ID   CDPD1_VIBCH             Reviewed;         492 AA.
AC   Q9KSG1;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cyclic di-GMP phosphodiesterase VC_1295 {ECO:0000305};
DE            EC=3.1.4.- {ECO:0000269|PubMed:25343965};
GN   OrderedLocusNames=VC_1295 {ECO:0000312|EMBL:AAF94454.1};
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, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
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: Phosphodiesterase (PDE) that catalyzes the hydrolysis of
CC       cyclic diguanylate (c-di-GMP) to GMP in vitro. 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:0000269|PubMed:25343965};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE003852; AAF94454.1; -; Genomic_DNA.
DR   PIR; C82217; C82217.
DR   RefSeq; NP_230940.1; NC_002505.1.
DR   AlphaFoldDB; Q9KSG1; -.
DR   SMR; Q9KSG1; -.
DR   STRING; 243277.VC_1295; -.
DR   PRIDE; Q9KSG1; -.
DR   DNASU; 2614749; -.
DR   EnsemblBacteria; AAF94454; AAF94454; VC_1295.
DR   KEGG; vch:VC_1295; -.
DR   PATRIC; fig|243277.26.peg.1233; -.
DR   eggNOG; COG2770; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   HOGENOM; CLU_044477_0_0_6; -.
DR   OMA; FWLEHNP; -.
DR   BioCyc; VCHO:VC1295-MON; -.
DR   PHI-base; PHI:3232; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF01966; HD; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
PE   1: Evidence at protein level;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..492
FT                   /note="Cyclic di-GMP phosphodiesterase VC_1295"
FT                   /id="PRO_0000439659"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          226..278
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          280..490
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01176"
SQ   SEQUENCE   492 AA;  54566 MW;  E97FC3CAC00A692C CRC64;
     MTIWVLSLAM KNTIYHAPLT FGLYALAGVL FALYTSRVCP FLATLSTREI ATQVGAVFIL
     AWLIRHTLLR QHIWARKQQF IQLDTALLFA MSLPLALYYN LQYQFTLDSN LKVLFGMTLF
     GFFTGALLQL SSKLRTLRQM PQSQNLALSS DERRSLVKQL IGLIVLLIST LTVMLSMVAI
     KDIHWLENNP ARLLDGSGKI SIVKEFAFLS LVLGGYITAI LVLWSRMMKE ILDHQERSLQ
     AVTQGNLQVR LPVYSNDELG NVAMLTNQML DSLEATQNEV KTTRDVAIVS LSALAESRDN
     ETGAHILRTQ EYVKALAEYL AAFPQYSTLL TPAYIELLYK SAPLHDVGKV GIPDSVLLKP
     GKLTDEEFTV MKEHPRIGAQ ALAIAERHLG TSSFLAIAKE IALTHHEKWD GTGYPAQLQG
     EAIPLSGRLM ALADVYDALI SARVYKPAFS HDKAKAIIVE GSGHHFDPAV VEAFLAVEEK
     FVAIAAHFKD AA