PLED_CAUVN
ID PLED_CAUVN Reviewed; 454 AA.
AC B8GZM2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 {ECO:0000269|PubMed:15075296};
DE AltName: Full=Diguanylate kinase;
GN Name=pleD; OrderedLocusNames=CCNA_02546;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP ROLE IN POLAR DEVELOPMENT, AND PHOSPHORYLATION AT ASP-53.
RX PubMed=12622822; DOI=10.1046/j.1365-2958.2003.03401.x;
RA Aldridge P., Paul R., Goymer P., Rainey P., Jenal U.;
RT "Role of the GGDEF regulator PleD in polar development of Caulobacter
RT crescentus.";
RL Mol. Microbiol. 47:1695-1708(2003).
RN [3]
RP FUNCTION AS A NUCLEOTIDE CYCLASE, CELL POLE LOCALIZATION, AND
RP PHOSPHORYLATION AT ASP-53.
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).
RN [4] {ECO:0007744|PDB:1W25}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH C-DI-GMP, ALLOSTERIC
RP REGULATION, AND SUBUNIT.
RX PubMed=15569936; DOI=10.1073/pnas.0406134101;
RA Chan C., Paul R., Samoray D., Amiot N.C., Giese B., Jenal U., Schirmer T.;
RT "Structural basis of activity and allosteric control of diguanylate
RT cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17084-17089(2004).
RN [5] {ECO:0007744|PDB:2V0N}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 2-454 OF DIMER WITH C-DI-GMP IN
RP THE ACTIVATED FORM, AND COFACTOR.
RX PubMed=17697997; DOI=10.1016/j.str.2007.06.016;
RA Wassmann P., Chan C., Paul R., Beck A., Heerklotz H., Jenal U.,
RA Schirmer T.;
RT "Structure of BeF(3-)-modified response regulator PleD: implications for
RT diguanylate cyclase activation, catalysis, and feedback inhibition.";
RL Structure 15:915-927(2007).
RN [6] {ECO:0007744|PDB:2WB4}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RA Wassmann P., Massa C., Zaehringer F., Schirmer T.;
RT "Crystal structure of activated Pled, identification of dimerization and
RT catalysis relevant regulatory mechanisms.";
RL Submitted (FEB-2009) to the PDB data bank.
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:0000269|PubMed:12622822}.
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:0000269|PubMed:15075296}.
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 Evidence={ECO:0000269|PubMed:15075296};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17697997};
CC Note=Binds 2 Mg(2+) per monomer. {ECO:0000269|PubMed:17697997};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by dimers of the product
CC c-di-GMP. {ECO:0000269|PubMed:15569936}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC -!- SUBUNIT: Homodimer. Inactive monomer in solution, dimerization seems to
CC be required for activity. Dimerization in vitro is enhanced by BeF(3-)
CC and by 1 mM Mn(2+) or 10 mM Mg(2+). {ECO:0000269|PubMed:15569936}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Phosphorylated PleD localizes to
CC the differentiating pole. {ECO:0000269|PubMed:15075296}.
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.
CC {ECO:0000305}.
CC -!- PTM: Phosphorylated by PleC and DivJ. Phosphorylation stimulates
CC cyclase activity. {ECO:0000269|PubMed:12622822,
CC ECO:0000269|PubMed:15075296}.
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DR EMBL; CP001340; ACL96011.1; -; Genomic_DNA.
DR RefSeq; WP_010920320.1; NC_011916.1.
DR RefSeq; YP_002517919.1; NC_011916.1.
DR PDB; 1W25; X-ray; 2.70 A; A/B=2-454.
DR PDB; 2V0N; X-ray; 2.71 A; A/B=2-454.
DR PDB; 2WB4; X-ray; 2.80 A; A/B=1-454.
DR PDBsum; 1W25; -.
DR PDBsum; 2V0N; -.
DR PDBsum; 2WB4; -.
DR AlphaFoldDB; B8GZM2; -.
DR SMR; B8GZM2; -.
DR EnsemblBacteria; ACL96011; ACL96011; CCNA_02546.
DR GeneID; 7333643; -.
DR KEGG; ccs:CCNA_02546; -.
DR PATRIC; fig|565050.3.peg.2497; -.
DR HOGENOM; CLU_000445_11_28_5; -.
DR OMA; NDYFVYP; -.
DR OrthoDB; 1635706at2; -.
DR PhylomeDB; B8GZM2; -.
DR BRENDA; 2.7.7.65; 1218.
DR UniPathway; UPA00599; -.
DR EvolutionaryTrace; B8GZM2; -.
DR Proteomes; UP000001364; 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: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; IEA:UniProtKB-KW.
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 3D-structure; Cell cycle; Cytoplasm; Differentiation; GTP-binding;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..454
FT /note="Response regulator PleD"
FT /id="PRO_0000396955"
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 /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15569936"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15569936,
FT ECO:0000269|PubMed:17697997, ECO:0000269|Ref.6"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15569936,
FT ECO:0000269|PubMed:17697997, ECO:0000269|Ref.6"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15569936,
FT ECO:0000269|PubMed:17697997, ECO:0000269|Ref.6"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17697997"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17697997"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15569936, ECO:0000305|Ref.6"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15569936, ECO:0000305|Ref.6"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17697997"
FT SITE 178
FT /note="Allosteric product binding, non-activate state"
FT SITE 313
FT /note="Allosteric product binding, active state"
FT SITE 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT SITE 359
FT /note="Allosteric product phosphate group binding, activate
FT and inactive state"
FT SITE 362
FT /note="Allosteric product binding, activate and inactive
FT state"
FT SITE 390
FT /note="Allosteric product binding, activate and inactive
FT state"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:12622822, ECO:0000269|PubMed:15075296"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1W25"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 109..133
FT /evidence="ECO:0007829|PDB:1W25"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1W25"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2WB4"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2WB4"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1W25"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 258..279
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2V0N"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2WB4"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 340..356
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 381..396
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2V0N"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:2V0N"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:1W25"
FT HELIX 427..443
FT /evidence="ECO:0007829|PDB:1W25"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:1W25"
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
