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Database: UniProt
Entry: A0A0M2PHI8_9BACI
LinkDB: A0A0M2PHI8_9BACI
Original site: A0A0M2PHI8_9BACI 
ID   A0A0M2PHI8_9BACI        Unreviewed;       544 AA.
AC   A0A0M2PHI8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=WQ54_19760 {ECO:0000313|EMBL:KKI90223.1};
OS   Bacillus sp. SA1-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI90223.1, ECO:0000313|Proteomes:UP000034887};
RN   [1] {ECO:0000313|EMBL:KKI90223.1, ECO:0000313|Proteomes:UP000034887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1-12 {ECO:0000313|EMBL:KKI90223.1,
RC   ECO:0000313|Proteomes:UP000034887};
RA   Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-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};
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:KKI90223.1}.
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DR   EMBL; LATZ01000119; KKI90223.1; -; Genomic_DNA.
DR   RefSeq; WP_046586603.1; NZ_LATZ01000119.1.
DR   AlphaFoldDB; A0A0M2PHI8; -.
DR   PATRIC; fig|1455638.3.peg.4341; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000034887; Unassembled WGS sequence.
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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; 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; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 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; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
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, ECO:0000313|EMBL:KKI90223.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          148..202
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          203..273
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          341..544
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   544 AA;  62916 MW;  812AC657012C8B5B CRC64;
     MANKIKWLLL YIVFSFLWII VTDNLIVFIN VPTDIHLILQ NIKGTLFVIF TSIFIYYLIL
     KKEAYEKEKE EKNKLNILIN SMVDFVNFKD GEGRWTKANE FALKLFKIEH VDYRGKKDSD
     LAEYSEFYSE ALRYCEISDE EAWLKGKVSR CIEEIKKPDG TVKTFDTIKI PIFDDETGSR
     KELVVMGRDV TDRIAAEKKL AESEQRYKSL FEFNPALVYM IDLQGKLSNV NDHFFKYTGY
     QKEAFLQNSI ISLIAKQDRS RVKEAYQKVI RENTPWINEE IEMVTKDRFK KILRCTAVPM
     IINDETVGVI GYAVDITKEK ETEELLLKTE KLSVVGELAA SVAHEIRNPL TSLKGFVQIL
     QTSSKENQKF YKIMLDELER INIIASELLV LAKPQQIQFQ TRDINELLRN VKSLLESEAN
     LYSAELEIIT NEKLPPIDCE PNQLKQLFIN IIKNSIEASS NKIQVTVEMF DQEHICIQFI
     DNGCGINQER LKHLGEPFYS MKEKGTGLGL TVSYRIVEFH KGKIDFKSKV NEGTTVSLVL
     PIKK
//
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