ID A0A117SFY1_9FIRM Unreviewed; 584 AA.
AC A0A117SFY1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=APF77_03040 {ECO:0000313|EMBL:KUO69215.1};
OS Clostridia bacterium BRH_c25.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO69215.1, ECO:0000313|Proteomes:UP000057710};
RN [1] {ECO:0000313|EMBL:KUO69215.1, ECO:0000313|Proteomes:UP000057710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO69215.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO69215.1}.
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DR EMBL; LOES01000232; KUO69215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SFY1; -.
DR STRING; 1734399.APF77_03040; -.
DR Proteomes; UP000057710; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR029151; Sensor-like_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 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 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 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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..364
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 347..578
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 352..386
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 584 AA; 66746 MW; E7FC1DCD0712795D CRC64;
MNRIKVFNSL RVKLGIIAIV LIAIPLLVVS FTYSSTVKDI IKNKYTETAI QSVFETGEKL
DFILDDIREF STVITSNSEL LYMLNHKYDF RADEYGRVLR SFITSRDDIE VIDLVLADAY
YSVGAKKINR LERISPQLEK SSGQPLWLPT KSEEIEILSG KFKKNYFTLA RKVVDFNTLE
AYGYLLIDLE EVILEQAYSG ILDSEKVEVL ICDDQGNIIS HSDKKKIGSS IKGEPYANEV
LADINGHNYV QYKTNIDNVA IYSTIENNGW KIIKTISTDY LYEEINRIQR YFNVGGVIYG
LVIILYILFF SFRYTEPMMK MMSVIKKVEQ GDLTVRTEVK SNDEVGQLGN SLNNMIGEMQ
VLIEQLIREE QEKKEVELEA LHAQINPHFL YNTLNTIKWM AKIQGNSSVS KAITALVKLL
RISTNLGRGM ISLKEEIDYV MNYIVIQKLR FRKSIDIAYN IDDDCMNLTV PKLILQPIVE
NSIIHGMEDE QQELNIEING FVKEDKLIIE VQDDGPGIED EILKDILRNA SDKDKFSKVG
LNNVNQRIKL YCGADFGLKV ETELGMGTKV VVTLPINPMY IERT
//