ID A0A0P6WWT3_9CHLR Unreviewed; 526 AA.
AC A0A0P6WWT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ADM99_03265 {ECO:0000313|EMBL:KPL73257.1};
OS Leptolinea tardivitalis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Leptolinea.
OX NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL73257.1, ECO:0000313|Proteomes:UP000050430};
RN [1] {ECO:0000313|EMBL:KPL73257.1, ECO:0000313|Proteomes:UP000050430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL73257.1,
RC ECO:0000313|Proteomes:UP000050430};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL Submitted (JUL-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:KPL73257.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGCK01000006; KPL73257.1; -; Genomic_DNA.
DR RefSeq; WP_062421662.1; NZ_BBYA01000009.1.
DR AlphaFoldDB; A0A0P6WWT3; -.
DR STRING; 229920.ADM99_03265; -.
DR PATRIC; fig|229920.5.peg.2281; -.
DR Proteomes; UP000050430; 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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050430};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 235..287
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 309..526
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 526 AA; 59462 MW; E4FB5C619D0B86CA CRC64;
MKPRMRLSSF LLSVQPWQGL LEAWLVGCLI LGLTSHLEGY TDPFVFQTAM FFLCGSCGMW
AVLRIRLPDG GWKKQTFWEF CVGLALSFMM VFALRLCGLF LHWDAIWRLT TWDEWQVLLL
FGLTGPGYFF TRGGLRLWLR WNRMRKQRMR WSITHAHLLV ALFIAFIFAF LAFLITPYST
TALRIWEKTR DPMASLLTGL LVTFFPALTL IVVGMGATLF FILPPSALFS YFVARRTTRR
LEALTVTTAA LRSGDYQARV TVEGEDEVAH LQSDFNAMAD KLSLTLMDLN EEKDRVAQIL
ESKRELVANV SHELRTPVAT LRAAIESMLA HWQETPSEEL HRKVELMENE IQQLSGLIDD
LFTLSQVDVD HLALDCIRVD LHSLINQAVD SFSPLAWQSG RVEVTAQLPK ELPFVNADPR
RLNQVILNLL RNGVRHTPPG GIVAIQAEKV ERYVQIDVRD TGEGIDPEDI GHIFERFYRG
KNATSESAGL GLALVKELIE AMGGSITVES QPGQGSCFYV RIPAIA
//