ID   CDGJ_VIBCH              Reviewed;         432 AA.
AC   Q9KVK6;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cyclic di-GMP phosphodiesterase CdgJ {ECO:0000305};
DE            EC=3.1.4.52 {ECO:0000269|PubMed:20622061};
GN   Name=cdgJ {ECO:0000303|PubMed:20622061};
GN   OrderedLocusNames=VC_0137 {ECO:0000312|EMBL:AAF93314.1};
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, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   46-GLU--LEU-48.
RC   STRAIN=El Tor A1552 / Serotype O1;
RX   PubMed=20622061; DOI=10.1128/jb.00209-10;
RA   Liu X., Beyhan S., Lim B., Linington R.G., Yildiz F.H.;
RT   "Identification and characterization of a phosphodiesterase that inversely
RT   regulates motility and biofilm formation in Vibrio cholerae.";
RL   J. Bacteriol. 192:4541-4552(2010).
CC   -!- FUNCTION: Phosphodiesterase (PDE) that catalyzes the hydrolysis of
CC       cyclic diguanylate (c-di-GMP). Positively regulates motility and
CC       negatively regulates biofilm formation. {ECO:0000269|PubMed:20622061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclic di-3',5'-guanylate + H2O = 5'-
CC         phosphoguanylyl(3'->5')guanosine + H(+); Xref=Rhea:RHEA:24902,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58754,
CC         ChEBI:CHEBI:58805; EC=3.1.4.52;
CC         Evidence={ECO:0000269|PubMed:20622061};
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant exhibits decreased motility.
CC       Mutation causes a slight decrease in flaA expression but does not
CC       affect flagellar morphology. Mutant has enhanced biofilm formation and
CC       vps gene expression. {ECO:0000269|PubMed:20622061}.
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DR   EMBL; AE003852; AAF93314.1; -; Genomic_DNA.
DR   PIR; H82358; H82358.
DR   AlphaFoldDB; Q9KVK6; -.
DR   SMR; Q9KVK6; -.
DR   STRING; 243277.VC_0137; -.
DR   DNASU; 2615266; -.
DR   EnsemblBacteria; AAF93314; AAF93314; VC_0137.
DR   KEGG; vch:VC_0137; -.
DR   eggNOG; COG3434; Bacteria.
DR   HOGENOM; CLU_044951_2_0_6; -.
DR   OMA; RQPIFNR; -.
DR   BioCyc; VCHO:VC0137-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.450; -; 1.
DR   InterPro; IPR014408; dGMP_Pdiesterase_EAL/HD-GYP.
DR   InterPro; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
DR   InterPro; IPR013976; HDOD.
DR   Pfam; PF00563; EAL; 1.
DR   Pfam; PF08668; HDOD; 1.
DR   PIRSF; PIRSF003180; DiGMPpdiest_YuxH; 1.
DR   SMART; SM00052; EAL; 1.
DR   SUPFAM; SSF141868; SSF141868; 1.
DR   PROSITE; PS50883; EAL; 1.
DR   PROSITE; PS51833; HDOD; 1.
PE   1: Evidence at protein level;
KW   c-di-GMP; Hydrolase; Reference proteome.
FT   CHAIN           1..432
FT                   /note="Cyclic di-GMP phosphodiesterase CdgJ"
FT                   /id="PRO_0000439658"
FT   DOMAIN          1..232
FT                   /note="EAL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT   DOMAIN          226..413
FT                   /note="HDOD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01177"
FT   MUTAGEN         46..48
FT                   /note="ELL->AAA: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:20622061"
SQ   SEQUENCE   432 AA;  50458 MW;  B853D23F69703A7D CRC64;
     MVRCLWAAEC CWLPPKRKQP FEDTMYTTYV ARQPILNAKR HTLGYELLFR DGEKNAFPEY
     MDADRATYRL IVENFLSLGT NPRIARSRCF INFPHKSLIR RLPLTLPREQ IVVEILETCQ
     PTDDLFEAVQ ELSQRGYLLA LDDFVYSPAW ERFLPYVQIV KIDIMAMGLD KACEFVRGRL
     AQGSRRRFLA ERVETEDEFH QARHAGFTFF QGYFFSKPEI IKQRYVSPEH VIAMQLFREV
     CQPEVDYVRV ERLVAQDIAL SYKLLRFVNT MSDRISVSIS SFRQALVYLG QDKLRIFVSL
     AVASYISSKK PKELYNLSLQ RAQFCQLMAT HTHFKAHREQ AFLIGMFSVL DALLDTSIEQ
     LVEQLPLADD VKLALREREG PLGTLLDLEE CFEKADWQGV EQHCLELGFD LEDVRQELIE
     AQRWSQDINR LI