ID A0A1G0XJK7_9BACT Unreviewed; 1121 AA.
AC A0A1G0XJK7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2020_03475 {ECO:0000313|EMBL:OGV33882.1};
OS Lentisphaerae bacterium GWF2_45_14.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798572 {ECO:0000313|EMBL:OGV33882.1, ECO:0000313|Proteomes:UP000176538};
RN [1] {ECO:0000313|EMBL:OGV33882.1, ECO:0000313|Proteomes:UP000176538}
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:OGV33882.1}.
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DR EMBL; MHBG01000078; OGV33882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XJK7; -.
DR STRING; 1798572.A2020_03475; -.
DR Proteomes; UP000176538; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 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); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 400..452
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 470..539
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 592..655
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 669..721
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 738..960
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 992..1111
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 440..477
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1042
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1121 AA; 127365 MW; 55F65B45FEC6627D CRC64;
MIFYSGHSSG ERIFRGIMAF RINLTQKMII IFTVILVVFF FLLGSRLRNM LEEYMISNAN
TLIRTTVLEE KRLIDSHFRD IEKIGETSAE YFETLVKDAL TREEDPLFNK KYKMKDGAIR
TNPAASDKKD ISGVFVSSLA NLSSSDRKII SAMELYFSSY SKGMSKSLLD NYFISKNQFI
RIYPPKWAME VESDHDFTKD IFFSTADPEN NPSRRQVWTP VYYDSIWKQW MTSLLVPIYV
RDEFIGIIGN DLILNSIYKT ILGKKYYSSG YGFIFDSNEN IIIHQKYMTT LQSSGKTMGQ
RFTLFKIDDK TMGKNIKSAA DALKRGNLRN RGVFFTKIKV NGEKYFFHAC RLDFMDWNYG
IMLPESAVLE NVQKFKAQYF NSVLGFAILF LLAVILVIWH YVIAPVTEIF KAAQRLGKAD
FDYRIPYHSR DEISDLAIVL NNAAANLKTL TASKDTLNKQ IEERIKTEEE LEKFKAASDG
ANCGIAILTA DGAFAYINDY YANIHGYSKN EATGTNMKNF HSHDQMKSVN RLIKKLEAGE
SVTSEEIWHK HKDGKNFPML MSWYKIKETR GGTDLMAATA IEISAWKNAE QRRIELERVI
NLSNAIVFVW ENEQGWPIKY VSENVKNILG YSSELFYSGQ LKFFDIICEE DLPTVSTPIP
NSGKYPKFLS RQYRIRKKSG DFIWVDDRIL VRRNRAGKIT LLEGITIDIT DRKKTEELDR
QKSVAENANK AKSEFIANMS HEIRTPMNAI LGFTEIVLAS AGISEENKTA LGVVKDSGDA
LLRIINDILD ISKIEAGKME IVPYPFSLRQ SMGMSLKSFE LSCRNNGLEF ISKIPPDIPD
LLLGDSIRLR QVLVNLVGNA AKFTARGGIY VNVSAENNDG ENIDIRFEVK DTGIGIPPDK
KEIIFEAFMQ ADSSTTRQYG GTGLGLAICA RIIKMMGGRI WVESEMEKGS NFFFTVPFKI
CTENIEDAHT FPSATEIEDS GQKEKTDISD IRIMLAEDNF GNQELIKMIF SLNAVNNFKV
VNNGIEAIEA FSREKFDIVL MDIHMPGMNG FEACQKIREM NRATGKQCII IALTASTGED
ERRKCMEGGM DDYLSKPITE KDLIEKIEAW CNASVGFLNS K
//
