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Database: UniProt
Entry: I3TXJ9_TISMK
LinkDB: I3TXJ9_TISMK
Original site: I3TXJ9_TISMK 
ID   I3TXJ9_TISMK            Unreviewed;       560 AA.
AC   I3TXJ9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=cyclic-guanylate-specific phosphodiesterase {ECO:0000256|ARBA:ARBA00012282};
DE            EC=3.1.4.52 {ECO:0000256|ARBA:ARBA00012282};
GN   OrderedLocusNames=TMO_c0877 {ECO:0000313|EMBL:AFK57487.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM3 {ECO:0000313|EMBL:AFK57487.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK57487.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK57487.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003239; AFK57487.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TXJ9; -.
DR   KEGG; tmo:TMO_c0877; -.
DR   HOGENOM; CLU_000445_131_1_5; -.
DR   Proteomes; UP000005258; Plasmid pTM3.
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:SF56; CYCLIC DI-GMP PHOSPHODIESTERASE PDEB-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, ECO:0000256|SAM:Phobius};
KW   Plasmid {ECO:0000313|EMBL:AFK57487.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          297..549
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
SQ   SEQUENCE   560 AA;  60398 MW;  C0CB491A49AB5EE2 CRC64;
     MAGALVRTMV TAGRAAFQGD GMRRRVLAVT LTLATLIGAL PVAGSLWIAW ENARRVETDL
     LIRATREMLT RSERLQEDAT RALAAMAAVP VGDACTPAGL ARLRTAAFAS RGVREVGVVE
     EGRVVCTGAG RLDSPMPLPL PDMSVGDMRI WYDRLPPGLD DSARAASRTT VIARGPYAVF
     LDTEQIYDLV LAEPRVVLSM VALGTGQVLG VRTRPERAIL SDMVDRFRNQ TEPEAIRLGD
     RLVVAATARD GTAMALASEP VSVVIETWRE QALLMGLPGL ASGGLIFWLI VTLVRRGDTM
     GARIRRGLAR GEFRVVYQPI VRLADGACLG GEALVRWQQR DGSMISPDRF IPVAEAEGLI
     ERLTDEIIEH VFADLGKFLA ARPSVWIAIN LSASDVESDR VRGRLDRLRK THGVAAAQIV
     LEATERTLID ARRAQSSMRS FRDAGYRLTI DDFGTGYSSL AYLATLPVDG LKLDKTFVDG
     IGSGSAADDV MGHILSLAAT LGLDVAAEGV EHQAQADYLI ARGVTYGQGW LYARAMDGNA
     FCGYVDGHLP AAPLANRRRA
//
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