ID   DGCQ_ECO57              Reviewed;         564 AA.
AC   Q8XB92;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable diguanylate cyclase DgcQ {ECO:0000250|UniProtKB:P76330};
DE            Short=DGC {ECO:0000250|UniProtKB:P76330};
DE            EC=2.7.7.65 {ECO:0000250|UniProtKB:P76330};
DE   AltName: Full=Cellulose synthesis regulatory protein {ECO:0000250|UniProtKB:P76330};
GN   Name=dgcQ {ECO:0000250|UniProtKB:P76330}; Synonyms=yedQ;
GN   OrderedLocusNames=Z3047, ECs2694;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P31129,
CC       ECO:0000250|UniProtKB:P76330}.
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:0000250|UniProtKB:P76330}.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC       {ECO:0000250|UniProtKB:P76330}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31129}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
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DR   EMBL; AE005174; AAG56970.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36117.1; -; Genomic_DNA.
DR   PIR; F85813; F85813.
DR   PIR; F90965; F90965.
DR   RefSeq; NP_310721.1; NC_002695.1.
DR   RefSeq; WP_001302088.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XB92; -.
DR   SMR; Q8XB92; -.
DR   STRING; 155864.EDL933_2963; -.
DR   EnsemblBacteria; AAG56970; AAG56970; Z3047.
DR   EnsemblBacteria; BAB36117; BAB36117; ECs_2694.
DR   GeneID; 912776; -.
DR   KEGG; ece:Z3047; -.
DR   KEGG; ecs:ECs_2694; -.
DR   PATRIC; fig|386585.9.peg.2822; -.
DR   eggNOG; COG3706; Bacteria.
DR   HOGENOM; CLU_000445_11_23_6; -.
DR   OMA; EWQAWHD; -.
DR   UniPathway; UPA00599; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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_0000169098"
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;  64287 MW;  BEBC2286ADBAECB0 CRC64;
     MQHETKMENQ SWLKKLARRL GPGHIVNLCF IVVLLFSTLL TWREVVVLED AYISSQRNHL
     ENVANALDKH LQYNVDKLIF LRNGMREALV APLDFTSLRD AVTEFEQHRD EHAWQIELNR
     RRTLSVNGVS 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