DGCJ_ECOLI
ID DGCJ_ECOLI Reviewed; 496 AA.
AC P76237;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable diguanylate cyclase DgcJ {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P31129};
GN Name=dgcJ {ECO:0000303|PubMed:26148715}; Synonyms=yeaJ;
GN OrderedLocusNames=b1786, JW5291;
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 DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18765794; DOI=10.1101/gad.475808;
RA Pesavento C., Becker G., Sommerfeldt N., Possling A., Tschowri N.,
RA Mehlis A., Hengge R.;
RT "Inverse regulatory coordination of motility and curli-mediated adhesion in
RT Escherichia coli.";
RL Genes Dev. 22:2434-2446(2008).
RN [5]
RP INDUCTION.
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 DISRUPTION PHENOTYPE.
RX PubMed=21181144; DOI=10.1007/s00253-010-3074-5;
RA Sanchez-Torres V., Hu H., Wood T.K.;
RT "GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and
RT swimming motility in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 90:651-658(2011).
RN [7]
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 = 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 -!- INTERACTION:
CC P76237; P32715: mdtO; NbExp=2; IntAct=EBI-555763, EBI-555775;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expressed during exponential and post-exponential growth, it
CC is slightly more highly expressed at 37 than 28 degrees Celsius and is
CC more highly induced on solid medium. {ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases swimming motility
CC (PubMed:21181144). Disruption of this gene partially suppresses the
CC reduced motility of a pdeH disruption. Full suppression i.e. wild-type
CC motility, requires concomitant disruption of dgcJ, dgcE and dgcQ
CC (PubMed:18765794). {ECO:0000269|PubMed:18765794,
CC ECO:0000269|PubMed:21181144}.
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DR EMBL; U00096; AAC74856.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15587.2; -; Genomic_DNA.
DR PIR; B64939; B64939.
DR RefSeq; NP_416300.2; NC_000913.3.
DR RefSeq; WP_000766132.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76237; -.
DR SMR; P76237; -.
DR BioGRID; 4260325; 7.
DR BioGRID; 850647; 1.
DR DIP; DIP-11789N; -.
DR IntAct; P76237; 2.
DR STRING; 511145.b1786; -.
DR jPOST; P76237; -.
DR PaxDb; P76237; -.
DR PRIDE; P76237; -.
DR EnsemblBacteria; AAC74856; AAC74856; b1786.
DR EnsemblBacteria; BAA15587; BAA15587; BAA15587.
DR GeneID; 946290; -.
DR KEGG; ecj:JW5291; -.
DR KEGG; eco:b1786; -.
DR PATRIC; fig|1411691.4.peg.468; -.
DR EchoBASE; EB3269; -.
DR eggNOG; COG2199; Bacteria.
DR HOGENOM; CLU_042022_1_0_6; -.
DR InParanoid; P76237; -.
DR OMA; SINRAQD; -.
DR PhylomeDB; P76237; -.
DR BioCyc; EcoCyc:G6972-MON; -.
DR BioCyc; MetaCyc:G6972-MON; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P76237; -.
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; 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; IMP:EcoCyc.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR033420; GAPES1.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF17155; GAPES1; 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.
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..496
FT /note="Probable diguanylate cyclase DgcJ"
FT /id="PRO_0000169016"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 374..496
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 387
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 56603 MW; 8E66D32CDB6F05DD CRC64;
MKLHHRMLRH FIAASVIVLT SSFLIFELVA SDRAMSAYLR YIVQKADSSF LYDKYQNQSI
AAHVMRALAA EQSEVSPEQR RAICEAFESA NNTHGLNLTA HKYPGLRGTL QTASTDCDTI
VEAAALLPAF DQAVEGNRHQ DDYGSGLGMA EEKFHYYLDL NDRYVYFYEP VNVEYFAMNN
WSFLQSGSIG IDRKDIEKVF TGRTVLSSIY QDQRTKQNVM SLLTPVYVAG QLKGIVLLDI
NKNNLRNIFY THDRPLLWRF LNVTLTDTDS GRDIIINQSE DNLFQYVSYV HDLPGGIRVS
LSIDILYFIT SSWKSVLFWI LTALILLNMV RMHFRLYQNV SRENISDAMT GLYNRKILTP
ELEQRLQKLV QSGSSVMFIA IDMDKLKQIN DTLGHQEGDL AITLLAQAIK QSIRKSDYAI
RLGGDEFCII LVDSTPQIAA QLPERIEKRL QHIAPQKEIG FSSGIYAMKE NDTLHDAYKA
SDERLYVNKQ NKNSRS
