ID Q97E95_CLOAB Unreviewed; 475 AA.
AC Q97E95;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=CA_C3219 {ECO:0000313|EMBL:AAK81155.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK81155.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK81155.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81155.1; -; Genomic_DNA.
DR PIR; H97295; H97295.
DR RefSeq; NP_349815.1; NC_003030.1.
DR RefSeq; WP_010966495.1; NC_003030.1.
DR AlphaFoldDB; Q97E95; -.
DR STRING; 272562.CA_C3219; -.
DR GeneID; 44999715; -.
DR KEGG; cac:CA_C3219; -.
DR PATRIC; fig|272562.8.peg.3398; -.
DR eggNOG; COG2770; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000000814; 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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 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:AAK81155.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 259..475
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 475 AA; 54334 MW; DF35FC32567E8429 CRC64;
MRKGIFSKMI ATYTGIIAIS FVVTSAVLSF WFQNFYFSQK RSQITTEAKY VQAVAFQYIE
GNMSVARVNE TLKEVVAYIN TDIGADIVVM DMYGYVYAVS NPKYDYLVGT QVNTKDLNEI
AKNQEAIEKT VDYSEIFKKP VRLYEIPMIF NKSFEGVIMI ATPASEVKHS VNRVYQIIWF
SAIIAIIAAC IIIYYFSQKI IISPLKNIND VARKIAKGEV EKRVNIESND EIGELGESFN
FMANAIEKSE KNRREFISNV SHEIRSPITS IKGFIGGMLD GVIPKEKERY YLSLTYDEIN
RLTRLVNDLL DLSSIEAGHL KLNLTKIDIN EIIRFTVLKF ETKIKEKKLN VDVCFNNDKV
YVIADKDRIS QVVTNLIDNA VKYVYAEGEI KISTKERYNK AYITIYNNGP QIPEEDFNHI
WDRFYKSDKA RTTKMSTGLG LPIVRSILTE HGQDINVINK KEGGVEFTFT LKLAK
//
