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Database: UniProt
Entry: Q0SHD3_RHOJR
LinkDB: Q0SHD3_RHOJR
Original site: Q0SHD3_RHOJR 
ID   Q0SHD3_RHOJR            Unreviewed;       845 AA.
AC   Q0SHD3;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=kdpD {ECO:0000313|EMBL:ABG93053.1};
GN   OrderedLocusNames=RHA1_ro01229 {ECO:0000313|EMBL:ABG93053.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG93053.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG93053.1; -; Genomic_DNA.
DR   RefSeq; WP_011594313.1; NC_008268.1.
DR   AlphaFoldDB; Q0SHD3; -.
DR   KEGG; rha:RHA1_ro01229; -.
DR   PATRIC; fig|101510.16.peg.1253; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_113_1_11; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005886; C:plasma 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   CDD; cd01987; USP_OKCHK; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   InterPro; IPR006016; UspA.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   Pfam; PF00582; Usp; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABG93053.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABG93053.1};
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        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        467..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          624..841
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   845 AA;  89428 MW;  3A2A5B908516CCE5 CRC64;
     MSGTGTDGER RDAEHRRGEL RIYLGAAPGV GKTFAMLGEA HRRRERGCDV VAAVVETHGR
     DRTAAQLGDL ELVPPKLIAY RGTLGRELDV EAVLARRPAL VLVDELAHTN TPGSVHEKRW
     QDVEILLAAG IDVLSTLNVQ HLESLNDVVQ RITGVVQQET VPDEVVRAAT QVELVDITPE
     ALRRRLSHGN IYAADKVDAA LSNYFRKGNL TALRELALLW VADQVDAALA KYRAENKITD
     TWEARERVVV AVTGGLESET LVRRAGRIAS RSSAELIVVH VVRGDGLAGV SAPEMGKVRT
     LAASIGASLH SVVGDDVPTT LLDFARTANA TQLVLGTSRR SRWARIFDEG IGASVLHQSG
     SIDVHMVTHG ESHRPRRLSP VGSRSRTAIA WIAAVLVPSV ATLVMSAVDR WLGLVGEGAL
     FFIVVLLVSL LGGVAPAAFS ALISGLFLNY FFTPPVRSFT IAEPDNFITT VVLLVVAVAV
     AVLVDAAAKR SREARRASQE AELLALFAGS VLRGADLGTL LEKVRETYGQ DSVSVLHRDR
     GPVGSVGPHP PVSVDDADTV CEVGEGEYAL ALRGSELHAR DRRVLLAVAN QAVGMIRQTE
     LAQEAGQAQA LAEADRLRRS LLSAVSHDLR TPLAAVKAAA SSLRSDDVDF SPEDTAELLA
     TIEESADVLT SLVGNLLDSS RLAAGVVTPT LRPVYLDEVV HRALVGLGIG GRTGTRARER
     VEVDVGTVAA MADSGLLERV LANLIDNALR YGEDSVIRVG AAAVGDRAVV TVADTGPGIP
     RGRADEMFAP FQRLGDRDTT TGVGLGLSVV RGFVDAMGGT ISATDTPGGG LTMVVELAGA
     GGAHP
//
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