DGCP_ECOLI
ID DGCP_ECOLI Reviewed; 341 AA.
AC P76245; P94742; P97193;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Diguanylate cyclase DgcP {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000269|PubMed:15716451};
GN Name=dgcP {ECO:0000303|PubMed:26148715}; Synonyms=yeaP;
GN OrderedLocusNames=b1794, JW5292;
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 FUNCTION AS A DIGUANYLATE CYCLASE, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=15716451; DOI=10.1128/jb.187.5.1792-1798.2005;
RA Ryjenkov D.A., Tarutina M., Moskvin O.V., Gomelsky M.;
RT "Cyclic diguanylate is a ubiquitous signaling molecule in bacteria:
RT insights into biochemistry of the GGDEF protein domain.";
RL J. Bacteriol. 187:1792-1798(2005).
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
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 [6]
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. Cyclic-di-GMP is a second messenger
CC which controls cell surface-associated traits in bacteria.
CC {ECO:0000269|PubMed:15716451}.
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:0000269|PubMed:15716451};
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 -!- INDUCTION: Expressed during exponential and post-exponential growth at
CC both 28 and 37 degrees Celsius. {ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Decreased expression of CsgB, decreased curli
CC expression at 28 degrees Celsius. {ECO:0000269|PubMed:19332833}.
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DR EMBL; U00096; AAC74864.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15592.1; -; Genomic_DNA.
DR PIR; B64940; B64940.
DR RefSeq; NP_416308.4; NC_000913.3.
DR RefSeq; WP_001310896.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76245; -.
DR SMR; P76245; -.
DR BioGRID; 4260330; 23.
DR BioGRID; 853223; 1.
DR DIP; DIP-11795N; -.
DR IntAct; P76245; 3.
DR STRING; 511145.b1794; -.
DR jPOST; P76245; -.
DR PaxDb; P76245; -.
DR PRIDE; P76245; -.
DR EnsemblBacteria; AAC74864; AAC74864; b1794.
DR EnsemblBacteria; BAA15592; BAA15592; BAA15592.
DR GeneID; 948969; -.
DR KEGG; ecj:JW5292; -.
DR KEGG; eco:b1794; -.
DR PATRIC; fig|1411691.4.peg.461; -.
DR EchoBASE; EB3275; -.
DR eggNOG; COG2199; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR HOGENOM; CLU_000445_11_32_6; -.
DR InParanoid; P76245; -.
DR OMA; DTLCKRA; -.
DR PhylomeDB; P76245; -.
DR BioCyc; EcoCyc:G6980-MON; -.
DR BioCyc; MetaCyc:G6980-MON; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P76245; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00065; GAF; 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 GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..341
FT /note="Diguanylate cyclase DgcP"
FT /id="PRO_0000169024"
FT DOMAIN 18..154
FT /note="GAF"
FT DOMAIN 204..337
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 217
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 341 AA; 38546 MW; 6A8EA4053E59A4E2 CRC64;
MSDQIIARVS QSLAKEQSLE SLVRQLLEML EMVTDMESTY LTKVDVEARL QHIMFARNSQ
KMYIPENFTV SWDYSLCKRA IDENCFFSDE VPDRWGDCIA ARNLGITTFL STPIHLPDGS
FYGTLCAASS EKRQWSERAE QVLQLFAGLI AQYIQKEALV EQLREANAAL IAQSYTDSLT
GLPNRRAIFE NLTTLFSLAR HLNHKIMIAF IDLDNFKLIN DRFGHNSGDL FLIQVGERLN
TLQQNGEVIG RLGGDEFLVV SLNNENADIS SLRERIQQQI RGEYHLGDVD LYYPGASLGI
VEVDPETTDA DSALHAADIA MYQEKKHKQK TPFVAHPALH S
