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Database: UniProt
Entry: C0R4Z5_WOLWR
LinkDB: C0R4Z5_WOLWR
Original site: C0R4Z5_WOLWR 
ID   C0R4Z5_WOLWR            Unreviewed;       475 AA.
AC   C0R4Z5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=WRi_013110 {ECO:0000313|EMBL:ACN95987.1};
OS   Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=66084 {ECO:0000313|EMBL:ACN95987.1, ECO:0000313|Proteomes:UP000001293};
RN   [1] {ECO:0000313|EMBL:ACN95987.1, ECO:0000313|Proteomes:UP000001293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wRi {ECO:0000313|Proteomes:UP000001293};
RX   PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA   Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA   Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA   Andersson S.G.;
RT   "The mosaic genome structure of the Wolbachia wRi strain infecting
RT   Drosophila simulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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; CP001391; ACN95987.1; -; Genomic_DNA.
DR   RefSeq; WP_006280108.1; NZ_MKIF01000109.1.
DR   AlphaFoldDB; C0R4Z5; -.
DR   STRING; 66084.WRi_013110; -.
DR   KEGG; wri:WRi_013110; -.
DR   HOGENOM; CLU_040413_0_0_5; -.
DR   Proteomes; UP000001293; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ACN95987.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:ACN95987.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          246..466
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   475 AA;  54540 MW;  6612EFDC3743BCFD CRC64;
     MYKIGKLMFS ALGKNKYTKV IALFSSIFMI LFSVIYCNYL LRSNFLSSYR DSSVNLKSVL
     ENGIIKKYHY LLIEKHHIKY KNFDYINQLV KLRAELLQSV SKVKDFSLIL YDQNGRIIFS
     NFNTQDYDYE QLLTNDEIDK LLSDQEILYT TGNTLTSIFP IFHENSAKPS FFLKILRSYN
     NSYVIAYGLF LIFLGLLLII LILIMFYLHF SNTKMLAKQH KTNIELQQIK EALEQENANK
     LKFFASVTHE LRTPLNAIIG FAELIKNETL GSMDDSQYKE YADDIYNAGT HLLALINDVL
     DFSKAESSSL TVEKVKFNLN KIIDSCVNML LPKLKEAGIN LKKEMTNKQL LVIADPKRMK
     QVIINLLSNS IKFTPKDGLI RMVIKENIEK NLLTIEFHDN GIGIMQQDIY KVMSVFGQAD
     SGYRNEGTGI GLPLSKKLVE LMGGTFDIKS EAKLGTTITL NFFYEEQTCE DSIDF
//
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