PLED_CAUVC
ID PLED_CAUVC Reviewed; 454 AA.
AC Q9A5I5; Q46020;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Response regulator PleD;
DE AltName: Full=Stalked cell differentiation-controlling protein;
DE Includes:
DE RecName: Full=Diguanylate cyclase;
DE Short=DGC;
DE EC=2.7.7.65;
DE AltName: Full=Diguanylate kinase;
GN Name=pleD; OrderedLocusNames=CC_2462;
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=7592388; DOI=10.1128/jb.177.21.6223-6229.1995;
RA Hecht G.B., Newton A.;
RT "Identification of a novel response regulator required for the swarmer-to-
RT stalked-cell transition in Caulobacter crescentus.";
RL J. Bacteriol. 177:6223-6229(1995).
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).
CC -!- FUNCTION: Response regulator that is part of a signal transduction
CC pathway controlling cell differentiation in the swarmer-to-stalked cell
CC transition. {ECO:0000250}.
CC -!- FUNCTION: Catalyzes the condensation of two GTP molecules to the cyclic
CC dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate;
CC Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:58805; EC=2.7.7.65;
CC -!- ACTIVITY REGULATION: Allosterically inhibited by the product c-di-GMP.
CC {ECO:0000250}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC -!- SUBUNIT: Homodimer. Inactive monomer in solution (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9A5I5; Q03228: divJ; NbExp=3; IntAct=EBI-1784732, EBI-1785038;
CC Q9A5I5; P37894: pleC; NbExp=4; IntAct=EBI-1784732, EBI-1784742;
CC Q9A5I5; Q9A5I5: pleD; NbExp=4; IntAct=EBI-1784732, EBI-1784732;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Phosphorylated PleD
CC localizes to the differentiating pole.
CC -!- DOMAIN: Activated by phosphorylation at the first response regulatory
CC domain, which induces dimerization mediated by the two response
CC regulatory domains and allows the two substrate-binding sites to
CC approach each other and the condensation reaction to occur (Probable).
CC The diguanylate cyclase activity is harbored by the GGDEF domain (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- PTM: Phosphorylated by PleC and DivJ. Phosphorylation stimulates
CC cyclase activity (By similarity). {ECO:0000250}.
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DR EMBL; L42554; AAA87378.1; -; Genomic_DNA.
DR EMBL; AE005673; AAK24433.1; -; Genomic_DNA.
DR PIR; E87554; E87554.
DR RefSeq; NP_421265.1; NC_002696.2.
DR RefSeq; WP_010920320.1; NC_002696.2.
DR AlphaFoldDB; Q9A5I5; -.
DR SMR; Q9A5I5; -.
DR DIP; DIP-29503N; -.
DR IntAct; Q9A5I5; 2.
DR STRING; 190650.CC_2462; -.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR EnsemblBacteria; AAK24433; AAK24433; CC_2462.
DR KEGG; ccr:CC_2462; -.
DR PATRIC; fig|190650.5.peg.2479; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_28_5; -.
DR OMA; NDYFVYP; -.
DR BioCyc; CAULO:CC2462-MON; -.
DR BRENDA; 2.7.7.65; 1218.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052621; F:diguanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:CACAO.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00072; Response_reg; 2.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Differentiation; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transducer; Transferase; Two-component regulatory system.
FT CHAIN 1..454
FT /note="Response regulator PleD"
FT /id="PRO_0000081206"
FT DOMAIN 4..120
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 155..269
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 319..454
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 178
FT /note="Allosteric product binding"
FT /evidence="ECO:0000250"
FT SITE 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT SITE 359
FT /note="Allosteric product phosphate group binding"
FT /evidence="ECO:0000250"
FT SITE 362
FT /note="Allosteric product binding"
FT /evidence="ECO:0000250"
FT SITE 390
FT /note="Allosteric product binding"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 45..48
FT /note="DLPD -> ICPT (in Ref. 1; AAA87378)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="Y -> C (in Ref. 1; AAA87378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 49624 MW; D44909D42B581516 CRC64;
MSARILVVDD IEANVRLLEA KLTAEYYEVS TAMDGPTALA MAARDLPDII LLDVMMPGMD
GFTVCRKLKD DPTTRHIPVV LITALDGRGD RIQGLESGAS DFLTKPIDDV MLFARVRSLT
RFKLVIDELR QREASGRRMG VIAGAAARLD GLGGRVLIVD DNERQAQRVA AELGVEHRPV
IESDPEKAKI SAGGPVDLVI VNAAAKNFDG LRFTAALRSE ERTRQLPVLA MVDPDDRGRM
VKALEIGVND ILSRPIDPQE LSARVKTQIQ RKRYTDYLRN NLDHSLELAV TDQLTGLHNR
RYMTGQLDSL VKRATLGGDP VSALLIDIDF FKKINDTFGH DIGDEVLREF ALRLASNVRA
IDLPCRYGGE EFVVIMPDTA LADALRIAER IRMHVSGSPF TVAHGREMLN VTISIGVSAT
AGEGDTPEAL LKRADEGVYQ AKASGRNAVV GKAA
