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Database: UniProt
Entry: Q8XIL8_CLOPE
LinkDB: Q8XIL8_CLOPE
Original site: Q8XIL8_CLOPE 
ID   Q8XIL8_CLOPE            Unreviewed;       482 AA.
AC   Q8XIL8;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Histidine protein kinase SaeS {ECO:0000256|ARBA:ARBA00044126};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   AltName: Full=Sensor protein SaeS {ECO:0000256|ARBA:ARBA00044288};
DE   AltName: Full=Staphylococcus exoprotein expression protein S {ECO:0000256|ARBA:ARBA00044353};
GN   Name=virJ {ECO:0000313|EMBL:BAB81804.1};
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81804.1, ECO:0000313|Proteomes:UP000000818};
RN   [1] {ECO:0000313|EMBL:BAB81804.1, 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   -!- FUNCTION: Member of the two-component regulatory system SaeR/SaeS
CC       involved in the regulation of staphylococcal virulence factors in a
CC       strain-dependent fashion. Probably functions as a membrane-associated
CC       protein kinase that upon sensing the appropriate signal,
CC       autophosphorylates and in turn activates the cytosolic response
CC       regulator SaeR. {ECO:0000256|ARBA:ARBA00043865}.
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; BA000016; BAB81804.1; -; Genomic_DNA.
DR   RefSeq; WP_011010762.1; NC_003366.1.
DR   AlphaFoldDB; Q8XIL8; -.
DR   STRING; 195102.gene:10491368; -.
DR   KEGG; cpe:CPE2098; -.
DR   HOGENOM; CLU_000445_89_6_9; -.
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   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:SF13; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAB81804.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW   Transferase {ECO:0000256|ARBA: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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          196..248
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          270..482
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          236..263
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   482 AA;  56004 MW;  8C9AD7F6050A5702 CRC64;
     MKVKHKFSGG FLIIFLIAFI ILNCFLGKAF INYHENKIKN EMDSLYKSSY SILRLYFQVN
     NLEGNKGNFN RYIPKISNDI SEQGKCQIDV FNEALEKEYS YYLDDFSFDY EKDGGYDVLK
     EANKNKAALN IYRDENAVKA YLAFPVYVDE SFLGNILLSK DYSKEYLELR DLMSNIKFIV
     SITFLLILIF TYFLFERIIN PLNYIKNSFK RIGDGDFKIN LKVNSKDEIG DLACGVNKMA
     NKIEEQIEKI NEEKEKVLTL EKTRTEFFNN ITHELKTPLT NISGYAQIMS EEDFHDNDFR
     KFALERINKE SKRMHELIVS LIEISKNKSD IEGGEIENVN LKTLIEDLCE DFKVKGDKQG
     ICISNNLEDI EFMCREDEIR RIIINLLDNA IKYSIKGSEI NISLFKDKEE KHIEIENFSD
     EISSEGVEKI FEPFYRENTK KSRELGGNGL GLYICSELVK KYGGDISFSY SNGKVKVSII
     FK
//
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