ID A0A1F8R3S2_9CHLR Unreviewed; 481 AA.
AC A0A1F8R3S2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=A2W36_05920 {ECO:0000313|EMBL:OGO41941.1};
OS Chloroflexi bacterium RBG_16_58_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797654 {ECO:0000313|EMBL:OGO41941.1, ECO:0000313|Proteomes:UP000180315};
RN [1] {ECO:0000313|EMBL:OGO41941.1, ECO:0000313|Proteomes:UP000180315}
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:OGO41941.1}.
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DR EMBL; MGNV01000039; OGO41941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8R3S2; -.
DR Proteomes; UP000180315; 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; cd00075; HATPase; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..229
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 237..452
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 481 AA; 52994 MW; 2151EE005D54B5BF CRC64;
MLHSLRFRLL LTLMIVTGAA LGIIALYASQ VTTREFERSV VGILRYQDPR LEVKIIMIQK
TVTQLTGESS IWVDLQDLLE QMGASARSRF VMADLYGTVY ADSENKMIGY RMDTKQSKPI
AVYLIEGIPI LMYFEPLDVP DLEKIGKEFS NSVNRSLLLA ILGAGGLALL MTLALSRSFL
RPVDALREAA RRMGSGDLSQ RVDMQAKGEV GELAKAFNSM ADNLERLELL RRTMVTDIAH
ELRTPLSNVR GYLEAIQDGM VQPMPEVINS LHEEAMLLNR LVNDLQELAL AEAGKLKIET
QPLDTRQMVL RAAGREQQNA SQKKLRLRTE LPAELPPVCA DPERLGQILH NLLDNAIQHT
PEGGEIAITA ERQAGFIEIK VQDTGSGIAA EHLPFIFERF YRADQSRSRT TGGAGLGLAI
VKQLVEAQGG EVSAYSKVGQ GTTISFSLPI AQEGEAVAIE EAAASTRIRN QQPPIDQHST
P
//
