DGCE_ECOLI
ID DGCE_ECOLI Reviewed; 1105 AA.
AC P38097; P76391;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Probable diguanylate cyclase DgcE {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P31129};
GN Name=dgcE {ECO:0000303|PubMed:26148715}; Synonyms=yegE;
GN OrderedLocusNames=b2067, JW2052;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 965-1105.
RX PubMed=6094528; DOI=10.1016/s0021-9258(18)89806-4;
RA Nakabeppu Y., Miyata T., Kondo H., Iwanaga S., Sekiguchi M.;
RT "Structure and expression of the alkA gene of Escherichia coli involved in
RT adaptive response to alkylating agents.";
RL J. Biol. Chem. 259:13730-13736(1984).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
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 [7]
RP INDUCTION, RPOS-DEPENDENCE, 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 [8]
RP ROLE IN MOTILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20303158; DOI=10.1016/j.cell.2010.01.018;
RA Boehm A., Kaiser M., Li H., Spangler C., Kasper C.A., Ackermann M.,
RA Kaever V., Sourjik V., Roth V., Jenal U.;
RT "Second messenger-mediated adjustment of bacterial swimming velocity.";
RL Cell 141:107-116(2010).
RN [9]
RP FUNCTION.
RX PubMed=23708798; DOI=10.1038/emboj.2013.120;
RA Lindenberg S., Klauck G., Pesavento C., Klauck E., Hengge R.;
RT "The EAL domain protein YciR acts as a trigger enzyme in a c-di-GMP
RT signalling cascade in E. coli biofilm control.";
RL EMBO J. 32:2001-2014(2013).
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: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the
CC condensation of 2 GTP molecules (By similarity). Involved in the
CC control of the switch from cell motility to adhesion via regulation of
CC cellular levels of c-di-GMP (Probable). Part of a signaling cascade
CC that regulates curli biosynthesis. The cascade is composed of two c-di-
CC GMP control modules, in which c-di-GMP controlled by the DgcE/PdeH pair
CC (module I) regulates the activity of the DgcM/PdeR pair (module II),
CC which in turn regulates activity of the transcription factor MlrA and
CC expression of the master biofilm regulator csgD (PubMed:23708798).
CC {ECO:0000250|UniProtKB:P31129, ECO:0000269|PubMed:23708798,
CC ECO:0000305|PubMed:20303158}.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expressed during transition into stationary phase,
CC expression is equal at 28 and 37 degrees Celsius. Expression is RpoS
CC dependent. {ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Decreased biofilm formation, decreased expression
CC of DgcC, a probable diguanylate cyclase and of the curli regulator CsgD
CC (PubMed:19332833). Disruption leads to decreaseded expression of
CC adhesive curli fimbriae genes (PubMed:18765794). Also partially
CC suppresses the reduced motility of a pdeH disruption; concomitant
CC disruption of dosC, dgcE, dgcQ and dgcN completely restores motility,
CC suggesting these 4 genes, together with the c-di-GMP phosphodiesterase
CC PdeH, form a network that regulates cell motility by altering levels of
CC c-di-GMP. {ECO:0000269|PubMed:18765794, ECO:0000269|PubMed:19332833,
CC ECO:0000269|PubMed:20303158}.
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DR EMBL; U00096; AAC75128.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15920.1; -; Genomic_DNA.
DR EMBL; K02498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B64973; B64973.
DR RefSeq; NP_416571.1; NC_000913.3.
DR RefSeq; WP_000043761.1; NZ_LN832404.1.
DR AlphaFoldDB; P38097; -.
DR SMR; P38097; -.
DR BioGRID; 4259682; 200.
DR IntAct; P38097; 1.
DR STRING; 511145.b2067; -.
DR jPOST; P38097; -.
DR PaxDb; P38097; -.
DR PRIDE; P38097; -.
DR EnsemblBacteria; AAC75128; AAC75128; b2067.
DR EnsemblBacteria; BAA15920; BAA15920; BAA15920.
DR GeneID; 946600; -.
DR KEGG; ecj:JW2052; -.
DR KEGG; eco:b2067; -.
DR PATRIC; fig|1411691.4.peg.184; -.
DR EchoBASE; EB2297; -.
DR eggNOG; COG3447; Bacteria.
DR eggNOG; COG5001; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_126_1_6; -.
DR InParanoid; P38097; -.
DR OMA; IVYTHMT; -.
DR PhylomeDB; P38097; -.
DR BioCyc; EcoCyc:EG12396-MON; -.
DR UniPathway; UPA00599; -.
DR PRO; PR:P38097; -.
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; 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 GO; GO:1900231; P:regulation of single-species biofilm formation on inanimate substrate; IMP:EcoCyc.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 3.20.20.450; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF141868; SSF141868; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF55785; SSF55785; 3.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; GTP-binding; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1105
FT /note="Probable diguanylate cyclase DgcE"
FT /id="PRO_0000169122"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 300..370
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 374..426
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 501..552
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 553..623
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 626..680
FT /note="PAC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 712..845
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT DOMAIN 855..1104
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT ACT_SITE 763
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 728
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 737
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 763
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 783
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 725
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT CONFLICT 965..966
FT /note="EQ -> NS (in Ref. 4; K02498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1105 AA; 123887 MW; 22BE64B963CB9739 CRC64;
MSKQSQHVLI ALPHPLLHLV SLGLVSFIFT LFSLELSQFG TQLAPLWFPT SIMMVAFYRH
AGRMWPGIAL SCSLGNIAAS ILLFSTSSLN MTWTTINIVE AVVGAVLLRK LLPWYNPLQN
LADWLRLALG SAIVPPLLGG VLVVLLTPGD DPLRAFLIWV LSESIGALAL VPLGLLFKPH
YLLRHRNPRL LFESLLTLAI TLTLSWLSML YLPWPFTFII VLLMWSAVRL PRMEAFLIFL
TTVMMVSLMM AADPSLLATP RTYLMSHMPW LPFLLILLPA NIMTMVMYAF RAERKHISES
ETHFRNAMEY SAIGMALVGT EGQWLQTNKA LCQFLGYSQE ELRGLTFQQL TWPEDLNKDL
QQVEKLISGE INTYSMEKRY YNRNGDVVWA LLAVSLVRHT DGTPLYFIAQ IEDINELKRT
EQVNQQLMER ITLANEAGGI GIWEWELKPN IFSWDKRMFE LYEIPPHIKP NWQVWYECVL
PEDRQHAEKV IRDSLQSRSP FKLEFRITVK DGIRHIRALA NRVLNKEGEV ERLLGINMDM
TEVKQLNEAL FQEKERLHIT LDSIGEAVVC IDMAMKITFM NPVAEKMSGW TQEEALGVPL
LTVLHITFGD NGPLMENIYS ADTSRSAIEQ DVVLHCRSGG SYDVHYSITP LSTLDGSNIG
SVLVIQDVTE SRKMLRQLSY SASHDALTHL ANRASFEKQL RILLQTVNST HQRHALVFID
LDRFKAVNDS AGHAAGDALL RELASLMLSM LRSSDVLARL GGDEFGLLLP DCNVESARFI
ATRIISAVND YHFIWEGRVH RVGASAGITL IDDNNHQAAE VMSQADIACY ASKNGGRGRV
TVYEPQQAAA HSERAAMSLD EQWRMIKENQ LMMLAHGVAS PRIPEARNLW LISLKLWSCE
GEIIDEQTFR RSFSDPALSH ALDRRVFHEF FQQAAKAVAS KGISISLPLS VAGLSSATLV
NDLLEQLENS PLPPRLLHLI IPAEAILDHA ESVQKLRLAG CRIVLSQVGR DLQIFNSLKA
NMADYLLLDG ELCANVQGNL MDEMLITIIQ GHAQRLGMKT IAGPVVLPLV MDTLSGIGVD
LIYGEVIADA QPLDLLVNSS YFAIN
