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Database: UniProt
Entry: A0A0P9CAQ6_9BACL
LinkDB: A0A0P9CAQ6_9BACL
Original site: A0A0P9CAQ6_9BACL 
ID   A0A0P9CAQ6_9BACL        Unreviewed;       597 AA.
AC   A0A0P9CAQ6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AN477_17170 {ECO:0000313|EMBL:KPV42488.1};
OS   Alicyclobacillus ferrooxydans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV42488.1, ECO:0000313|Proteomes:UP000050482};
RN   [1] {ECO:0000313|EMBL:KPV42488.1, ECO:0000313|Proteomes:UP000050482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC-34 {ECO:0000313|EMBL:KPV42488.1,
RC   ECO:0000313|Proteomes:UP000050482};
RA   Hemp J.;
RT   "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL   Submitted (SEP-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   -!- 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:KPV42488.1}.
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DR   EMBL; LJCO01000076; KPV42488.1; -; Genomic_DNA.
DR   RefSeq; WP_054970406.1; NZ_LJCO01000076.1.
DR   AlphaFoldDB; A0A0P9CAQ6; -.
DR   STRING; 471514.AN477_17170; -.
DR   PATRIC; fig|471514.4.peg.3559; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000050482; 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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; 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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050482};
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        189..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..262
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          378..595
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          63..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65432 MW;  B594A76B6C1B51DF CRC64;
     MWRSIRIRLV AIQVLLLLFA LELIGGYFVS ALNQSLLRTE TDTVSRQTQL IATLTLPEIV
     TKQGTSSFPS TQGSTGGTTG ANTSSTAQPL LQSFPQLING VAYVLNKDGV VKDTSAGSAL
     IGQKRIDSLA TETLISHKKA VAVHYDTLTG QHLLSVVVPV FSQGHFVGLV ESVVSVQSTY
     ATMREVTTIF YTGSGLVLAL TAVLSVLLSR AIARPVLDVT KQARKLAAGD FSERVTVHSD
     DEFGALGTAI NDLTDKLQAA IAESQHEQGR LQAVIKYMGD GVIALDKELH YLFSNDAAMR
     MLPGASTPEF DPAHLLGLER IVQEEKGEWN FVKKLQDSLF NVHVTKIGTR QVQGYVALVR
     DVTEQEKLQA ARRDFVANVS HELKTPLTSM KSYIEVLQEY PDTDEETRKR FLSVIQNETE
     RMVRLTQDLL QLSGLETRQE PFRAGLINVS EWLSTAVNRF NLSAKQQGVT LVSEPYPTVS
     LRGDRDMLDR LVDNLISNAL KYTAREGVVR ITAAAESDQL LVSVQDSGIG IPAEDLPHVF
     ERFYTVDKAR TRKFGGTGLG LAIAREITER HGGRIAILSE LNEGTTVTVS LPTVEVR
//
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