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Database: UniProt
Entry: J2GXE3_9CAUL
LinkDB: J2GXE3_9CAUL
Original site: J2GXE3_9CAUL 
ID   J2GXE3_9CAUL            Unreviewed;       287 AA.
AC   J2GXE3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PMI01_03728 {ECO:0000313|EMBL:EJL27603.1};
OS   Caulobacter sp. AP07.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL27603.1, ECO:0000313|Proteomes:UP000007300};
RN   [1] {ECO:0000313|EMBL:EJL27603.1, ECO:0000313|Proteomes:UP000007300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP07 {ECO:0000313|EMBL:EJL27603.1,
RC   ECO:0000313|Proteomes:UP000007300};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(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};
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:EJL27603.1}.
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DR   EMBL; AKKF01000203; EJL27603.1; -; Genomic_DNA.
DR   AlphaFoldDB; J2GXE3; -.
DR   PATRIC; fig|1144304.3.peg.3562; -.
DR   Proteomes; UP000007300; Unassembled WGS sequence.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN 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:EJL27603.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:EJL27603.1}.
FT   DOMAIN          56..277
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  30627 MW;  7D53D83583EA434B CRC64;
     MPPLATTDVS AQAESPRESA GAELGSMSQT ATFRRAAARA RRKQALDDQK RSFLRMVSHE
     LRTPLNAVIG FSEILSCELY GPLGAPQYKE YAALVHESGL KLLRLVNQIV EIARLEGHVT
     DLDLGVEDLD EAVENVILQL RAEASARGVS IVAPEVGTLP SLRADGRGLR TILTNLLQNA
     VTHSPQGGLI VVEARQIGGA MVEIEVRDHG DGVDPADLGR LIRPFEQGGS TLTRSTEGAG
     LGLPIVDLLT RAMGGTLRLK STPGHGFTAI VTLPEAQARQ TLSRGRP
//
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