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Database: UniProt
Entry: A0A0A6V9F0_9BACI
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ID   A0A0A6V9F0_9BACI        Unreviewed;       747 AA.
AC   A0A0A6V9F0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NG54_17160 {ECO:0000313|EMBL:KHD84188.1};
OS   Heyndrickxia ginsengihumi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=363870 {ECO:0000313|EMBL:KHD84188.1, ECO:0000313|Proteomes:UP000030588};
RN   [1] {ECO:0000313|EMBL:KHD84188.1, ECO:0000313|Proteomes:UP000030588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2.11 {ECO:0000313|EMBL:KHD84188.1,
RC   ECO:0000313|Proteomes:UP000030588};
RA   Toymentseva A., Boulygina E.A., Kazakov S.V., Kayumov I., Suleimanova A.D.,
RA   Mardanova A.M., Maria S.N., Sergey M.Y., Sharipova M.R.;
RT   "Draft genome of phytase producing Bacillus ginsengihumi strain M2.11.";
RL   Submitted (OCT-2014) 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:KHD84188.1}.
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DR   EMBL; JRUN01000087; KHD84188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6V9F0; -.
DR   STRING; 363870.NG54_17160; -.
DR   Proteomes; UP000030588; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd01948; EAL; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.20.20.450; EAL domain; 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; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR   PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR   Pfam; PF00563; EAL; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00052; EAL; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF141868; EAL domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50883; EAL; 1.
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:UP000030588};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..249
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
FT   DOMAIN          397..468
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          470..522
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          535..739
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   747 AA;  85548 MW;  C67EE5D6BEB2B19E CRC64;
     MNLNEILARK ELRLYFQPML NLNSGKINEV EALFHWEHPE KGVISSFELF ALAEETGAII
     QIGEWLMRKA CEQNKLWQKM GLPSFPIAVC LSACQLTQPN FVESVQRILE ETQLSPEYLE
     LEITESIMMD AHIVLPILRE LKRIGVQISL DDFGMGYCSL YYLKEFPIDK IKISRSFVCN
     CTTDKKDATL IKAIIAMAHQ LSLEVAAKGI ESKDQLLFLQ QHLCNIGEGA FFSDPLLPNE
     FYESFYNIER IIREEGISPV LCRQKQLEEE LENARQELRD TVSLQQGMIF KFVKENGKFI
     HTLCYGELFY RIGIIPEKLI GKELFDFFPK DVAEKKLQYY ERAWAGEENV KYEGFQNGIW
     YLTSLRPVKQ GEKIIEVICS SIDITERKKM EETLREREQK YRLIAENMQD LIAVVNTNGI
     ILYASPSYET VLGFPPNVYE GNAPTLLVHP DDVSKIHSQY EHMALTKSPG YVEFRYQHAQ
     NGWVYVESLG TPVLNGHGEV EHFVVVARDI SKRKKVEELM RKSEKLSVVG QLAAGVAHEI
     RNPLTSIKGF VQLLRQEVNH SFYMDIIISE INRLESIVGE FLTLAKNQPP KRERLDLRIL
     LQQVVSLFDT KSLYKNVEII QEYDEGLPFI YCDGNQMKQV FMNIIKNAIE AMPNGGIIEI
     QISCHNFHSV RLTFIDQGVG ISAERIKHIG EPYFSTKEKG TGLGLMISHK IVQEHGGTIH
     IESQVNKGTK VEVMLPIKQP SPVENSI
//
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