ID A0A370GEY2_9BACI Unreviewed; 566 AA.
AC A0A370GEY2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DFR59_10580 {ECO:0000313|EMBL:RDI42241.1};
OS Falsibacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=493781 {ECO:0000313|EMBL:RDI42241.1, ECO:0000313|Proteomes:UP000255326};
RN [1] {ECO:0000313|EMBL:RDI42241.1, ECO:0000313|Proteomes:UP000255326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25281 {ECO:0000313|EMBL:RDI42241.1,
RC ECO:0000313|Proteomes:UP000255326};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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 -!- 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:RDI42241.1}.
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DR EMBL; QQAY01000005; RDI42241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370GEY2; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000255326; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
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; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000255326};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 223..274
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 300..352
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 365..566
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 566 AA; 64707 MW; 602501D4A17EE1D6 CRC64;
MQKTVRSDMT DVLLNHIPHP AILMKKDGTI TASNQIFKEL IGHGAISSKD LKKYIEESLS
SAKSEFSISL ISLRTTLIIE KNAAEDSFFG KFIMHSLSRS AGESKFSMFI QHYPDAIFYL
NLEGEITRQN LSAKRFTHSF GKEREVNVPL TKFILEEDHE IHNRMMKQTF SLNRMPVLLR
MRDSENEIHL LEVSYIPRIE NDQYAGVYVI GQDKTQRLLI EDELKEVRVL LESYFQNAEK
SSCILDENGY ILKANTAFEQ MVGRTKNELI GYSLSHIQRC GDCLDFNSQL YRVRDREYIT
GFETNVYDKQ GNKKIISMSF SPMLGKKGRV IGMLVGLEDI TSEKQTEDLL KKSEQLALIG
QLAAGVAHEI RNPLTTLKGF MQLLREEMTQ RAYFDVILDE LQRIELITGE FLSLAKPHSI
HFKQCSINKL LFEVAEFINI ECLKNNVTLE VHVHEFMEVM CDIHQLKQVL LNIMKNALEA
MPKGGELNIH LKRYEQMAII QVKDSGIGIP EHRLKHLGEP FYSTKEKGTG LGLMISNKII
KEHKGNFVIE SIEGEGTSVI LELPLV
//