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Database: UniProt
Entry: C5TA67_ACIDE
LinkDB: C5TA67_ACIDE
Original site: C5TA67_ACIDE 
ID   C5TA67_ACIDE            Unreviewed;       182 AA.
AC   C5TA67;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   ORFNames=AcdelDRAFT_3797 {ECO:0000313|EMBL:EER58625.1};
OS   Acidovorax delafieldii 2AN.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=573060 {ECO:0000313|EMBL:EER58625.1, ECO:0000313|Proteomes:UP000003856};
RN   [1] {ECO:0000313|EMBL:EER58625.1, ECO:0000313|Proteomes:UP000003856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2AN {ECO:0000313|EMBL:EER58625.1,
RC   ECO:0000313|Proteomes:UP000003856};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA   Picardal F., Roden E., Emerson D.;
RT   "The draft genome of Acidovorax delafieldii 2AN.";
RL   Submitted (MAY-2009) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EER58625.1}.
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DR   EMBL; ACQT01000231; EER58625.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5TA67; -.
DR   PATRIC; fig|573060.9.peg.1170; -.
DR   OrthoDB; 9808408at2; -.
DR   Proteomes; UP000003856; Unassembled WGS sequence.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EER58625.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003856};
KW   Transferase {ECO:0000313|EMBL:EER58625.1}.
FT   DOMAIN          53..168
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EER58625.1"
SQ   SEQUENCE   182 AA;  19118 MW;  0D61FC96C9CC7F19 CRC64;
     RAIRALARKR VPVRALNDPV ALANEAVALF CGLLGQAPPI RVECAQGSAG LRVPGDPQQI
     QQVLLNLLKN ALDAHRAAGR AEAPITITIE RQGDRLVMAV QDQGAPLSEA ERARLFEPFY
     TTRPDGLGLG LAICRGIAET HGGALQARPA GAAGDPGMVF ELLLPLAPTA IRLPPTPQDI
     AP
//
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