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Database: UniProt
Entry: K0I024_9BURK
LinkDB: K0I024_9BURK
Original site: K0I024_9BURK 
ID   K0I024_9BURK            Unreviewed;       460 AA.
AC   K0I024;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C380_13555 {ECO:0000313|EMBL:AFU46412.1};
OS   Acidovorax sp. KKS102.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU46412.1, ECO:0000313|Proteomes:UP000006306};
RN   [1] {ECO:0000313|EMBL:AFU46412.1, ECO:0000313|Proteomes:UP000006306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KKS102 {ECO:0000313|EMBL:AFU46412.1,
RC   ECO:0000313|Proteomes:UP000006306};
RX   PubMed=23209225; DOI=10.1128/JB.01848-12;
RA   Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT   Polychlorinated-Biphenyl Degrader.";
RL   J. Bacteriol. 194:6970-6971(2012).
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; CP003872; AFU46412.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0I024; -.
DR   STRING; 358220.C380_13555; -.
DR   KEGG; ack:C380_13555; -.
DR   PATRIC; fig|358220.3.peg.2766; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG2770; Bacteria.
DR   HOGENOM; CLU_000445_89_27_4; -.
DR   OrthoDB; 9804645at2; -.
DR   Proteomes; UP000006306; 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   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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:AFU46412.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        27..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          183..238
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          246..460
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   460 AA;  51314 MW;  A28196E7F2A0BC33 CRC64;
     MKKICSPVHD PNCPWHRRAR HAVGHSLRIR LVLVFMALAV AVAVTFMGGV QKAVSVGWRE
     AARPLLMDYV DRLAAEIGSP PSIERAQAIA NRLPLTLRID GPQIHWASHP DQQNPDWMSD
     KVRQESRWTG DENGHSLLRR TTADGHHIEF GLNALSWDKR PRIAWGTLTV LLLLTALAYV
     YVRHLLRPLD DIRQGAQRFG NGNFAQPIPV RHAHRPDELG QLAETINTMG DDIHQMLEAK
     RALLLAMSHE LRSPLTRARL NTELLPETAD VQPQRLALMR DLGEMAGLIT DLLESERLAG
     RHAALHREPT DVAELAREVV ADLCSRHAGA SDIALHAAPD LPAVRLDRSR LRLLLRNLLD
     NSLRHSESGA FPPELHLRLV DEGRVLELEV RDHGRGVPPE HLPHLAQAFY RPDTARQRAT
     GGVGLGLYLC RLVAQAHDGQ LNMRNAEPGL SVTVRLPVVE
//
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