DGCI_ECO57
ID DGCI_ECO57 Reviewed; 442 AA.
AC Q8X6V3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Flags: Precursor;
GN Name=dgcI {ECO:0000250|UniProtKB:P75801}; Synonyms=yliF;
GN OrderedLocusNames=Z1058, ECs0913;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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: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; AE005174; AAG55208.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34336.1; -; Genomic_DNA.
DR PIR; A90743; A90743.
DR PIR; D85593; D85593.
DR RefSeq; NP_308940.1; NC_002695.1.
DR RefSeq; WP_000086905.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X6V3; -.
DR SMR; Q8X6V3; -.
DR STRING; 155864.EDL933_0959; -.
DR EnsemblBacteria; AAG55208; AAG55208; Z1058.
DR EnsemblBacteria; BAB34336; BAB34336; ECs_0913.
DR GeneID; 917650; -.
DR KEGG; ece:Z1058; -.
DR KEGG; ecs:ECs_0913; -.
DR PATRIC; fig|386585.9.peg.1028; -.
DR eggNOG; COG2199; Bacteria.
DR HOGENOM; CLU_056913_0_0_6; -.
DR OMA; EYRRRIC; -.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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: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 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 Pfam; PF17156; GAPES2; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 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_0000168731"
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; 49877 MW; 52244FBE6E48F643 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 SNECTTVERL
KMLADERLYK SKKNGRAQIS WQ
