DIVJ_CAUVC
ID DIVJ_CAUVC Reviewed; 597 AA.
AC Q03228;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histidine protein kinase DivJ;
DE EC=2.7.13.3;
GN Name=divJ; OrderedLocusNames=CC_1063;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=1438215; DOI=10.1073/pnas.89.21.10297;
RA Ohta N., Lane T., Ninfa E.G., Sommer J.M., Newton A.;
RT "A histidine protein kinase homologue required for regulation of bacterial
RT cell division and differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10297-10301(1992).
RN [2]
RP SEQUENCE REVISION TO 315-319.
RA Ohta N.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [4]
RP PHOSPHORYLATION OF PLED.
RX PubMed=15075296; DOI=10.1101/gad.289504;
RA Paul R., Weiser S., Amiot N.C., Chan C., Schirmer T., Giese B., Jenal U.;
RT "Cell cycle-dependent dynamic localization of a bacterial response
RT regulator with a novel di-guanylate cyclase output domain.";
RL Genes Dev. 18:715-727(2004).
CC -!- FUNCTION: Kinase required for the regulation of cell division and
CC differentiation. Is part of a signal transduction pathway, activating
CC PleD by phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- INTERACTION:
CC Q03228; Q9A5I5: pleD; NbExp=3; IntAct=EBI-1785038, EBI-1784732;
CC Q03228; Q45976: divK; Xeno; NbExp=5; IntAct=EBI-1785038, EBI-1784754;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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DR EMBL; M98873; AAA23034.2; -; Genomic_DNA.
DR EMBL; AE005673; AAK23047.1; -; Genomic_DNA.
DR PIR; C87381; C87381.
DR RefSeq; NP_419879.1; NC_002696.2.
DR AlphaFoldDB; Q03228; -.
DR SMR; Q03228; -.
DR DIP; DIP-46002N; -.
DR IntAct; Q03228; 3.
DR STRING; 190650.CC_1063; -.
DR ChEMBL; CHEMBL4295589; -.
DR EnsemblBacteria; AAK23047; AAK23047; CC_1063.
DR KEGG; ccr:CC_1063; -.
DR PATRIC; fig|190650.5.peg.1080; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_22_5; -.
DR OMA; DIMRARM; -.
DR BioCyc; CAULO:CC1063-MON; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:CACAO.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:CACAO.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Differentiation;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..597
FT /note="Histidine protein kinase DivJ"
FT /id="PRO_0000074757"
FT TRANSMEM 40..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 335..553
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 561..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 338
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 529
FT /note="H -> L (in Ref. 1; AAA23034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 62373 MW; 802B532B749B37EA CRC64;
MILPTALKSR LALEFETLPD PFRRPAARAA GLDPAHAWRL GWLAAVCLAA AAALFTADSG
GWPVWAALGA GALPALVSLI FTREDERTQS WLLVLWAVGG SLAAVLTGGV GGAMAAWCLA
PVAAASTQDQ PKRLAEGAAL ALIGACVAAL TQLSGLAPAA PTGPLAFVLG FLALVTTGLG
LAAGLLIGRR RQGARDDRYA SEIIGLETLL DGLPHLAIAV RGQGQVTAVR GAAPPGVTRA
DLVNRGLTGA AAPGDRQRLT AAIAQAHREG SASLTFNPAL GVERVVALDM HRVAPNQLVG
VLRDITVERH REHALDQARI DAEALAAGRA RFLANMSHEL RTPLNAIMGF SDIMRARMFG
PLSDRYAEYA ELIHESGGHL LDLINDVLDM SKIEAERFEL QRGVFDAREA VQAAMRLLRV
QSDTAGVQLR GVLPPGELEV DADRRALKQI VLNLVSNALK FTPRGGQVTV TAHGYDGVLE
IVVADTGVGI SPEDLERLGR PYEQAGGAEQ RARGTGLGLS LVRAFAQLHG GEMVIESRLG
AGTTVSVRLP VLLAPMVAAT PTPPAAPEAP SAPEPAPTVE EPPPASLGDN VIAFAPR
