ID A0A1M3KH26_9CHLR Unreviewed; 493 AA.
AC A0A1M3KH26;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=BGO78_16725 {ECO:0000313|EMBL:OJX47123.1};
OS Chloroflexi bacterium 44-23.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895927 {ECO:0000313|EMBL:OJX47123.1, ECO:0000313|Proteomes:UP000184201};
RN [1] {ECO:0000313|EMBL:OJX47123.1, ECO:0000313|Proteomes:UP000184201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-23 {ECO:0000313|EMBL:OJX47123.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJX47123.1}.
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DR EMBL; MKUW01000006; OJX47123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3KH26; -.
DR STRING; 1895927.BGO78_16725; -.
DR Proteomes; UP000184201; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 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; IPR033463; sCache_3.
DR InterPro; IPR017204; Sig_transdc_His_kin_STH3221.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR PIRSF; PIRSF037433; STHK_STH3221_prd; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..259
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 289..478
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 250..289
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 493 AA; 54811 MW; 2617F4163E7AC5D7 CRC64;
MWKKSNNFSR INSIFNRFWE IAGAVRIQTK ILGLALGLVI LVGFGNTLQT RSVLSKNMEA
QLREQSISVA RDLAARSADP ILLNNLLELQ DILLETKSNN DNFQYAFILD QNRQVLAHTF
GEGFPVGLLD LNIPTDLAYN QTVLIETNMG YIYDTAVPIL NGKAGIARIG LSNEIVQKAV
SQVTLQSISF TLLGVLFGVA VAFFLTRILA RPILELVEAT RSVSRGDFSK RIHPWAKDEL
GTLAQAFNKM SEDLAQVHDL RQEREGLQRQ LLEKVISTQE EERRRIAREL HDSTSQSLTS
LLVGLRMLEA NSTDTDRKQA SDLRNIAAQT LDEVHALAMQ LRPRSLDDLG LSAALERLVF
DWQSRNKVPV DLAITLGGLR LSEGVETALY RIIQETLTNV VRHAQAHSVS ILVERRNDII
IAVIEDDGKG FEVSTTKGEL HLGLLGMRER AELLGGRLTI ESNAGRGTSV FVEIPIREEE
NSIGEEKTRS VSG
//
