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Database: UniProt
Entry: A0A3D8GTD3_9BACI
LinkDB: A0A3D8GTD3_9BACI
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ID   A0A3D8GTD3_9BACI        Unreviewed;       948 AA.
AC   A0A3D8GTD3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DRW41_07280 {ECO:0000313|EMBL:RDU37637.1};
OS   Neobacillus piezotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=2259171 {ECO:0000313|EMBL:RDU37637.1, ECO:0000313|Proteomes:UP000257144};
RN   [1] {ECO:0000313|EMBL:RDU37637.1, ECO:0000313|Proteomes:UP000257144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLB-04 {ECO:0000313|EMBL:RDU37637.1,
RC   ECO:0000313|Proteomes:UP000257144};
RA   Yu L., Tang X.;
RT   "Bacillus sp. YLB-04 draft genome sequence.";
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   -!- 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:RDU37637.1}.
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DR   EMBL; QNQT01000002; RDU37637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8GTD3; -.
DR   OrthoDB; 9790669at2; -.
DR   Proteomes; UP000257144; Unassembled WGS sequence.
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; cd19411; MCP2201-like_sensor; 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; 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; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR047347; YvaQ-like_sensor.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 1.
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:RDU37637.1};
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:UP000257144};
KW   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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          209..263
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          518..748
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          829..946
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          763..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          432..508
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         879
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   948 AA;  104391 MW;  0106CF4AED77780A CRC64;
     MVVTFKKKQF FGLGLTLLFM TLLLFVILSL TGKIKTNMLS IVEDRYDKVN DAMEIRQAVL
     LTDRELVNAI QEGNSPDIET LIPLLESNQK IVQESIVKLD GILNKPTSKK LLKEIDIAYR
     EYLDTEKQLI SGLKAGAKPA DLRKIYYGSV AEKGELVKKV NEFKSYQERL MNESLKSANK
     SYDQLFAALF ISVIAAAILI TGVTLWVIRS TSRRLDSVAE GIKTIDYNNL AEIPRIKVEA
     HDEIGQISAA FNSMAVSLET YYNKEKKFTA EISEQNWVQT QSAELINLYH KSTEVEGLAE
     QLMANLAPAV GASLGAFYLM ENQTLKKVGS FADGGGTAGR AEIALREGLA GQCAVKKEAI
     YIEDIPEDYT VISTGLGSMK PKSLLIAPVL VKDETVAVIE LASLKPFTRA ERILANKVFE
     TLGMAVMNIL GRMEIERLLL ESQAQAEELQ SQSEELQAQS EELQTQAEEL RMINEQLEER
     TKDAEIKSAE LLIAKEELEV KAKELQLSSK YKSEFLANMS HELRTPLNSI LLLSEMLGED
     TDENLTDEQK DFAKVIHTSG QDLLNLINDI LDLSKVEVGK LEVVFDGVNI ADFGGRLEHL
     FSHHAVRKGL GFMVDIEDNL PDLFYTDEQR LQQIVKNLLA NAFKFTESGA VIASINRAEP
     NEIPAEPVSD TWLKFSVSDT GIGIAEDKQQ LIFEAFQQVD GATMRKYGGT GLGLSISSEF
     ARLLGGTVTV ESEEGKGSTF TLLIPSLPKG VPTSGEAITP AVHNGASEDE GGVEASVGGE
     HPSGQVKAAS VEVAAGNSVL FADGNPLMAE EEGHEESGSV PFNNLRGKTV VVADDDHRNI
     YALDKALSRE GMRVLSVENG MECLEILQRT DNVDIILMDI MMPIMDGYET MQQIRGMDRY
     GNIPIIALTA KAMKGDKEKC LEAGASDYIS KPLKMDQLFS AMRVWLAR
//
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