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Database: UniProt
Entry: A0A0P6XAI5_9CHLR
LinkDB: A0A0P6XAI5_9CHLR
Original site: A0A0P6XAI5_9CHLR 
ID   A0A0P6XAI5_9CHLR        Unreviewed;       584 AA.
AC   A0A0P6XAI5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AC812_04340 {ECO:0000313|EMBL:KPL77243.1};
OS   Bellilinea caldifistulae.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Bellilinea.
OX   NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL77243.1, ECO:0000313|Proteomes:UP000050514};
RN   [1] {ECO:0000313|EMBL:KPL77243.1, ECO:0000313|Proteomes:UP000050514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL77243.1,
RC   ECO:0000313|Proteomes:UP000050514};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Draft genome of Bellilinea caldifistulae DSM 17877.";
RL   Submitted (JUL-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:KPL77243.1}.
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DR   EMBL; LGHJ01000010; KPL77243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P6XAI5; -.
DR   STRING; 360411.AC812_04340; -.
DR   PATRIC; fig|360411.5.peg.3396; -.
DR   Proteomes; UP000050514; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd06225; HAMP; 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; 6.10.340.10; -; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR031967; PhoR_single_Cache-like_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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   Pfam; PF00989; PAS; 1.
DR   Pfam; PF16736; sCache_like; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050514};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..243
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          248..296
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          369..584
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          235..262
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   584 AA;  65318 MW;  D95396651FB3EBD6 CRC64;
     MKRSLLWRLA IPFILLIILS VGGVSLYAYR FMERTYYENL RTTLRTEADL IARDVLEHLR
     EGEINPQLDN LVNDYASITG VRVTIILPDG RVIGESGRDP TQVENHLNRP EVQQALAEGE
     GTAIRLSNTV HQRLYYLALR VDGNGVPLGV VRLASSIEKI ESDLLELRNT ILGSALLTIG
     LTILLAFLAA NQTITPLRQL TREVSRLGIG NFNIELPTYR QDEIGILSQA FVRIAKRLSE
     QIEGYREERS KLDAVLRNMN DAILIVDGQG LVTLINPAAE RIFNVDSSRA LGHSLVEVVR
     QHAFVELWRS CVKTKRQQIA TIETAPERLF IQGIATPLEP LLPENTLLVF QDLTRVRRLE
     VVRRDFISNV SHELRTPLAS LKALTETLQE GALEDPPAAR RFLQKMENEI DNMTQLVREL
     LELSRIESGK VPLNLKPVPP NELVARAVER MQLQAERAGL TLRRECAEDL PNVLADAERI
     EQVLVNLLHN AIKFTPAGGE IVARTWKEAG QVIFSVQDTG VGIEPAALTR IFERFYKADQ
     SRSGGGTGLG LSIARHTVEA HSGRIWAESE VNRGSTFYFS IPTA
//
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