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Database: UniProt
Entry: A5MZR5_CLOK5
LinkDB: A5MZR5_CLOK5
Original site: A5MZR5_CLOK5 
ID   A5MZR5_CLOK5            Unreviewed;       509 AA.
AC   A5MZR5;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=CKL_2349 {ECO:0000313|EMBL:EDK34361.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK34361.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK34361.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK34361.1; -; Genomic_DNA.
DR   RefSeq; WP_012102693.1; NC_009706.1.
DR   AlphaFoldDB; A5MZR5; -.
DR   STRING; 431943.CKL_2349; -.
DR   KEGG; ckl:CKL_2349; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   Proteomes; UP000002411; 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; 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   PANTHER; PTHR45453:SF3; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
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:EDK34361.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002411};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..265
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          294..509
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   509 AA;  59085 MW;  A2DD8E166F2CCC2E CRC64;
     MKIRSIIYKN KLIEKIRKNI TWKLFIVTAL IFTIFISSTL TFQSLFFGKF YINKKERIIE
     SEVKKFRALY NNTENDNEVT ELIRKFEDSN NAKIVIMDSE GKINFITKLD DRGYDEERIK
     IIQNIIVTWI RDSNLLDEIK RYNKSITFIT EKKINGTKNI ITVVPDNNRQ EILFAVTSLQ
     PVDEASSVIK EFYIYFYMGA IVLILISSLI YTNTVSKPLV KLNDTAKKMA LMDFSKKCTV
     KSRDEIGNLA DTLNFLAYNL DKALTSLKEA NVKLEKDIEK EREIERIRKE FIASASHELK
     TPINLIGGYA EGLKDNIFES SEKDHYIDII IDESNKMANL VADMLNLSHL ESGVLKLNKE
     EFFMDEFIMY SLKKFSKVIK DKNITINFNM IPKIRVYADW DKMEQVIDNF TTNAIKNTEE
     GGYINFVIED KEKDKIIVSI ENTGENIPEG ELNNLWNSFY KVDKSRNREL GGTGIGLSIV
     KNILMLHDFQ YGVENTDTGV RFYFIMDKI
//
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