DGC_VIBC3
ID DGC_VIBC3 Reviewed; 321 AA.
AC A0A0H3AFM6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Diguanylate cyclase {ECO:0000305};
DE EC=2.7.7.65 {ECO:0000269|PubMed:28647124, ECO:0000269|PubMed:31862141};
GN OrderedLocusNames=VC0395_0300 {ECO:0000312|EMBL:ABQ19213.1};
GN ORFNames=GG844_01425 {ECO:0000312|EMBL:QGF29862.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Langlete P., Winther-Larsen H.C., Krabberoed A.K.;
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-237; GLU-238 AND GLU-239.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=26728467; DOI=10.1186/s13568-015-0168-6;
RA Chouhan O.P., Bandekar D., Hazra M., Baghudana A., Hazra S., Biswas S.;
RT "Effect of site-directed mutagenesis at the GGEEF domain of the biofilm
RT forming GGEEF protein from Vibrio cholerae.";
RL AMB Express 6:2-2(2016).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=28647124; DOI=10.1016/j.micres.2017.05.003;
RA Bandekar D., Chouhan O.P., Mohapatra S., Hazra M., Hazra S., Biswas S.;
RT "Putative protein VC0395_0300 from Vibrio cholerae is a diguanylate cyclase
RT with a role in biofilm formation.";
RL Microbiol. Res. 202:61-70(2017).
RN [5]
RP MUTAGENESIS OF GLY-237 AND GLU-238.
RX PubMed=29956605; DOI=10.2174/0929866525666180628162405;
RA Chouhan O.P., Biswas S.;
RT "Subtle changes due to mutations in the GGDEF domain result in loss of
RT biofilm forming activity in the VC0395_0300 protein from Vibrio cholerae,
RT but no major change in the overall structure.";
RL Protein Pept. Lett. 25:740-747(2018).
RN [6] {ECO:0007744|PDB:6EIB}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 161-321, CATALYTIC ACTIVITY, AND
RP DOMAIN.
RX PubMed=31862141; DOI=10.1016/j.bbrc.2019.11.179;
RA Chouhan O.P., Roske Y., Heinemann U., Biswas S.;
RT "Structure of the active GGEEF domain of a diguanylate cyclase from Vibrio
RT cholerae.";
RL Biochem. Biophys. Res. Commun. 523:287-292(2020).
CC -!- FUNCTION: Involved in biofilm formation (PubMed:26728467,
CC PubMed:28647124). Catalyzes the conversion of GTP to c-di-GMP
CC (PubMed:28647124). {ECO:0000269|PubMed:26728467,
CC ECO:0000269|PubMed:28647124}.
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:28647124, ECO:0000269|PubMed:31862141};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28647124};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P31129};
CC -!- DOMAIN: The disordered N-terminal region is not required for
CC diguanylate cyclase activity. {ECO:0000269|PubMed:31862141}.
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DR EMBL; CP000626; ABQ19213.1; -; Genomic_DNA.
DR EMBL; CP045718; QGF29862.1; -; Genomic_DNA.
DR RefSeq; WP_001894530.1; NZ_CP045718.1.
DR PDB; 6EIB; X-ray; 1.94 A; A/B/C/D=161-321.
DR PDBsum; 6EIB; -.
DR AlphaFoldDB; A0A0H3AFM6; -.
DR SMR; A0A0H3AFM6; -.
DR STRING; 345073.VC395_A0964; -.
DR EnsemblBacteria; ABQ19213; ABQ19213; VC0395_0300.
DR KEGG; vco:VC0395_0300; -.
DR PATRIC; fig|345073.21.peg.3689; -.
DR eggNOG; COG2199; Bacteria.
DR OMA; NRRWGAM; -.
DR BRENDA; 2.7.7.65; 15862.
DR Proteomes; UP000000249; Chromosome 1.
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 CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..321
FT /note="Diguanylate cyclase"
FT /id="PRO_0000449415"
FT DOMAIN 28..98
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 102..155
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 187..318
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31129"
FT MUTAGEN 237
FT /note="G->R: 3-fold decrease in biofilm formation. 60%
FT decrease in diguanylate cyclase activity. Does not affect
FT the overall structure."
FT /evidence="ECO:0000269|PubMed:26728467,
FT ECO:0000269|PubMed:29956605"
FT MUTAGEN 238
FT /note="E->K: 2-fold decrease in biofilm formation. 50%
FT decrease in diguanylate cyclase activity. Does not affect
FT the overall structure."
FT /evidence="ECO:0000269|PubMed:26728467,
FT ECO:0000269|PubMed:29956605"
FT MUTAGEN 239
FT /note="E->K: 3-fold decrease in biofilm formation."
FT /evidence="ECO:0000269|PubMed:26728467"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6EIB"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:6EIB"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:6EIB"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:6EIB"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:6EIB"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:6EIB"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:6EIB"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:6EIB"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:6EIB"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:6EIB"
FT HELIX 291..306
FT /evidence="ECO:0007829|PDB:6EIB"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:6EIB"
SQ SEQUENCE 321 AA; 37183 MW; 1F8D77AB19582CE4 CRC64;
MKNWLCQAVR GEPMIELNRI EELFDNQQFS LHELVLNELG VYVFVKNRRG EYLYANPLTL
KLFETNAQSL LGKTDHDFFH DDQLSDILAA DQQVFETRLS VVHEERAIAK SNGLVRIYRA
VKHPILHRVT GEVIGLIGVS TDITDIVELR EQLYQLANTD SLTQLCNRRK LWADFRAAFA
RAKRLRQPLS CISIDIDNFK LINDQFGHDK GDEVLCFLAK LFQSVISDHH FCGRVGGEEF
IIVLENTHVE TAFHLAEQIR QRFAEHPFFE QNEHIYLCAG VSSLHHGDHD IADIYRRSDQ
ALYKAKRNGR NRCCIYRQST E
