ID A0A1H3EMJ7_9FIRM Unreviewed; 456 AA.
AC A0A1H3EMJ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05660923_02957 {ECO:0000313|EMBL:SDX79996.1};
OS Tepidimicrobium xylanilyticum.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC Tepidimicrobium.
OX NCBI_TaxID=1123352 {ECO:0000313|EMBL:SDX79996.1, ECO:0000313|Proteomes:UP000198828};
RN [1] {ECO:0000313|EMBL:SDX79996.1, ECO:0000313|Proteomes:UP000198828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23310 {ECO:0000313|EMBL:SDX79996.1,
RC ECO:0000313|Proteomes:UP000198828};
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; FNNG01000021; SDX79996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3EMJ7; -.
DR Proteomes; UP000198828; 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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF14; SENSOR HISTIDINE KINASE CSSS; 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, ECO:0000313|EMBL:SDX79996.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000198828};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW 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 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..243
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 251..456
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 456 AA; 53137 MW; D70E8B6B053A8F35 CRC64;
MINKMKNWPL SIQIWIVFAT ITLGISLILS FILPLTLKDF FTNEIYITIE SAQTLLFNQY
DLRSIMDLLE SQGPEKSRQT LENIRTVNHF IVYEDSPIIF PYTFPLDFLN EVRNQALTQK
NNSERYSGKV GTEKIFYVIT KGKALNQNAY LVSYMWDSYR EDLVQTLFRK LAIAMFLVFI
LSWIPAILLA RHLSSPLVSL EKRVGKLANN EWDEPVELDR SDEIGKLGES IERLRNQLIY
QQEMQQSFLQ HVSHELKTPV MVIRSFSQAI RDGIYPKGDL NCSVKVIDEE AERLEKRIRN
LLYITKLDYL NNYNILYAIF SLDELIKDVI DRLSWSRTDI DWRLDLPPTN IKGDVEQWRV
VVENLLDNQI RYAKNSISIS LKNIDDKVLL RFWNNGPNIE PETLNSLFTK FNKGYKGEFG
LGLAIAQRII TLHGGKIWAE NEKEEGVSFY VEIPMD
//
