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Database: UniProt
Entry: Q8XKS8_CLOPE
LinkDB: Q8XKS8_CLOPE
Original site: Q8XKS8_CLOPE 
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
//
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