ID A0A1G5FSA8_9FIRM Unreviewed; 485 AA.
AC A0A1G5FSA8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02910292_01668 {ECO:0000313|EMBL:SCY42205.1};
OS Lachnospiraceae bacterium XBB2008.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520826 {ECO:0000313|EMBL:SCY42205.1, ECO:0000313|Proteomes:UP000199089};
RN [1] {ECO:0000313|EMBL:SCY42205.1, ECO:0000313|Proteomes:UP000199089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBB2008 {ECO:0000313|EMBL:SCY42205.1,
RC ECO:0000313|Proteomes:UP000199089};
RA de Groot N.N.;
RL Submitted (OCT-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};
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DR EMBL; FMVL01000006; SCY42205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5FSA8; -.
DR STRING; 1520826.SAMN02910292_01668; -.
DR Proteomes; UP000199089; 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 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; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SCY42205.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199089};
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 22..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 377..482
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 485 AA; 55754 MW; D2489A28BE8C7912 CRC64;
MKLTQRIKTY YRNLSLADKL RLSYFAVLIP MLILVVISVF NMYFGNARYK DIIESAVVAS
EFSLDFKEDF DYETYLLVVE NKTIEESAVY PMLDEAGRIV DRLDELTKDD EDDSRLSSAK
QYLTNLHKYI ERIELNLLTG NMYEENMLIW ENDVQIVTAL LSETLNEYIY NEVRNIQEAR
DDLEHKTIIS IVMTAVGAVI LLGCTFLFSI LIPRSIIRPI YEIRDVTGQV AEGNLSVRTH
IEYGDEVKEL GESLNVMIDK IEALLDQVTV EQERLHHAEL ELLQAQINPH FLYNTLDTIV
WLAESGEQSK VVSMVGSLSK FFRTSLNQGK DNITIGEELQ HAGSYLEIQQ VRYQDILSYD
IAVPEKLWKY MIPKITIQPL IENALYHGIK NKRGMGCIRV TGEAYEDHFC IYVSDDGIGM
SEERLEKIRN RISHMDPSKG EIFGLYNVNE RIRLRAGDDY GISIDSKYGY GTTVCIKLPY
MVSEA
//
