CDGI_ECOLI
ID CDGI_ECOLI Reviewed; 491 AA.
AC P76236;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable diguanylate cyclase CdgI {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P31129};
GN Name=cdgI {ECO:0000303|PubMed:26148715}; Synonyms=yeaI;
GN OrderedLocusNames=b1785, JW1774;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION, AND RPOS-DEPENDENCE.
RC STRAIN=K12 / MC4100;
RX PubMed=17010156; DOI=10.1111/j.1365-2958.2006.05440.x;
RA Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.;
RT "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia
RT coli.";
RL Mol. Microbiol. 62:1014-1034(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-407.
RX PubMed=21181144; DOI=10.1007/s00253-010-3074-5;
RA Sanchez-Torres V., Hu H., Wood T.K.;
RT "GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and
RT swimming motility in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 90:651-658(2011).
RN [7]
RP NOMENCLATURE.
RX PubMed=26148715; DOI=10.1128/jb.00424-15;
RA Hengge R., Galperin M.Y., Ghigo J.M., Gomelsky M., Green J., Hughes K.T.,
RA Jenal U., Landini P.;
RT "Systematic nomenclature for GGDEF and EAL domain-containing cyclic di-GMP
RT turnover proteins of Escherichia coli.";
RL J. Bacteriol. 198:7-11(2015).
CC -!- FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the
CC condensation of 2 GTP molecules. {ECO:0000250|UniProtKB:P31129}.
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:0000250|UniProtKB:P31129};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P31129};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P31129};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC {ECO:0000250|UniProtKB:P31129}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31129}.
CC -!- INTERACTION:
CC P76236; P0A6Z3: htpG; NbExp=3; IntAct=EBI-552525, EBI-369221;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by 0.3M NaCl in an RpoS-dependent fashion.
CC {ECO:0000269|PubMed:17010156}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases swimming motility
CC and early biofilm formation. {ECO:0000269|PubMed:21181144}.
CC -!- CAUTION: Has a EGEVF motif instead of the conserved GG[D/E]EF motif
CC characteristic of active diguanylate cyclases, suggesting that CdgI may
CC be inactive. However, site-directed mutagenesis shows that it is
CC probably a functional diguanylate cyclase.
CC {ECO:0000305|PubMed:21181144}.
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DR EMBL; U00096; AAC74855.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15586.1; -; Genomic_DNA.
DR PIR; A64939; A64939.
DR RefSeq; NP_416299.1; NC_000913.3.
DR RefSeq; WP_000616433.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P76236; -.
DR SMR; P76236; -.
DR BioGRID; 4260314; 18.
DR BioGRID; 850723; 1.
DR DIP; DIP-11788N; -.
DR IntAct; P76236; 2.
DR STRING; 511145.b1785; -.
DR PaxDb; P76236; -.
DR PRIDE; P76236; -.
DR EnsemblBacteria; AAC74855; AAC74855; b1785.
DR EnsemblBacteria; BAA15586; BAA15586; BAA15586.
DR GeneID; 66674328; -.
DR GeneID; 946366; -.
DR KEGG; ecj:JW1774; -.
DR KEGG; eco:b1785; -.
DR PATRIC; fig|511145.12.peg.1858; -.
DR EchoBASE; EB3268; -.
DR eggNOG; COG2199; Bacteria.
DR HOGENOM; CLU_000445_11_31_6; -.
DR InParanoid; P76236; -.
DR OMA; VCVLVWE; -.
DR BioCyc; EcoCyc:G6971-MON; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P76236; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0052621; F:diguanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR033424; MASE4.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF17158; MASE4; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; GTP-binding; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Probable diguanylate cyclase CdgI"
FT /id="PRO_0000169015"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..89
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..158
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..236
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..293
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 356..491
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 369
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 407
FT /note="E->A: Abolishes impact on swimming motility."
FT /evidence="ECO:0000269|PubMed:21181144"
SQ SEQUENCE 491 AA; 56101 MW; 2CF33E70FB6551AB CRC64;
MIQSTRISMG LFFKYFLSLT KIDPGQNYIS LPSIKSSTHI ALLFMVSMGT QKLKAQSFFI
FSLLLTLILF CITTLYNENT NVKLIPQMNY LMVVVALFFL NAVIFLFMLM KYFTNKQILP
TLILSLAFLS GLIYLVETIV IIHKPINGST LIQTKSNDVS IFYIFRQLSF ICLTSLALFC
YGKDNILDNN KKKTGILLLA LIPFLVFPLL AHNLSSYNAD YSLYVVDYCP DNHTATWGIN
YTKILVCLWA FLLFFIIMRT RLASELWPLI ALLCLASLCC NLLLLTLDEY NYTIWYISRG
IEVSSKLFVV SFLIYNIFQE LQLSSKLAVH DVLTNIYNRR YFFNSVESLL SRPVVKDFCV
MLVDINQFKR INAQWGHRVG DKVLVSIVDI IQQSIRPDDI LARLEGEVFG LLFTELNSAQ
AKIIAERMRK NVELLTGFSN RYDVPEQMTI SIGTVFSTGD TRNISLVMTE ADKALREAKS
EGGNKVIIHH I
