ID A0A0R2JSA5_9LACO Unreviewed; 675 AA.
AC A0A0R2JSA5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=IV52_GL001411 {ECO:0000313|EMBL:KRN78277.1};
OS Fructilactobacillus lindneri DSM 20690 = JCM 11027.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN78277.1, ECO:0000313|Proteomes:UP000051565};
RN [1] {ECO:0000313|EMBL:KRN78277.1, ECO:0000313|Proteomes:UP000051565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN78277.1,
RC ECO:0000313|Proteomes:UP000051565};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRN78277.1}.
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DR EMBL; JQBT01000036; KRN78277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2JSA5; -.
DR STRING; 53444.AYR59_01480; -.
DR PATRIC; fig|1122148.6.peg.1449; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000051565; 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 InterPro; IPR029787; Nucleotide_cyclase.
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 SUPFAM; SSF55073; Nucleotide cyclase; 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:UP000051565};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..313
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 675 AA; 76342 MW; 529ADA9E919AC087 CRC64;
MKKSLRHLNL PPFLKNKRLR NISLFIAISL ILGLVIAFIY NVVIGLVLLI LASAGLTYTI
KELNIVEENT TKYVTDLSYL VSRGERESLL EMPIGILILD DDHRINWVNP YLQPYFGNNK
IFGKSLEEIA PELFDLIQEN WNEDEPFEIT WRGKHFTILI QRQYNTIYLM DITHYADVEV
KYENEKIVIG EVYLDNFDEV SQSMSDQEIS NLRNYVTNKL STWAKDYGVY LKRIDADHYM
IMMYVQALRE IEADKFNILD IIRKGTLQQN FPITLSIGIA YGDTDLNQLA DLAQNNLDLA
LGRGGDQAVI KPRDGEARFY GGKTNPMEKR TRVRARMITN ALQELMRTSD KIFVDGHQQP
DMDCWGAALG IRRIAQMNNK ECYIVFDDKD VHTDIKRLLD KIDDYPDILD SIVTPDKAVK
MATDESLLIM VDHSNPNIGV AKNLYERLIN RIVIIDHHRR GEDFPANPLL AYVEPYASSA
CELITEMFEY QSQSADPIND LEATVMLTGI VVDTQSFKVR TGTRTFDAAS YLRSAGADVD
EISSFMKENP NNYMAENHLI SLVNFVDDNL ALITAEDDVK YDSVTAAKAV DSLLSIDGVE
ASFVVYRRMD GNVGISARST GAINVQLIME ALGGGGHLVA GATQIKDKTV AEANEMLTEV
IDQKLFDNSN NKSDE
//
