DGCQ_ECOLI
ID DGCQ_ECOLI Reviewed; 564 AA.
AC P76330; P94746;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable diguanylate cyclase DgcQ {ECO:0000305};
DE Short=DGC {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000250|UniProtKB:P31129};
DE AltName: Full=Cellulose synthesis regulatory protein;
GN Name=dgcQ {ECO:0000303|PubMed:26148715}; Synonyms=yedQ;
GN OrderedLocusNames=b1956, JW5832;
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 REGULATION PATHWAY.
RC STRAIN=1094;
RX PubMed=16585767; DOI=10.1128/jb.188.8.3073-3087.2006;
RA Da Re S., Ghigo J.-M.;
RT "A CsgD-independent pathway for cellulose production and biofilm formation
RT in Escherichia coli.";
RL J. Bacteriol. 188:3073-3087(2006).
RN [5]
RP INDUCTION, AND RPOS-DEPENDENCE.
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 [6]
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 [7]
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 [8]
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 [9]
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). Cyclic-di-GMP is a
CC second messenger which controls cell surface-associated traits in
CC bacteria. Involved in the regulation of cellulose production
CC (PubMed:20303158). {ECO:0000250|UniProtKB:P31129,
CC ECO:0000269|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: Glycan metabolism; bacterial cellulose biosynthesis.
CC {ECO:0000305}.
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: Constitutively expressed at both 28 and 37 degrees Celsius.
CC Induced by 0.3 M NaCl. Expression is RpoS dependent.
CC {ECO:0000269|PubMed:17010156, ECO:0000269|PubMed:19332833}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases swimming motility
CC and early biofilm formation (PubMed:21181144). Disruption 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 (PubMed:20303158). {ECO:0000269|PubMed:20303158,
CC ECO:0000269|PubMed:21181144}.
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DR EMBL; U00096; AAC75022.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15784.1; -; Genomic_DNA.
DR PIR; H64959; H64959.
DR RefSeq; NP_416465.2; NC_000913.3.
DR RefSeq; WP_001350521.1; NZ_LN832404.1.
DR AlphaFoldDB; P76330; -.
DR SMR; P76330; -.
DR BioGRID; 4261052; 3.
DR STRING; 511145.b1956; -.
DR TCDB; 9.B.34.1.4; the kinase/phosphatase/cyclic-gmp synthase/cyclic di-gmp hydrolase (kpsh) family.
DR jPOST; P76330; -.
DR PaxDb; P76330; -.
DR PRIDE; P76330; -.
DR EnsemblBacteria; AAC75022; AAC75022; b1956.
DR EnsemblBacteria; BAA15784; BAA15784; BAA15784.
DR GeneID; 946471; -.
DR KEGG; ecj:JW5832; -.
DR KEGG; eco:b1956; -.
DR PATRIC; fig|1411691.4.peg.296; -.
DR EchoBASE; EB3794; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_23_6; -.
DR OMA; EWQAWHD; -.
DR PhylomeDB; P76330; -.
DR BioCyc; EcoCyc:G7049-MON; -.
DR BioCyc; MetaCyc:G7049-MON; -.
DR UniPathway; UPA00599; -.
DR UniPathway; UPA00694; -.
DR PRO; PR:P76330; -.
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:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
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; IPR033416; CHASE7.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF17151; CHASE7; 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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Cellulose biosynthesis; GTP-binding;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..564
FT /note="Probable diguanylate cyclase DgcQ"
FT /id="PRO_0000169097"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 428..563
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 479
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 441
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 564 AA; 64283 MW; 05FB02C1BE2A8938 CRC64;
MQHETKMENQ SWLKKLARRL GPGHVVNLCF IVVLLFSTLL TWREVVVLED AYISSQRNHL
ENVANALDKH LQYNVDKLIF LRNGMREALV APLDFTSLRD AVTEFEQHRD EHAWKIELNR
RRTLPVNGVS DALVSEGNLL SRENESLDNE ITAALEVGYL LRLAHNSSSM VEQAMYVSRA
GFYVSTQPTL FTRNVPTRYY GYVTQPWFIG HSQRENRHRA VRWFTSQPEH ASNTEPQVTV
SVPVDSNNYW YGVLGMSIPV RTMQQFLRNA IDKNLDGEYQ LYDSKLRFLT SSNPDHPTGN
IFDPRELALL AQAMEHDTRG GIRMDSRYVS WERLDHFDGV LVRVHTLSEG VRGDFGSISI
ALTLLWALFT TMLLISWYVI RRMVSNMYVL QSSLQWQAWH DTLTRLYNRG ALFEKARPLA
KLCQTHQHPF SVIQVDLDHF KAINDRFGHQ AGDRVLSHAA GLISSSLRAQ DVAGRVGGEE
FCVILPGASL TEAAEVAERI RLKLNEKEML IAKSTTIRIS ASLGVSSSEE TGDYDFEQLQ
SLADRRLYLA KQAGRNRVFA SDNA
