DGCA_TREDE
ID DGCA_TREDE Reviewed; 371 AA.
AC Q73RG3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Diguanylate cyclase A {ECO:0000303|PubMed:33452878};
DE Short=DGC {ECO:0000303|PubMed:33452878};
DE EC=2.7.7.65 {ECO:0000269|PubMed:33452878};
GN Name=dgcA {ECO:0000303|PubMed:33452878};
GN OrderedLocusNames=TDE_0125 {ECO:0000312|EMBL:AAS10623.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-273; ASP-276 AND
RP 282-GLY-GLY-283.
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=33452878; DOI=10.1093/femspd/ftab004;
RA Patel D.T., O'Bier N.S., Schuler E.J.A., Marconi R.T.;
RT "The Treponema denticola DgcA protein (TDE0125) is a functional diguanylate
RT cyclase.";
RL Pathog. Dis. 79:0-0(2021).
CC -!- FUNCTION: Catalyzes the conversion of GTP to cyclic-di-GMP (c-di-GMP).
CC Shows activity under aerobic and anaerobic reaction conditions.
CC {ECO:0000269|PubMed:33452878}.
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:0000269|PubMed:33452878};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:33452878};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:33452878};
CC Note=Shows higher activity with Mn(2+) than Mg(2+).
CC {ECO:0000269|PubMed:33452878};
CC -!- ACTIVITY REGULATION: Allosterically regulated by a feedback inhibition
CC loop. {ECO:0000269|PubMed:33452878}.
CC -!- SUBUNIT: Exists as a homodimer and as larger aggregates. Both dimers
CC and aggregates possess DGC activity. {ECO:0000269|PubMed:33452878}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33452878}.
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DR EMBL; AE017226; AAS10623.1; -; Genomic_DNA.
DR RefSeq; NP_970742.1; NC_002967.9.
DR SMR; Q73RG3; -.
DR STRING; 243275.TDE_0125; -.
DR EnsemblBacteria; AAS10623; AAS10623; TDE_0125.
DR KEGG; tde:TDE_0125; -.
DR PATRIC; fig|243275.7.peg.125; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_24_12; -.
DR OMA; TTDMMTK; -.
DR OrthoDB; 1635706at2; -.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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 Allosteric enzyme; Cytoplasm; GTP-binding; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..371
FT /note="Diguanylate cyclase A"
FT /id="PRO_0000453204"
FT DOMAIN 233..366
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT SITE 246
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 273
FT /note="R->A: Forms dimers and tetramers and shows enhanced
FT activity; when associated with A-276."
FT /evidence="ECO:0000269|PubMed:33452878"
FT MUTAGEN 276
FT /note="D->A: Forms dimers and tetramers and shows enhanced
FT activity; when associated with A-273."
FT /evidence="ECO:0000269|PubMed:33452878"
FT MUTAGEN 282..283
FT /note="GG->AA: Loss of activity. Forms exclusively large
FT aggregates."
FT /evidence="ECO:0000269|PubMed:33452878"
SQ SEQUENCE 371 AA; 41992 MW; EBBE02028C3310FB CRC64;
MKTTPNEKLL KKALHSCNNK KYADKILHQE KEIFDLKQLL QISKSLNSVL EFDRLIEAIL
YIVMAQLKTL GAAIFTKKSF DDNLFVLNRD HYGFDIIRDA QYSINVDHPL INFLDKSDSG
CTPDEISKNI KTDKIVKDLF SLSPSFFVPL KAKNRMIGFL LLGEKMESSH QFTDYEKNII
ENIASLAAIA INNSQLLEMT TTDIMTHLKL KHYFFTLLME HLYTINSSGE KKETLSILMI
DIDFFKNIND TYGHAAGDIV LEEVAKIIKS CTRNADTAAR YGGEEFIVML NNTSASAAMA
VAERIRKSVE EKSIMYDGKK INVTISIGVS SYNFDLESAK SIVERADKAL YESKQNGRNR
VTLSKNNLPK A
