ID Q6HMG5_BACHK Unreviewed; 896 AA.
AC Q6HMG5;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BT9727_0917 {ECO:0000313|EMBL:AAT62380.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT62380.1, ECO:0000313|Proteomes:UP000001301};
RN [1] {ECO:0000313|EMBL:AAT62380.1, ECO:0000313|Proteomes:UP000001301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27 {ECO:0000313|EMBL:AAT62380.1,
RC ECO:0000313|Proteomes:UP000001301};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017355; AAT62380.1; -; Genomic_DNA.
DR RefSeq; WP_000836726.1; NC_005957.1.
DR RefSeq; YP_035256.1; NC_005957.1.
DR AlphaFoldDB; Q6HMG5; -.
DR KEGG; btk:BT9727_0917; -.
DR PATRIC; fig|281309.8.peg.965; -.
DR HOGENOM; CLU_000445_127_2_9; -.
DR Proteomes; UP000001301; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAT62380.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAT62380.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..257
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 502..734
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 777..894
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 423..485
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 827
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 896 AA; 101567 MW; A167849F31155BAB CRC64;
MKSKAKFSIR YKIMAGYLVI ILFLLISFIV LNNQISNLQK SRNFIIDHDF KVLNLTNQVE
KDLLTIENKA KGFITSNNAN YLQSLNSAER DYEKHYHNLF SLLEDNPSQQ EKLKEINGNI
TNWMNKEIHP LIANHNSNKI QEIDTTEIQS LQSQLTDFRS TEEQLTKKRA AQLDTKNNKL
ELWLYSLLFL LSCISIIVSL YISNSITKTI KNVIQAIKSI SSKEKITERI HVNTHDEIKD
LAHTTNHLLD EISKREWLQT EIAELILMYQ GVSSIEMLGN KILSGIIQKT QTSCGAFYVR
EEVEETVYFV KKASFADQGI DIGKQSIKMG EGFIGQSALE KKSFILRDIP EEFRYVTTGL
LEIRPKNLLV IPVLFEDEVI AVMELVSVTD ISDLHQDLIH QTVDNLGLTI HSIMGRMRIQ
TLLHESQAMT EELQVQSEEL QTQAEELQMQ AEELRTTNEQ LESRTEEAEQ KTADLQVTKL
ELEEKASELL RSSKYKSEFL ANMSHELRTP LNSILLLSEM LKENHDNHLS DDEIELATVI
HSSGKDLLTL INDILDLSKV EAGKLDVIFE ATNISDMAAS MQQNFLHIAA QKNVEFTVED
SDTIPDLFYT DAKRIEQIIK NLLSNAFKFT EKGSVSLHFD SIETSNLSHD MQSISKDWIT
ISVKDTGIGI AKEQHQLIFE AFQQADGATI RKYGGTGLGL SICKEFARLL GGWITLQSHV
GEGSTFTVYI PNLPNGLHDV QLSNLEVAAT VDEVIPAEVV EETIVLPETN NVFQEKTILI
VDDDHRNIFA LQNALKKHHA NIITAQNGLE CLEILKNNTN IDLILMDIMM PNMDGYETME
HIRMNLGLHE IPIIALTAKA MPNDKEKCLS AGASDYISKP LNLHQLYSVM SVWLIK
//
