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Database: UniProt
Entry: A0A0M4GB72_9BACI
LinkDB: A0A0M4GB72_9BACI
Original site: A0A0M4GB72_9BACI 
ID   A0A0M4GB72_9BACI        Unreviewed;       339 AA.
AC   A0A0M4GB72;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AM500_05570 {ECO:0000313|EMBL:ALC89313.1};
OS   Bacillus sp. FJAT-18017.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC89313.1, ECO:0000313|Proteomes:UP000060713};
RN   [1] {ECO:0000313|EMBL:ALC89313.1, ECO:0000313|Proteomes:UP000060713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC89313.1,
RC   ECO:0000313|Proteomes:UP000060713};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) 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};
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DR   EMBL; CP012602; ALC89313.1; -; Genomic_DNA.
DR   RefSeq; WP_053598344.1; NZ_CP012602.1.
DR   AlphaFoldDB; A0A0M4GB72; -.
DR   STRING; 1705566.AM500_05570; -.
DR   PATRIC; fig|1705566.3.peg.1200; -.
DR   Proteomes; UP000060713; Chromosome.
DR   GO; GO:0016020; C: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; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF2; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ALC89313.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060713};
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        20..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..338
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   339 AA;  38651 MW;  F301952C210C9057 CRC64;
     MMQKAIFINF LKDKLPTITL YLACVAAIII FFHLSEPSNT EIFYPVSIAV FLLAACLAID
     WLRYYPANQA IALMLMNQDT ELQPHTEEQK AFQKLVHKMT GQYTRKNNEL KEQNKERLYF
     LSHWLHHLKT PVSVIELLTN KGNQAQDDNE IFEKIRHENN RLHTSIQQGL TMIRMEGFEN
     DLEVKSVDLL PSLRKLINDR KKECIYHSIY PSIEFEGESA MIASDPKWNE ILLEQIISNA
     IKYSSPKLGS KKLILQIEKT GKHVSLTVKD EGIGIPAYDL ERVFQPFFTG DNGRAHSNST
     GIGLYLSKKI AEKLGASINI ESEPSKGTAV TIRWLAGTD
//
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