ID   D4GG59_PANAM            Unreviewed;       521 AA.
AC   D4GG59;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE            EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN   Name=yoaD {ECO:0000313|EMBL:ADD77310.1};
GN   OrderedLocusNames=PANA_2143 {ECO:0000313|EMBL:ADD77310.1};
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD77310.1, ECO:0000313|Proteomes:UP000001702};
RN   [1] {ECO:0000313|EMBL:ADD77310.1, ECO:0000313|Proteomes:UP000001702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD77310.1,
RC   ECO:0000313|Proteomes:UP000001702};
RX   PubMed=20348253; DOI=10.1128/JB.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA   Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(2010).
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; CP001875; ADD77310.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GG59; -.
DR   STRING; 706191.PANA_2143; -.
DR   KEGG; pam:PANA_2143; -.
DR   eggNOG; COG4943; Bacteria.
DR   HOGENOM; CLU_000445_131_2_6; -.
DR   Proteomes; UP000001702; 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:SF9; CYCLIC DI-GMP PHOSPHODIESTERASE PDED-RELATED; 1.
DR   PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 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   Reference proteome {ECO:0000313|Proteomes:UP000001702};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          267..516
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
SQ   SEQUENCE   521 AA;  59034 MW;  D943956539D96C55 CRC64;
     MMFMAQQYVG QYRRKRLLIA LVIASIVLTL TLAFRYFEEK SRIQKRAISF ADTAITRFDR
     MFSPLDVSAN NMLGLVGMPC QDARFPLIEK ISSLQTVRAV LLVDGDTLYC SSIFGTRDIS
     FSQTYPELAL NDRRMVLSTD EYLLKGSPVL LLWTPTTLDN RSGILQAINI ELMSSYLLEP
     QAPWVERAIF NVNGKSLEYG NPLIESTQPS EDEVTYTEAS LRYPYTVTLY GPSPSRLALE
     SLPSQLPLAL MLSLLIGYVV WLATANRMSL SWQISYGITA REFMVYCQPL INARTSECEG
     IELLLRWHNP RQGWIPPDVF IPLVERQNLI KPLTRFVLNR VVEALPDLPH SPHFHIAINV
     AASHFRDRAI LEDLQTLWWP AEPVPTLVVE LTERDALPVV DQAVISQLHD IGVRLAIDDF
     GTGHSSLSYL KDLQPDVLKL DKIFTASIGT DAINAIVTDM VISLAQRLNI SLVAEGVETE
     EQAHYLRDRG VEHLQGYYFA RPMPLEDFPE WLRQHQLTLG L
//