ID   Q1I952_PSEE4            Unreviewed;       514 AA.
AC   Q1I952;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE            EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN   OrderedLocusNames=PSEEN3057 {ECO:0000313|EMBL:CAK15826.1};
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK15826.1, ECO:0000313|Proteomes:UP000000658};
RN   [1] {ECO:0000313|EMBL:CAK15826.1, ECO:0000313|Proteomes:UP000000658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48 {ECO:0000313|EMBL:CAK15826.1,
RC   ECO:0000313|Proteomes:UP000000658};
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine +
CC         H(+); Xref=Rhea:RHEA:24902, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58754, ChEBI:CHEBI:58805; EC=3.1.4.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00034290};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CT573326; CAK15826.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1I952; -.
DR   STRING; 384676.PSEEN3057; -.
DR   KEGG; pen:PSEEN3057; -.
DR   eggNOG; COG2200; Bacteria.
DR   HOGENOM; CLU_000445_131_0_6; -.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IEA:UniProtKB-EC.
DR   CDD; cd01948; EAL; 1.
DR   Gene3D; 3.20.20.450; EAL domain; 1.
DR   InterPro; IPR024744; CSS-motif_dom.
DR   InterPro; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
DR   PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR   PANTHER; PTHR33121:SF80; CYCLIC DI-GMP PHOSPHODIESTERASE PDEL-RELATED; 1.
DR   Pfam; PF12792; CSS-motif; 1.
DR   Pfam; PF00563; EAL; 1.
DR   SMART; SM00052; EAL; 1.
DR   SUPFAM; SSF141868; EAL domain-like; 1.
DR   PROSITE; PS50883; EAL; 1.
PE   4: Predicted;
KW   c-di-GMP {ECO:0000256|ARBA:ARBA00022636};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          244..498
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
SQ   SEQUENCE   514 AA;  56530 MW;  40EEA8BFA9CE8B3C CRC64;
     MLLPWCVGVL PLLCGVAVMR WQTERELQAS SAATAREVVK HLETVLDSLS IAARHLLPKA
     GQPCQDAQLA LRIEVTRNAF VRSTNLFERD TLYCSSLFGD FDEPVDASDY TGGQLWLMDG
     NSVTPGQPLL AYRVSEGDRG AITTVDGNHL LTALRLIGED EELQVQVGNH WMGRDGLVRN
     GTPPVAASAA VTFSSTRYPI SVHGGYGPAK PGELMRSRYP ALLSLLLVLG ILAGATCRWQ
     IRRASSPRAE LHRALEAGEF LPYFQPVVRK GDYHWAGVEV LMRWQHPREG LVRPDLFIPY
     AEHSGQIVAM TRSLMLNTAQ ALAPHAELLE DGFHIGINIT ADHCRDLGLL DDCQTFLQHF
     PPGRVVLTLE LTERKLIEPT PVTLELFEKL HAMGVMIALD DFGTGQSSLN YLRQFKVDYL
     KIDQSFVAMI GGDALSQHIL DTIIELSAKL GLGIVAEGVE TDIQRDYLAR HGVDFQQGYL
     FARPMPIAEL LLALAARPGG PRLPQGAAPE IMRG
//