ID A0A347STG1_9LACO Unreviewed; 679 AA.
AC A0A347STG1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=DS830_07425 {ECO:0000313|EMBL:AXX65320.1};
OS Bombilactobacillus bombi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1303590 {ECO:0000313|EMBL:AXX65320.1, ECO:0000313|Proteomes:UP000261753};
RN [1] {ECO:0000313|EMBL:AXX65320.1, ECO:0000313|Proteomes:UP000261753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI-2.5 {ECO:0000313|EMBL:AXX65320.1,
RC ECO:0000313|Proteomes:UP000261753};
RX PubMed=30249635; DOI=10.1073/pnas.1803880115;
RA Motta E.V., Raymann K., Moran N.A.;
RT "Glyphosate perturbs the gut microbiota of honey bees.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:10305-10310(2018).
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}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. 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}.
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DR EMBL; CP031513; AXX65320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347STG1; -.
DR KEGG; lbm:DS830_07425; -.
DR Proteomes; UP000261753; Chromosome.
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..315
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 679 AA; 75683 MW; A261EC8C54176F09 CRC64;
MDKDKMAKKS LLALNWPLKI SLIVILILAI SLVIVGFFVN PILAFLEAII LAFILSIGIY
AFISLIKQTT KYLDDLSFRE DRGEQEALIN IPLGMLLYSD NKEHTVQWIN PKLQNYFGKK
DIIGNPLAKV DSQLEQLIKQ DAEHPTNINL IKIGKSRFKA TVQTDLRVIY LLDVTTYENI
QKHYEEEKIA IGQIFLDNYD EVTQSMEDRD QSNLTNYVTN QLTDWAKSNS MFIKRVSEDQ
FIVIAYARSL AAVEQDNFAI LDKIRRDTSK QNYPLTLSVG FAYGRSDLGE LARDAQKNLD
LALGRGGDQV VVKKADEKAR FYGGNTNPME KRTRVRARMI SQALRDLFNQ TADIYVMGHA
QPDMDVLGAC LGIHRIAQMN DKKCHIVVDR NNNHTDIERL LKLIDDDADL KADLISPAAA
IEQANSDSML IMVDTSKPSI SMSTKLCQKL ADHLVVIDHH RRGEEFPPNP LLVYIEPYAS
SACELITEMV EYQPQTRASL SKLEATAMLA GISVDTRSFT LRSGTRTFDA ASYLRSVGAD
GTLVQNLLKE NVDSYIQKSH LIDTITMITS DIALCAGQDD QVYDSVIAAQ AADTLLSLNN
IEAAFVITKR NDGKIAISAR SLGKINVQVI MEEMGGGGHL SNAATQLAET TIADAKQQLI
AIVQQKVENK STKKTNNNS
//
