ID A0A365L909_9BACL Unreviewed; 658 AA.
AC A0A365L909;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=DP120_04505 {ECO:0000313|EMBL:RAZ81541.1};
OS Planococcus halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=2233542 {ECO:0000313|EMBL:RAZ81541.1, ECO:0000313|Proteomes:UP000251002};
RN [1] {ECO:0000313|EMBL:RAZ81541.1, ECO:0000313|Proteomes:UP000251002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCU63 {ECO:0000313|EMBL:RAZ81541.1,
RC ECO:0000313|Proteomes:UP000251002};
RA Gan L.;
RT "The draft genome sequences of strains SCU63 and S1.";
RL Submitted (JUN-2018) 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:RAZ81541.1}.
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DR EMBL; QLZR01000001; RAZ81541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365L909; -.
DR Proteomes; UP000251002; 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 Reference proteome {ECO:0000313|Proteomes:UP000251002};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..302
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 658 AA; 73568 MW; EB1B8CBDF7863655 CRC64;
MSAFFRKRKL RYPLLALLIL GLVASILIAF VSELIAGIFF FLFAAAFAFT WLIEKRTYEA
TEKHIETLSY RMKKVGEEAL LEMPIGILLA DEEFKIEWAN PYISSVLEYD TLIGESIYSL
SDDFHTLVKS EEIRDLTVTL GDRKYRVYYK SDDRLFYLFD ITEQVEIESL YYADRTVIGI
LFIDNYDELA QGMDDQTRSN LNSLVTSLVN DWGATHGIFV KRVSSDRFMA VFNESILKQL
ETSKFAILDD IREVTAKDNL ALTLSIGVGA GSASLVELGS MAQSGLDLVL GRGGDQVAIK
HPSGKVKFYG GKTNPVEKRT RVRARVISHA LRDLIQDSDQ VFIMGHKMPD MDSIGAAVGV
AKMAAMNKVK ASIVLDFDEY DRSVSRLMEE IESDADLFEQ FITPEEALAD MTDNSLLVVV
DTHKPSMVIE ERLLQRMERV VLIDHHRRGE EFITNTMLVY MEPYASSTAE LVTELIEYQP
KHEKLSMLEA TAMLAGIIVD TKSFTLRTGA RTFEAASYLR ANGADTVLVQ RLLKEDMDTY
LERARIVETV EFVGDGIAIA HGEPDRIYSP VLIAQTADIL LTMKDVNASF VIAERSEGGV
GISARSLGEV NVQVIMENLG GGGHLTNAAT QMPDATIDEA IEKLRETISE IYEGEQTE
//
