DIVL_CAUVC
ID DIVL_CAUVC Reviewed; 769 AA.
AC Q9RQQ9; Q9A2S2;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Sensor protein DivL;
DE EC=2.7.13.3;
GN Name=divL; OrderedLocusNames=CC_3484;
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], AND PHOSPHORYLATION AT TYR-550.
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=10557274; DOI=10.1073/pnas.96.23.13068;
RA Wu J., Ohta N., Zhao J.L., Newton A.;
RT "A novel bacterial tyrosine kinase essential for cell division and
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13068-13073(1999).
RN [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 523-769.
RC STRAIN=ATCC 19089 / CB15;
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a C-terminal part of tyrosine kinase (DivL) from
RT Caulobacter crescentus CB15 at 2.50 A resolution (PSI community target,
RT Shapiro L.).";
RL Submitted (APR-2013) to the PDB data bank.
CC -!- FUNCTION: Required for cell division and growth. It catalyzes the
CC phosphorylation of CtrA and activates transcription in vitro of the
CC cell cycle-regulated fliF promoter.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10557274}.
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DR EMBL; AF083422; AAF08344.2; -; Genomic_DNA.
DR EMBL; AE005673; AAK25446.1; -; Genomic_DNA.
DR PIR; B87681; B87681.
DR RefSeq; NP_422278.1; NC_002696.2.
DR RefSeq; WP_010921313.1; NC_002696.2.
DR PDB; 4Q20; X-ray; 2.50 A; A/B=523-769.
DR PDBsum; 4Q20; -.
DR AlphaFoldDB; Q9RQQ9; -.
DR SMR; Q9RQQ9; -.
DR STRING; 190650.CC_3484; -.
DR iPTMnet; Q9RQQ9; -.
DR PRIDE; Q9RQQ9; -.
DR EnsemblBacteria; AAK25446; AAK25446; CC_3484.
DR KEGG; ccr:CC_3484; -.
DR PATRIC; fig|190650.5.peg.3494; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_018130_0_0_5; -.
DR OMA; NEFVQHV; -.
DR BioCyc; CAULO:CC3484-MON; -.
DR BRENDA; 2.7.13.3; 1218.
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; IEA:InterPro.
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; IPR035965; PAS-like_dom_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; SSF55785; SSF55785; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..769
FT /note="Sensor protein DivL"
FT /id="PRO_0000074729"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 547..758
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 550
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10557274"
FT CONFLICT 200
FT /note="Q -> H (in Ref. 1; AAF08344)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="V -> E (in Ref. 1; AAF08344)"
FT /evidence="ECO:0000305"
FT HELIX 527..567
FT /evidence="ECO:0007829|PDB:4Q20"
FT HELIX 574..604
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:4Q20"
FT HELIX 617..634
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:4Q20"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:4Q20"
FT HELIX 654..671
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 677..684
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 686..697
FT /evidence="ECO:0007829|PDB:4Q20"
FT HELIX 702..705
FT /evidence="ECO:0007829|PDB:4Q20"
FT TURN 706..709
FT /evidence="ECO:0007829|PDB:4Q20"
FT HELIX 723..733
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 737..742
FT /evidence="ECO:0007829|PDB:4Q20"
FT STRAND 748..755
FT /evidence="ECO:0007829|PDB:4Q20"
SQ SEQUENCE 769 AA; 82796 MW; 002B2428F18A57EF CRC64;
MTSYDLILAA AAGAVCLAIS VALWSHGQRR NLEARIVALK TRLIQQGGSD DAPAWLDAFD
TAVIAVEGGR ANLVAGGEGL IACAKALGAD AEVSAVVAAL SDADPNYAQK LTALFERGEP
CVFEARGPHG LVSVEGRAAG ALAWLRLAPI DRADSGLPTA ARFAAFVDSV VEPCWIAGAD
GQAIWGNAAF VRAVGAASAQ APALAGKSFD RGADAVVVEA AGKGERREAL RWINVEGRRR
AFRLSAQPLD GGGVGVFCAD VTEIEDVRDA FKKHVEAHDE TLNHIAEAVA IFSQTRRLSY
HNTAFAELWG LEPAWLADRP THGEVLDRLR QRRRLPETID YAGWKAAELA RYEDLGPQAD
DLWDLPDGRT LKVVRQPHPL GGMLLIYSDI TGELRLKAQY NALIQVQQAT LDKLNDAVAV
FGSDGRLRLH NEAFETFWNV TPHALEAAGD FEGVVELCVP RLHDLSFWRE LKGRVADPDP
QMRAPTSGEV RTSDSRIVLY QSRPLPDGAT LIAFADVTDT RDLQSALADR SAALAEAERL
KRDFVGNVSY ELRTPLTTII GYSELLERAD GISERGRNHV AAVRAAATQL ARSIDDVLDM
AQIDAGEMAL EIEDIRVSDL LLNAQERALK DAQLGGVTLA VECEEDVGLI RGDGKRLAQT
LDHLVENALR QTPPGGRVTL SARRALGEVR LDVSDTGRGV PFHVQAHIFD RFVGRDRGGP
GLGLALVKAL VELHGGWVAL ESEPGNGSTF TCHLPETQQP GAMQPELGF
