ID   CDPD2_VIBCH             Reviewed;         441 AA.
AC   Q9KSB1;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable cyclic di-GMP phosphodiesterase VC_1348 {ECO:0000305};
DE            EC=3.1.4.- {ECO:0000269|PubMed:25343965};
GN   OrderedLocusNames=VC_1348 {ECO:0000312|EMBL:AAF94506.1};
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, INDUCTION, AND MUTAGENESIS OF
RP   279-HIS-ASP-280.
RC   STRAIN=El Tor C6706;
RX   PubMed=25343965; DOI=10.1186/s12866-014-0272-9;
RA   McKee R.W., Kariisa A., Mudrak B., Whitaker C., Tamayo R.;
RT   "A systematic analysis of the in vitro and in vivo functions of the HD-GYP
RT   domain proteins of Vibrio cholerae.";
RL   BMC Microbiol. 14:272-272(2014).
CC   -!- FUNCTION: Probable phosphodiesterase (PDE) that catalyzes the
CC       hydrolysis of cyclic diguanylate (c-di-GMP). Increases motility and
CC       decreases biofilm formation in vivo. {ECO:0000269|PubMed:25343965}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclic di-3',5'-guanylate + 2 H2O = 2 GMP + 2 H(+);
CC         Xref=Rhea:RHEA:52928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:58805;
CC         Evidence={ECO:0000250|UniProtKB:Q9KSG1};
CC   -!- INDUCTION: Transcripts are more abundant in biofilm cells than in
CC       planktonic cells. {ECO:0000269|PubMed:25343965}.
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DR   EMBL; AE003852; AAF94506.1; -; Genomic_DNA.
DR   PIR; G82211; G82211.
DR   AlphaFoldDB; Q9KSB1; -.
DR   SMR; Q9KSB1; -.
DR   STRING; 243277.VC_1348; -.
DR   DNASU; 2614802; -.
DR   EnsemblBacteria; AAF94506; AAF94506; VC_1348.
DR   KEGG; vch:VC_1348; -.
DR   eggNOG; COG3437; Bacteria.
DR   HOGENOM; CLU_000445_92_10_6; -.
DR   OMA; LMKAGPL; -.
DR   BioCyc; VCHO:VC1348-MON; -.
DR   PHI-base; PHI:3230; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProt.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   c-di-GMP; Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..441
FT                   /note="Probable cyclic di-GMP phosphodiesterase VC_1348"
FT                   /id="PRO_0000439660"
FT   DOMAIN          72..187
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          214..425
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01176"
FT   MOD_RES         120
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MUTAGEN         279..280
FT                   /note="HD->AA: Does not increase motility."
FT                   /evidence="ECO:0000269|PubMed:25343965"
SQ   SEQUENCE   441 AA;  49422 MW;  5531BFC5786ACEB4 CRC64;
     MATANIAIKQ NSSTNIAFIE RMPSPSLHRI LYNLFSKFSY SLSNSCHFNL KCLNFVMNRM
     FHMSMEDLSQ CTILIVDDSP DNIAFMSQGL AQYYRIKAAR SGKVALEILA QYPIDLVLLD
     IVMPEMSGYE VINQIKHNPH TEHIPVIFLT GKSNPEDEQL GFELGAVDYV FKPVSIPLLK
     SRVHTHLQNK RSKDILLNQN DYLETEVLRR SGELDRMQDA VVFALASLAE TRDPETGNHL
     LRTQHYVKVL AQRLATTDKY RDVLSPTVID TYFKAAPLHD IGKVGIPDNI LLKPGKLTPD
     EFTTMRNHAL LGKLALEKAE KLSGACTALI NVAKEIAMGH HEKWDGSGYP LGLKGDDIPL
     SARLMALADV YDALICRRVY KEPMSHEEAK AIILQGRGSH FDPMVIDAFL IEEQNFIDIA
     QKFADEESAM VPIQLGQQAS G