ID A0A1F8LVR6_9CHLR Unreviewed; 644 AA.
AC A0A1F8LVR6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2Y88_00415 {ECO:0000313|EMBL:OGN90440.1};
OS Chloroflexi bacterium RBG_13_48_10.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797620 {ECO:0000313|EMBL:OGN90440.1, ECO:0000313|Proteomes:UP000177902};
RN [1] {ECO:0000313|EMBL:OGN90440.1, ECO:0000313|Proteomes:UP000177902}
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:OGN90440.1}.
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DR EMBL; MGMN01000177; OGN90440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8LVR6; -.
DR Proteomes; UP000177902; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 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 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; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF17202; sCache_3_3; 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; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 323..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..399
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 424..635
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 644 AA; 71143 MW; 473F29DA7D02DE61 CRC64;
MPIAHKLILS FLLISIITNV IFTIAGIRLM ANRVVAEAQE RIRNDLNAAR EIYLSEARHI
NDVIRLTARR PIIEDALTSG ITAAITDDLI NVKQSEGLDI LTLTDQTGTI VFRTNAPLTK
GDSLAQDEVI NYVIKYNKTV TTSSILSAER LQVESPILAG KAYLELIDTP MARPLTKSDQ
TSGMMLVSAS PVFDSNRQLI GILYGGVLLN RNYDLVDKIK QTIFQNVVYK GKDIGTTTIF
QDDVRIATNV LNSDGSRAIG TRIAEDVYNQ VVVRGEPWVD RAYVVNNWYI TAYEPIKNIN
DDVIGILYVG ILEQKYVDIR NQAVLAFLII SIFGVLFSIG LSSLLSRSIS VPVHKLVVAS
KELANGNLDV KVEKTSNDEI GVLADAYNAM STALRERDEQ LKEFTRKKFM ESERLALIGQ
LAANVAHELN NPLQGIVTYS HLLLERSTID DPIKQTLQKI VVQANRSRDI IRGLLDFSRQ
RKPDKTLSNI NNLLNESVSF LENQALMQNV QVITQLVDDL PSVVIDPSQV QRVFINMIVN
AAEAMNGNGQ LTVSTKRDVV GECIEISFTD TGMGIKEENL EKIFDPFFTT KETGHGVGLG
LAISYGIIKE HGGTISVESE VGKGTTFIIR LPINVTKSGV ENGQ
//
