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Database: UniProt
Entry: Q81H18_BACCR
LinkDB: Q81H18_BACCR
Original site: Q81H18_BACCR 
ID   Q81H18_BACCR            Unreviewed;       896 AA.
AC   Q81H18;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=BC_1008 {ECO:0000313|EMBL:AAP07995.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP07995.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP07995.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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}.
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DR   EMBL; AE016877; AAP07995.1; -; Genomic_DNA.
DR   RefSeq; NP_830794.1; NC_004722.1.
DR   RefSeq; WP_001084970.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81H18; -.
DR   SMR; Q81H18; -.
DR   KEGG; bce:BC1008; -.
DR   PATRIC; fig|226900.8.peg.962; -.
DR   HOGENOM; CLU_000445_127_2_9; -.
DR   OrthoDB; 9790669at2; -.
DR   Proteomes; UP000001417; 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:AAP07995.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAP07995.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        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;  101539 MW;  B19865FD383D0013 CRC64;
     MNSKAKFSIR YKIMAGYLVI ILFLLVSFIM LNNEISSLQK SRNFIIDHDF KVLNLTNQVE
     KELLTIENKA KGFIISNNPT YVQSLNSAEK DYEKHYQDLF ALLEDNPSQQ EKLKQINENI
     TSWINKEIHP LIANNNSNNV QTIDTTQIQS LQSQLTNFRN TEEQLTKKRA AQLDTENNKL
     EIWLYSLLFL LSCISIIVSL YISNAITKTI KNVIQAIKSI SSKEKITERI HVNTHDEIKD
     LAHTTNHLLD EISKREWLQT ELAELILMYQ GVSSIEMLGK KILSGIIQKT QTSCGAFYVR
     EEYEETVYYV KKASFADQGA DVGKQSIKMG EGFIGQSALE KKSFILRDIP EEFRYVTTGL
     LEIRPKNILV IPVLFEDEVI AVMELVSVTE ISDLHQDLIH QTVDNLGLTI HSIMGRMRIQ
     TLLHESQAMT EELQVQSEEL QTQAEELQMQ AEELRTTNEQ LESRTEEAEQ KTADLQITKL
     ELEEKASELL RSSKYKSEFL ANMSHELRTP LNSILLLSEM LRENHDNNLS DDEIELATVI
     HSSGKDLLTL INDILDLSKV EAGKLDIIFE ATNISDMAAN MHQNFLHIAA QKNVEFTIED
     SDTIPDLFYT DAKRIEQIIK NLLSNAFKFT EKGSVSLHFD SIETTNLSHD MQSISKDWIT
     ISVKDTGIGI AKEQHQLIFE AFQQADGATI RKYGGTGLGL SICKEFARLL GGWITLESNV
     GEGSTFTVYI PNLPNGLHDI QLSNLEVAAT IEDVIPAKVV EETIVTTETN NVFQEKTILI
     VDDDHRNIFA LQNALKKQNA NIITAQNGIE CLEILKSNTN IDLILMDIMM PNMDGYETME
     NIRMNLGLHE IPIIALTAKA MPNDKEKCLS AGASDYISKP LNLHQLYSVM SVWLIK
//
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