ID A4XT96_PSEMY Unreviewed; 520 AA.
AC A4XT96;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN OrderedLocusNames=Pmen_1798 {ECO:0000313|EMBL:ABP84562.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84562.1};
RN [1] {ECO:0000313|EMBL:ABP84562.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP84562.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP000680; ABP84562.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XT96; -.
DR STRING; 399739.Pmen_1798; -.
DR KEGG; pmy:Pmen_1798; -.
DR PATRIC; fig|399739.8.peg.1825; -.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_000445_131_0_6; -.
DR OrthoDB; 675397at2; -.
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 258..512
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 520 AA; 57291 MW; A0BE6214F6969A61 CRC64;
MPLTAYRTRR SRLRLCASLA VGMLPVVLGL MFLYAQAGIV LRDISRTSAA DAVRQIDLML
DNASQAAGEV LPQVGRPCAE VELVLREQVA TVPFVRSVNL MDGGRLYCSS LFGAFEEPVD
SAAYVAGRLR LLAGNPVTPN HSLLVYRDVV DERGALVAID GRYLANVLQS VDRGAFMQLL
VGEQWMPRSG LVRAGRLPEY PLARVALSST RYPYQVRAAF PRGARLRYMG EQYPVLFVLL
GLLGALAGVG SHWLLARSSS PSLELRRALQ AGEFIPYFQP LVRSGTQQWI GAEVLMRWQH
PREGLVRPDL FIPLAESSGL IVPMTRELMR QTAELLAPVA DRLGGGFHVG INIAAAHCRS
RELVEDCRNF LQAFEPGQVV LSLELTEREL LEPDAFTDQL FADLHEMGVK IALDDFGTGH
SSLSYLHKLK VDYLKIDQSF VAMIGKDALS LHILDSVIDL CAKLQLEVIA EGVEDELQLR
YLGNRRVDYL QGYLFGRPLP AAEFVACALD EPAASVQLPG
//
