ID D7GTJ9_9FIRM Unreviewed; 382 AA.
AC D7GTJ9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CK3_14340 {ECO:0000313|EMBL:CBL41141.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41141.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL41141.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41141.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL41141.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41141.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929062; CBL41141.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GTJ9; -.
DR KEGG; bprs:CK3_14340; -.
DR PATRIC; fig|245014.3.peg.3142; -.
DR HOGENOM; CLU_000445_89_3_9; -.
DR BioCyc; BBAC245014:G1314-1227-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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; 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:CBL41141.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..158
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 166..378
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 382 AA; 42541 MW; 867292DC070DC42C CRC64;
MKRLSLQWRI TLMTVLLIGI TCVAMNLLLC SSGVYYMDTI ADSLQGGTVI LNDGGAASFD
PQLIAPNEEL TIVVDGVQGR FRTTNWYITA AVTLLSGILA YFVSGRALKP LRSFTSQVEQ
VQLNNLADMR IDEDAISEFR QLSRSFNQML ERLNNAFSAQ RQFTGNAAHE LRTPLALMQA
QLELFSAEHP DVRPETAEFL TLLREQTERL IQLTRTLLEM SNLRQVERNE RIQLAPMIEE
IFTDLAPLSD KLGVTLTAEG DGIMTGSDAL IYRLIFNLTE NAVKYNRPGG SVRVSVTQEL
EKLLLRVSDT GCGIPEVYQR SIFQPFFRVD KSRSREYGGA GLGLSLVWEI ADLHGGSVWV
EKSSEKGTTI AVGLPTQQST KR
//