DGCC_ECOLI
ID DGCC_ECOLI Reviewed; 371 AA.
AC P0AAP1; P21830; P77719; Q2MC40;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable diguanylate cyclase DgcC {ECO:0000305};
DE Short=DGC;
DE EC=2.7.7.65 {ECO:0000305|PubMed:19707751};
GN Name=dgcC {ECO:0000303|PubMed:26148715}; Synonyms=adrA, yaiC;
GN OrderedLocusNames=b0385, JW0376;
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 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
RC STRAIN=K12;
RX PubMed=3533724; DOI=10.1016/0378-1119(86)90050-8;
RA Chang C.N., Kuang W.-J., Chen E.Y.;
RT "Nucleotide sequence of the alkaline phosphatase gene of Escherichia
RT coli.";
RL Gene 44:121-125(1986).
RN [5]
RP LACK OF CELLULOSE PRODUCTION IN K12 STRAINS.
RC STRAIN=K12 / MC4100;
RX PubMed=11260463; DOI=10.1046/j.1365-2958.2001.02337.x;
RA Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U.;
RT "The multicellular morphotypes of Salmonella typhimurium and Escherichia
RT coli produce cellulose as the second component of the extracellular
RT matrix.";
RL Mol. Microbiol. 39:1452-1463(2001).
RN [6]
RP REGULATION BY CSGD.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16513732; DOI=10.1128/jb.188.6.2027-2037.2006;
RA Brombacher E., Baratto A., Dorel C., Landini P.;
RT "Gene expression regulation by the Curli activator CsgD protein: modulation
RT of cellulose biosynthesis and control of negative determinants for
RT microbial adhesion.";
RL J. Bacteriol. 188:2027-2037(2006).
RN [7]
RP INDUCTION, RPOS-DEPENDENCE, AND REGULATION CASCADE.
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 [8]
RP INDUCTION, AND RPOS-DEPENDENCE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19332833; DOI=10.1099/mic.0.024257-0;
RA Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N.,
RA Hengge R.;
RT "Gene expression patterns and differential input into curli fimbriae
RT regulation of all GGDEF/EAL domain proteins in Escherichia coli.";
RL Microbiology 155:1318-1331(2009).
RN [9]
RP FUNCTION, PROBABLE ENZYME ACTIVITY, AND MUTAGENESIS OF 291-ASP-GLU-292.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19707751; DOI=10.1007/s00253-009-2199-x;
RA Antoniani D., Bocci P., Maciag A., Raffaelli N., Landini P.;
RT "Monitoring of diguanylate cyclase activity and of cyclic-di-GMP
RT biosynthesis by whole-cell assays suitable for high-throughput screening of
RT biofilm inhibitors.";
RL Appl. Microbiol. Biotechnol. 85:1095-1104(2010).
RN [10]
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: A probable diguanylate cyclase. The last member of a cascade
CC of expressed proteins, its expression requires DgcM. DgcC production
CC induces biosynthesis of cellulose in some E.coli isolates, but not in
CC K12 strains. Cyclic-di-GMP is a second messenger which controls cell
CC surface-associated traits in bacteria. {ECO:0000269|PubMed:11260463,
CC ECO:0000269|PubMed:19707751}.
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:0000305|PubMed:19707751};
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:0000305};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expressed at 28 degrees Celsius in late stationary phase,
CC more highly expressed on plates than in liquid medium. Expression is
CC RpoS-, CsgD- and DgcM-dependent. {ECO:0000269|PubMed:16513732,
CC ECO:0000269|PubMed:17010156, ECO:0000269|PubMed:19332833}.
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DR EMBL; U73857; AAB18109.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73488.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76166.1; -; Genomic_DNA.
DR EMBL; M13345; AAA83895.1; -; Genomic_DNA.
DR PIR; A64767; A64767.
DR RefSeq; NP_414919.1; NC_000913.3.
DR RefSeq; WP_000484048.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P0AAP1; -.
DR SMR; P0AAP1; -.
DR BioGRID; 4262033; 19.
DR STRING; 511145.b0385; -.
DR TCDB; 9.B.34.1.2; the kinase/phosphatase/cyclic-gmp synthase/cyclic di-gmp hydrolase (kpsh) family.
DR PaxDb; P0AAP1; -.
DR PRIDE; P0AAP1; -.
DR EnsemblBacteria; AAC73488; AAC73488; b0385.
DR EnsemblBacteria; BAE76166; BAE76166; BAE76166.
DR GeneID; 58460372; -.
DR GeneID; 945037; -.
DR KEGG; ecj:JW0376; -.
DR KEGG; eco:b0385; -.
DR PATRIC; fig|1411691.4.peg.1893; -.
DR EchoBASE; EB1237; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_1_6; -.
DR InParanoid; P0AAP1; -.
DR OMA; HGAWKDL; -.
DR PhylomeDB; P0AAP1; -.
DR BioCyc; EcoCyc:EG11257-MON; -.
DR BioCyc; MetaCyc:EG11257-MON; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P0AAP1; -.
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; IBA:GO_Central.
DR GO; GO:0052621; F:diguanylate cyclase activity; IDA:EcoCyc.
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 GO; GO:2001008; P:positive regulation of cellulose biosynthetic process; IMP:EcoCyc.
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 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..371
FT /note="Probable diguanylate cyclase DgcC"
FT /id="PRO_0000168588"
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"
FT MUTAGEN 291..292
FT /note="DE->AA: No c-di-GMP produced in an overexpressing
FT strain."
FT /evidence="ECO:0000269|PubMed:19707751"
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
