ID C3FZA9_BACTU Unreviewed; 896 AA.
AC C3FZA9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=bthur0009_8810 {ECO:0000313|EMBL:EEM73091.1};
OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM73091.1};
RN [1] {ECO:0000313|EMBL:EEM73091.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM73091.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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:EEM73091.1}.
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; ACNG01000030; EEM73091.1; -; Genomic_DNA.
DR RefSeq; WP_000834154.1; NZ_CM000754.1.
DR AlphaFoldDB; C3FZA9; -.
DR HOGENOM; CLU_000445_127_2_9; -.
DR Proteomes; UP000001380; 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};
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}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 13..32
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; 101738 MW; A761404956DDC06F CRC64;
MKSEAKFSIR YKIMAGYLVI ILFLLISFIM LNNQISNLQK SRNFIIDHDF KVLNLTNQVE
KDLLTIENKA KGFITSNNAN YLQSLNSAER DYEKHYHDLF SLLEDNPSQQ EKLKEINENI
TNWMNKEIHP LIANHNSNKI QEIDTTEIQS LQSQLTDFRS TEEQLTKKRA AQLDTKNNKL
ELWLYSLLFL LSCISIIVSL YISNSITKTI KNVIQAIKSI SSKEKITERI HVNTHDEIKD
LAHTTNHLLD EISKREWLQT EIAELILMYQ GVSSIEMLGN KILSGIIQKT QTSCGAFYVR
EEYEETVYYV KKASFADQGV DIGKQSIKMG EGFIGQSALE KKSFILRDIP EEFRYVTTGL
LEIRPKNLLV IPVLFEDEVI AVMELVSVTD ISDLHQDLIH QTVDNLGLTI HSIMGRMRIQ
TLLHESQAMT EELQVQSEEL QTQAEELQMQ AEELRTTNEQ LESRTEEAEQ KTADLQITKL
ELEEKASELL RSSKYKSEFL ANMSHELRTP LNSILLLSEM LKENHDNHLS DDEIELATVI
HSSGKDLLTL INDILDLSKV EAGKLDVIFE ATNISDMAAS MHQNFLHIAA QKNVEFTVED
SDTIPDLFYT DAKRIEQIIK NLLSNAFKFT EKGSVSLHFD SIETSNLSHD MQSISKDWIT
ISVKDTGIGI AKEQHQLIFE AFQQADGATI RKYGGTGLGL SICKEFARLL GGWITLESHV
GEGSTFTVYI PNLPNGLHDV QLSNLEVAAT VDEVIPAEVI EETIVLPEAN NVFQEKTILI
VDDDHRNIFA LQNALKKQHA NIITAQNGLE CLEILKNNTN IDLILMDIMM PNMDGYETME
HIRMNLGLHE IPIIALTAKA MPNDKEKCLS AGASDYISKP LNLHQLYSVM SVWLIK
//
