; -.
DR STRING; 157838.AN964_13180; -.
DR PATRIC; fig|157838.3.peg.2927; -.
DR Proteomes; UP000051888; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 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; 2.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQL54352.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051888};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..537
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 543 AA; 60449 MW; 7A91B22B5FAB83F9 CRC64;
MYGFQEEKYL NVKQISIRWK ITILSYCVVI LSLLIGGILL VVNIQSAKEQ EINTAAMNTA
RTVAELSDVR KAVQKSKGWN NISHLIEQIR LINEEDYIVV MNMDRIRYSH PVPKLLGTPS
LGKDEDAAFA EHNYFSKAKG EMGTFTRAFF PIKDANLNQI GVVLVGHRIP SFWEISANLK
NEMIIILSLT LSAGLIGSFL LARHIKKQMF QLEPHQIARI LEERTATFHS MNEGVIAIDS
RENITIFNEK AKGIFSVKGD VVGKPIRSVL EDTRLPEIVE RNKAVYNETI IVGGKNILSS
RFPVLINQKV VGAVAICQDR TEVVKIAEEL TGVKNFVEAL RVQNHEYMNN LHTIAGLIQL
GKSEQALDLA FTTSEQQINV SKSIKEMIQS DALAGLLLSK IRRGKELGIE VRVDPNSCLS
QFPNQVDEHD FVVLLGNMLE NAFGSFEQVE KEGRFIDISI EQNEGICAIM LEDNGCGIAV
EDLPFIFDKG FTKNKQNGTG YGLFLVKQIV TKGNADVEVD SQVGEGTSFT ITFPMSLGVE
MNG
//
