VDCA_VIBCH
ID VDCA_VIBCH Reviewed; 339 AA.
AC Q9KKZ4;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Diguanylate cyclase VdcA;
DE Short=DGC;
DE EC=2.7.7.65;
GN Name=vdcA; OrderedLocusNames=VC_A0956;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND MUTAGENESIS OF GLU-258.
RC STRAIN=El Tor C6709 / Serotype O1;
RX PubMed=18227161; DOI=10.1128/iai.01337-07;
RA Tamayo R., Schild S., Pratt J.T., Camilli A.;
RT "Role of cyclic di-GMP during el tor biotype Vibrio cholerae infection:
RT characterization of the in vivo-induced cyclic di-GMP phosphodiesterase
RT CdpA.";
RL Infect. Immun. 76:1617-1627(2008).
CC -!- FUNCTION: Diguanylate cyclase (DGC) that catalyzes the synthesis of
CC cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules.
CC Is involved in the modulation of intracellular c-di-GMP levels. Cyclic-
CC di-GMP is a second messenger which positively regulates biofilm
CC formation and negatively regulates virulence in V.cholerae, and is
CC proposed to play an important role in the transition from persistence
CC in the environment to survival in the host. Overexpression of vdcA
CC results in increased biofilm formation, and reduced motility and
CC virulence. {ECO:0000269|PubMed:18227161}.
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:18227161};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
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DR EMBL; AE003853; AAF96852.1; -; Genomic_DNA.
DR PIR; D82396; D82396.
DR RefSeq; NP_233340.1; NC_002506.1.
DR AlphaFoldDB; Q9KKZ4; -.
DR SMR; Q9KKZ4; -.
DR STRING; 243277.VC_A0956; -.
DR DNASU; 2612301; -.
DR EnsemblBacteria; AAF96852; AAF96852; VC_A0956.
DR KEGG; vch:VC_A0956; -.
DR PATRIC; fig|243277.26.peg.3567; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_5_6; -.
DR OMA; MLKHQIP; -.
DR BioCyc; VCHO:VCA0956-MON; -.
DR BRENDA; 2.7.7.65; 15862.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0052621; F:diguanylate cyclase activity; IBA:GO_Central.
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:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
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 GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..339
FT /note="Diguanylate cyclase VdcA"
FT /id="PRO_0000425961"
FT DOMAIN 206..339
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 258
FT /note="E->A: Loss of DGC activity."
FT /evidence="ECO:0000269|PubMed:18227161"
SQ SEQUENCE 339 AA; 37995 MW; C5C43170A10A7DBF CRC64;
MMTTEDFKKS TANLKKVVPL MMKHHVAATP VNYALWYTYV DQAIPQLNAE MDSVLKNFGL
CPPASGEHLY QQYIATKAET NINQLRANVE VLLGEISSSM SDTLSDTSSF ANVIDKSFKD
LERVEQDNLS IEEVMTVIRR LVSDSKDIRH STNFLNNQLN AATLEISRLK EQLAKVQKDA
LFDSLSGLYN RRAFDGDMFT LIHAGQQVSL IMLDIDHFKA LNDNYGHLFG DQIIRAIAKR
LQSLCRDGVT AYRYGGEEFA LIAPHKSLRI ARQFAESVRR SIEKLTVKDR RSGQSVGSIT
ASFGVVEKIE GDSLESLIGR ADGLLYEAKN LGRNRVMPL
