ID   DGCC_ECOL6              Reviewed;         371 AA.
AC   P0AAP2; P21830; P77719;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable diguanylate cyclase DgcC {ECO:0000250|UniProtKB:P0AAP1};
DE            Short=DGC {ECO:0000250|UniProtKB:P0AAP1};
DE            EC=2.7.7.65 {ECO:0000250|UniProtKB:P0AAP1};
GN   Name=dgcC {ECO:0000250|UniProtKB:P0AAP1}; Synonyms=adrA;
GN   OrderedLocusNames=c0492;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: A probable diguanylate cyclase.
CC       {ECO:0000250|UniProtKB:P0AAP1}.
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:P0AAP1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:B8GZM2};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P0AAP1};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC       {ECO:0000250|UniProtKB:P0AAP1}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
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DR   EMBL; AE014075; AAN78970.1; -; Genomic_DNA.
DR   RefSeq; WP_000484048.1; NC_004431.1.
DR   AlphaFoldDB; P0AAP2; -.
DR   SMR; P0AAP2; -.
DR   STRING; 199310.c0492; -.
DR   EnsemblBacteria; AAN78970; AAN78970; c0492.
DR   GeneID; 58460372; -.
DR   KEGG; ecc:c0492; -.
DR   eggNOG; COG3706; Bacteria.
DR   HOGENOM; CLU_000445_11_1_6; -.
DR   OMA; HGAWKDL; -.
DR   BioCyc; ECOL199310:C0492-MON; -.
DR   UniPathway; UPA00599; -.
DR   Proteomes; UP000001410; 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; IPR000160; GGDEF_dom.
DR   InterPro; IPR007894; MASE2.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF05230; MASE2; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   TIGRFAMs; TIGR00254; GGDEF; 1.
DR   PROSITE; PS50887; GGDEF; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; GTP-binding; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..371
FT                   /note="Probable diguanylate cyclase DgcC"
FT                   /id="PRO_0000168589"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          240..371
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:B8GZM2"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:B8GZM2"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B8GZM2"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B8GZM2"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:B8GZM2"
FT   SITE            253
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   371 AA;  41537 MW;  1F5111C43481F32B CRC64;
     MFPKIMNDEN FFKKAAAHGE EPPLTPQNEH QRSGLRFARR VRLPRAVGLA GMFLPIASTL
     VSHPPPGWWW LVLVGWAFVW PHLAWQIASR AVDPLSREIY NLKTDAVLAG MWVGVMGVNV
     LPSTAMLMIM CLNLMGAGGP RLFVAGLVLM VVSCLVTLEL TGITVSFNSA PLEWWLSLPI
     IVIYPLLFGW VSYQTATKLA EHKRRLQVMS TRDGMTGVYN RRHWETMLRN EFDNCRRHNR
     DATLLIIDID HFKSINDTWG HDVGDEAIVA LTRQLQITLR GSDVIGRFGG DEFAVIMSGT
     PAESAITAML RVHEGLNTLR LPNTPQVTLR ISVGVAPLNP QMSHYREWLK SADLALYKAK
     KAGRNRTEVA A