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Database: UniProt
Entry: A0A1F8NZX9_9CHLR
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Original site: A0A1F8NZX9_9CHLR 
ID   A0A1F8NZX9_9CHLR        Unreviewed;      1026 AA.
AC   A0A1F8NZX9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A2Z14_19510 {ECO:0000313|EMBL:OGO16475.1};
OS   Chloroflexi bacterium RBG_16_48_8.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797641 {ECO:0000313|EMBL:OGO16475.1, ECO:0000313|Proteomes:UP000177106};
RN   [1] {ECO:0000313|EMBL:OGO16475.1, ECO:0000313|Proteomes:UP000177106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO16475.1}.
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DR   EMBL; MGNI01000171; OGO16475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8NZX9; -.
DR   STRING; 1797641.A2Z14_19510; -.
DR   Proteomes; UP000177106; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
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; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 3.
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; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          547..617
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          622..674
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          675..731
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          746..800
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          804..1026
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          523..550
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1026 AA;  114836 MW;  489C8284AB016942 CRC64;
     MVQLKHKETE VYPKSVWAEA MRATVAVARR SLKGEDALLR AVSDELQRLE MTGFILLLCE
     DGLLELRATP SVLEQRLKEL TGLDVRGLRF DPHKVDVYQR VLKDLESFFE SSHKPILEQV
     LPKETRPLTG KLIEALGVHP IIYAPLFVEE KVLGVMNVSA EWFTVEDVPM VSSLADHIAI
     SLSHMRTSLE FQNILKRERL RTRVAEVIAN SWDLDQILDR ILHMVVEAVR AEAGSIALVE
     PGAQLLRLYH LYALPQALGL KQVPRNQGLA WKMIEDGKPV IHNNYAQHPD ALQEWVDAGV
     QAVMSAPLIT GDEIIGTMAI FLLESGREFD QNHLEILKDI SHLAAGVINN VQLFNEATRY
     AEEAEALRRG SIAISSSLDY HTVLTEITEQ AKALLRADGS RVHLLDQESG LLRCVIALHP
     HAEEVMQIEL KPGEGLSGHV LLSSEPLLVN RPTDHPHSIQ VPGTPQDEAE VLAIAPMKIR
     KRTMGVMTVQ RDGYTRPFSE PDLRLLSAFA SQAAVAIENA HLYGQIESQA QRLEDEVKAR
     TRELTFSEAR YRSLVETSLT GIYQLDKNAK IAYVNDQLAE MLELEPEEII GRSVVDFLAP
     EYRESVLKWA VARLNGEEPL TEIVEVKLLS WSGRHIPVIL AAGVITNETG IPESISGLVL
     DISTQKRLEA ALRTERDRLE IILRNVGDAV VVTDPSGIIE FVNPAWEHLN GYHAQEALGK
     NANLVKSDEQ DPDFYFQMWD TILAGRVWRG EVINRRKDGS TYEAALTITP VKNESRQIVN
     FVGVQHDISM LKELDRLKSQ FVSDVSHELR TPLTNIRLYL ELLTQTEYDQ RAGRYMETLS
     RESERLSSLI EDLLSLSRLE ADSAPLNKEP VDINRMLSAL TQDREKLATQ YGLELRLECE
     AKLPLVMGDA LLLSQLFTNL LTNALNYTPE GGYILLRTRS QSSGEMIWVV AEVEDTGYGI
     PPMEHSLIFR RFFRGQASKP AAVPGTGLGL AICKEITERH GGKIMVESDG ILGHGSRFTV
     WLPVSG
//
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