ID DGCI_ECOLI Reviewed; 442 AA.
AC P75801;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Probable diguanylate cyclase DgcI {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P31129};
DE AltName: Full=Putative lipoprotein DgcI {ECO:0000305};
DE Flags: Precursor;
GN Name=dgcI {ECO:0000303|PubMed:26148715}; Synonyms=yliF;
GN OrderedLocusNames=b0834, JW0818;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 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 = 3',3'-c-di-GMP + 2 diphosphate; Xref=Rhea:RHEA:24898,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, 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:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31129}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC73921.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35529.1; -; Genomic_DNA.
DR PIR; B64821; B64821.
DR RefSeq; NP_415355.1; NC_000913.3.
DR RefSeq; WP_000086904.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P75801; -.
DR SMR; P75801; -.
DR BioGRID; 4261104; 16.
DR STRING; 511145.b0834; -.
DR PaxDb; 511145-b0834; -.
DR EnsemblBacteria; AAC73921; AAC73921; b0834.
DR GeneID; 945463; -.
DR KEGG; ecj:JW0818; -.
DR KEGG; eco:b0834; -.
DR PATRIC; fig|1411691.4.peg.1444; -.
DR EchoBASE; EB3250; -.
DR eggNOG; COG2199; Bacteria.
DR HOGENOM; CLU_056913_0_0_6; -.
DR InParanoid; P75801; -.
DR OMA; YIQICAL; -.
DR OrthoDB; 9812260at2; -.
DR PhylomeDB; P75801; -.
DR BioCyc; EcoCyc:G6434-MONOMER; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P75801; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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; IBA:GO_Central.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR033422; GAPES2.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR45138:SF9; DIGUANYLATE CYCLASE DGCM-RELATED; 1.
DR PANTHER; PTHR45138; REGULATORY COMPONENTS OF SENSORY TRANSDUCTION SYSTEM; 1.
DR Pfam; PF17156; GAPES2; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Palmitate; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..442
FT /note="Probable diguanylate cyclase DgcI"
FT /id="PRO_0000168730"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 319..442
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 442 AA; 49873 MW; 52244FBA2E0CF643 CRC64;
MSRINKFVLT VSLLIFIMIS AVACGIYTQM VKERVYSLKQ SVIDTAFAVA NIAEYRRSVA
IDLINTLNPT EEQLLVGLRT AYADSVSPSY LYDVGPYLIS SDECIQVKEF EKNYCADIMQ
VVKYRHVKNT GFISFDGKTF VYYLYPVTHN RSLIFLLGLE RFSLLSKSLA MDSENLMFSL
FKNGKPVTGD EYNAKNAIFT VSEAMEHFAY LPTGLYVFAY KKDVYLRVCT LIIFFAALVA
VISGASCLYL VRRVINRGIV EKEAIINNHF ERVLDGGLFF SAADVKKLYS MYNSAFLDDL
TKAMGRKSFD EDLKALPEKG GYLCLFDVDK FKNINDTFGH LLGDEVLMKV VKILKSQIPV
DKGKVYRFGG DEFAVIYTGG TLEELLSILK EIVHFQVGSI NLSTSIGVAH SNECPTVERL
KMLADERLYK SKKNGRAQIS WQ
//
