ID A0A3Q8T8A1_9RICK Unreviewed; 478 AA.
AC A0A3Q8T8A1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EF513_00290 {ECO:0000313|EMBL:AZL15009.1};
OS Rickettsiales endosymbiont of Stachyamoeba lipophora.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=2486578 {ECO:0000313|EMBL:AZL15009.1, ECO:0000313|Proteomes:UP000267655};
RN [1] {ECO:0000313|EMBL:AZL15009.1, ECO:0000313|Proteomes:UP000267655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RICK01 {ECO:0000313|EMBL:AZL15009.1,
RC ECO:0000313|Proteomes:UP000267655};
RA Munoz-Gomez S.A., Hess S., Burger G., Lang B.F., Susko E., Slamovits C.H.,
RA Roger A.J.;
RT "An updated phylogeny of the Alphaproteobacteria reveals that the parasitic
RT Rickettsiales and Holosporales have independent origins.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP033611; AZL15009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8T8A1; -.
DR KEGG; ren:EF513_00290; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000267655; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000267655};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 280..478
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 478 AA; 55866 MW; A33D0BD6AA9AD1B8 CRC64;
MFKLYALELK LKMTLKNLNI LSPYVTRDMG YLYKYLYMKN IKIIVKKLQP QSLFARFLAI
ILIPWFTLQA ITIYIFFDRH WEGVSYYMKQ SLINDIRIIV RLYNDQLYQE EQIIDYAANY
LSFEIKKISR QDAVNLINKS NKHKILQHLS RELQGVLDEE FGLYQDKQDQ DIIIITKQRN
NYYLIEIPRK RIITPTIGIF LTWIVSSAII LIVIAIIFMR NQVRSIIKLA TAAESFGRGQ
DISNFKPEGA REVRIAGINF LKMKDRIEQQ FTQRTLMLAG VSHDLKTPLT RIKLRLAMLP
ENSEIEAIQE DINEMQYMIS EYLELISSQD ELEDFNEIDI IEMIKDIIKK FDIHNIEFSP
QFAELQILIK PFSLKRAIIN IIDNAFKHGD KVWIDIRKDF ETIKIIIEDN GPGIPKEEED
KIFKAFYRAD YARNLNKAGA GLGLAISQNI ILTHGGNIYV SKRNYKLNGA SFVIELPS
//
