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
//