DGCT_ECOLI
ID DGCT_ECOLI Reviewed; 452 AA.
AC P75908; Q9R7P4; Q9R7P6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable diguanylate cyclase DgcT {ECO:0000305};
DE Short=DGC;
DE EC=2.7.7.65 {ECO:0000305|PubMed:18713317};
GN Name=dgcT {ECO:0000303|PubMed:26148715}; Synonyms=ycdT;
GN OrderedLocusNames=b1025, JW5143;
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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP PROBABLE ENZYME ACTIVITY, FUNCTION, MUTAGENESIS OF 359-GLY-GLY-360,
RP DISRUPTION PHENOTYPE, AND POST-TRANSCRIPTIONAL REGULATION BY CSRA.
RC STRAIN=K12;
RX PubMed=18713317; DOI=10.1111/j.1365-2958.2008.06411.x;
RA Jonas K., Edwards A.N., Simm R., Romeo T., Romling U., Melefors O.;
RT "The RNA binding protein CsrA controls cyclic di-GMP metabolism by directly
RT regulating the expression of GGDEF proteins.";
RL Mol. Microbiol. 70:236-257(2008).
RN [6]
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 [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: Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP)
CC via the condensation of 2 GTP molecules. Overexpression leads to a
CC strong repression of swimming; swimming returns to normal when residues
CC 359-360 are both mutated to Ala. Overexpression also leads to a 20-fold
CC increase in c-di-GMP levels in vivo. Cyclic-di-GMP is a second
CC messenger which controls cell surface-associated traits in bacteria.
CC {ECO:0000269|PubMed:18713317}.
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:18713317};
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}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: CsrA binds to the mRNA and reduces its levels. Expressed at
CC low levels at both 28 and 37 degrees Celsius.
CC {ECO:0000269|PubMed:18713317, ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: A slight increase in motility. No visible effect
CC on curli production. {ECO:0000269|PubMed:18713317}.
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DR EMBL; U00096; AAC74110.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35810.2; -; Genomic_DNA.
DR PIR; G64844; G64844.
DR RefSeq; NP_415544.1; NC_000913.3.
DR RefSeq; WP_000409873.1; NZ_LN832404.1.
DR AlphaFoldDB; P75908; -.
DR SMR; P75908; -.
DR BioGRID; 4263227; 10.
DR STRING; 511145.b1025; -.
DR PaxDb; P75908; -.
DR PRIDE; P75908; -.
DR EnsemblBacteria; AAC74110; AAC74110; b1025.
DR EnsemblBacteria; BAA35810; BAA35810; BAA35810.
DR GeneID; 945593; -.
DR KEGG; ecj:JW5143; -.
DR KEGG; eco:b1025; -.
DR PATRIC; fig|511145.12.peg.1065; -.
DR EchoBASE; EB3626; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_31_6; -.
DR InParanoid; P75908; -.
DR OMA; WNGVSVI; -.
DR PhylomeDB; P75908; -.
DR BioCyc; EcoCyc:G6532-MON; -.
DR BioCyc; MetaCyc:G6532-MON; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P75908; -.
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; IMP: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:0090609; P:single-species submerged biofilm formation; IMP:EcoCyc.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR033424; MASE4.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF17158; MASE4; 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..452
FT /note="Probable diguanylate cyclase DgcT"
FT /id="PRO_0000168806"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..45
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..111
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..195
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..254
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 310..445
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 323
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT VARIANT 130
FT /note="A -> V (in strain: K12 / W3110 / ATCC 27325 / DSM
FT 5911)"
FT MUTAGEN 359..360
FT /note="GG->AA: Cells overexpressing this mutant are no
FT longer swimming suppressed."
FT /evidence="ECO:0000269|PubMed:18713317"
SQ SEQUENCE 452 AA; 51783 MW; B6FB9E7EB894D701 CRC64;
MEKDYLRISS TVLVSLLFGL ALVLVNSWFN QPGVEEVVPR STYLMVMIAL FFIDTVAFIF
MQLYFIYDRR QFSNCVLSLA FLSCLIYFVI TVIIIQQIIE ERLTSSVVQN DIAIYYLFRQ
MSLCILIFLA LVNKVSENTK QRNLFSKKMT LCISLFFVFG GPIVAHILSS HYESYNLHIA
ELTNENGQVV WKASYVTIMI FMWLTLLSVN LYFNGLRYDI WNGVTVIAFC AVLYNISLLF
MSRYSVSTWY ISRTIEVVSK LTVMVIFMCH IFSALRVTKN IAHRDPLTNI FNRNYFFNEL
TVQSASAQKT PYCVMIMDID HFKKVNDTWG HPVGDQVIKT VVNIIGKSIR PDDLLARVGG
EEFGVLLTDI DTERAKALAE RIRENVERLT GDNPEYAIPQ KVTISIGAVV TQENALNPNE
IYRLADNALY EAKETGRNKV VVRDVVNFCE SP
