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Database: UniProt
Entry: A0A117SFY1_9FIRM
LinkDB: A0A117SFY1_9FIRM
Original site: A0A117SFY1_9FIRM 
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
//
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