ID A0A0M0G8W6_SPOGL Unreviewed; 657 AA.
AC A0A0M0G8W6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=AF332_03385 {ECO:0000313|EMBL:KON85947.1};
OS Sporosarcina globispora (Bacillus globisporus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1459 {ECO:0000313|EMBL:KON85947.1, ECO:0000313|Proteomes:UP000037109};
RN [1] {ECO:0000313|Proteomes:UP000037109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10036 dsm4.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has phosphodiesterase (PDE) activity against cyclic-di-AMP
CC (c-di-AMP). {ECO:0000256|PIRNR:PIRNR026583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-
CC adenosine + H(+); Xref=Rhea:RHEA:54420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:71500, ChEBI:CHEBI:138171;
CC Evidence={ECO:0000256|PIRNR:PIRNR026583};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GdpP/PdeA phosphodiesterase family.
CC {ECO:0000256|PIRNR:PIRNR026583}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KON85947.1}.
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DR EMBL; LGUF01000007; KON85947.1; -; Genomic_DNA.
DR RefSeq; WP_053433310.1; NZ_LGUF01000007.1.
DR AlphaFoldDB; A0A0M0G8W6; -.
DR STRING; 1459.AF332_03385; -.
DR PATRIC; fig|1459.3.peg.687; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000037109; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106409; F:cyclic-di-AMP phosphodiesterase activity; IEA:RHEA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.310.30; -; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR049553; GdpP-like_PAS.
DR InterPro; IPR014528; GdpP/PdeA.
DR InterPro; IPR000160; GGDEF_dom.
DR PANTHER; PTHR47618; BIFUNCTIONAL OLIGORIBONUCLEASE AND PAP PHOSPHATASE NRNA; 1.
DR PANTHER; PTHR47618:SF2; CYCLIC-DI-AMP PHOSPHODIESTERASE GDPP; 1.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF21370; GdpP_PAS; 1.
DR PIRSF; PIRSF026583; YybT; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR026583}; Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..301
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 657 AA; 74381 MW; D9634A534AE68616 CRC64;
MPSYLEKRSI RYPIFGLMGI TVVLLGILAY YNWLFALIGL ILAILPFYYL FQLIQQHRKD
TEEYISTLSY RVKKVGEEAL MEMPIGIMLI NDDYYIEWTN PFLASCFDED TLVGRSLYDV
ADSLVPLIKQ EVETEIITLH DRKFRVIHKP EERLLYFFDV TEQTEIEKMY QEERTVIAII
YLDNYDELTQ GMDDQTKSSL NSLVTQILNK WAQDNGVFLK RVSSERFIAV FNEHILQLLE
KGKFSILDDV RETTSKQNVP LTLSVGVGTG VSSLPELGSL AQSSLDLALG RGGDQVAIKQ
TNGKVKFFGG KTNPVEKRTR VRARVISHAL KELISESDKV IIMGHKSPDM DAIGAAIGIQ
KVARLNQREG YVVVNFNELD TGVRRMMKEI EKNEELFSKF ITPDQAMEIA TDDTLLVVVD
THKPSMVIEE KLLHKIEHVV VIDHHRRAEE FIHNPLLVYM EPYASSTAEL VTELLEYQPR
NGRIEMLEAT ALLAGIIVDT KSFSLRTGSR TFDAASYLRG QGADTVLVQK FLKEDVDTYI
KRAKLIETVQ FYREGIAIAK GQPDQIFDQV LIAQTADTLL TMDGVVSSFV ISNRSENMIG
VSARSLGDIN VQVIMENLEG GGHLTNAATQ LHDATLDDVE VRLKEAIDEY FEGRKKE
//