ID Q8XKS8_CLOPE Unreviewed; 821 AA.
AC Q8XKS8;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 143.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=CPE1316 {ECO:0000313|EMBL:BAB81022.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81022.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB81022.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; BA000016; BAB81022.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8XKS8; -.
DR STRING; 195102.gene:10490579; -.
DR KEGG; cpe:CPE1316; -.
DR HOGENOM; CLU_000445_89_20_9; -.
DR OMA; TEMIFIV; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAB81022.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAB81022.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 431..482
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 569..790
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 821 AA; 95817 MW; 2C1190537DE6ADD4 CRC64;
MNKFLKKEVF LLILNIYLIY NRSTMLNKNG ENLDMLIGLF NNLGIKEKTL KRIAIVTVIL
LSLFFIKGLN LICALNRDLF KDVSVVYAAE EIIVMTQIIL CIMILSICFI YYRGLKRKEF
FSISLVYVSI ITEMIFIVLT GKIVENQVYD LNLFSLLFRG ILLLLAVLCL ENFDAFIRKY
KKLTLVFVIL VTIILQILNV NYNIGIYTYN FIYNLTLVLI VLTYISCIIF CLVRIFQFRE
ITYLVIMISA SLMLLKLVYG LSLSITNNNL IKINIVFFNF ISFMSFVFGM FFDLLQVIKN
KNFMQEELSA FFNLIEFDCN SEVVVLSNNL KVLYANEKCR SKRISPKNRE NKTYIDLEKQ
IKGFLYDKNI ICIESVLRNS KEWKGIIKLN EEDEVVKVNL QRIKKEKNLY YVLRINDITE
EYKMEKNLKL EEQRLRGVTE NIKDLIFTID VEGKISYVNK AVIDVLGYSE EELIGKNYYD
LLLVESNLNI IDSKYFNEDK ILTIDKVRSK KGLVQLESIS SRIKDNKNNT LGWVRVARNI
EDVREIEILK NKFEEIKQYD KVRSEFFANL SHELRTPINI IYSCIQLLNT SKKNKANFAN
LYDKYEKTLK QNCFRMLRLV NNLIDITKID SGFIKMDFIN YDIIKLTEDI TMSVIPYVES
KNIDIIFDTD YEELEIRCDP DKIERIILNL LSNAIKFTEP GGKIEVSIFA DEAWVDIRVK
DTGIGIPSHM KEFIFERFIQ NDKSLNRNKE GSGIGLSLVK SLVELHEGKV FLRESNESGS
EFSILLPNVK LENDVCENGS LDYKTEVEKI SIEFADIYEI Y
//