ID Q8XNX5_CLOPE Unreviewed; 791 AA.
AC Q8XNX5;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-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=CPE0207 {ECO:0000313|EMBL:BAB79913.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB79913.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB79913.1, 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};
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DR EMBL; BA000016; BAB79913.1; -; Genomic_DNA.
DR RefSeq; WP_011009675.1; NC_003366.1.
DR AlphaFoldDB; Q8XNX5; -.
DR STRING; 195102.gene:10489455; -.
DR KEGG; cpe:CPE0207; -.
DR HOGENOM; CLU_000445_89_20_9; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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:0000313|EMBL:BAB79913.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Transferase {ECO:0000313|EMBL:BAB79913.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 22..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 402..457
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 538..760
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 791 AA; 91325 MW; CFF3D5572CEC598D CRC64;
MDNPIFFHIF NDDKNKLETQ RIIKLSIFIV FSIFFILLID LSYKVLIRKN IEFIPGNSMP
SFSLSLSLIL GTMAYISSLI YYSSTKKDDF FIISLIYMNL SVELLITKGH NLIIFDKFIF
IHAIFRIILL FYVAFNKKGI PPLITKHKII TSIVVFLFSV ITPMINYRIF SNNLFAKDIY
FYATLMTMII ILYIIACIFL SKKSLDDCEL IYSFIIASIL LIALRGLYWI CEVLLPNITL
LKTNNVVLLL TILSFLLAIS GVFNEITAKN KRSSLLQNEL QVFYHLVEFN TSSSIILYDN
KKKVIYTNKT IRERYCKSTK LKDQLKEVEK LFVDSIFIDD SEKNATKALF NKGNWEGKLI
LKNGKIVSAY IQILNVENKN YFAVNLKDIT EEYTLTKNIK RNEQLLSCIN NNVQDLIISV
DNNGLITYVN DSVLKTLNYT YEEIIGMPII NLLGKNDEIL NQLKLEDEED SIKCKLVGKH
SFVYVESIIR TLNDNNEIPY GKVIVAKNLT SKKRLENLAI KFKEAKAYEQ IRNEFFANIS
HELRTPLNII YSTIQLLNSK HETDPMDFNN FYDKYKQGLK INCYRMLRLI NNLIDVSKIE
VGFLKADFTN RDIVFLVENI VSLVIPHSEN KDINIIFDTN VEENIIKCDP VKIERLILNL
LSNAIKFTQN HGEIFVDLNI SKDWVKISIK DNGIGIPKEM QASIFDRFVQ ADKSLKRRNE
GSGIGLSIVK SIAELHDGKI ELISDGIKGS EFIVWLPNVK LNYTEESNNL VDYITDDKNI
ELELSDIYEV H
//
