ID A0A0R2A0Z6_9LACO Unreviewed; 672 AA.
AC A0A0R2A0Z6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-OCT-2025, entry version 33.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=FC26_GL000148 {ECO:0000313|EMBL:KRM60672.1};
OS Paucilactobacillus vaccinostercus DSM 20634.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM60672.1, ECO:0000313|Proteomes:UP000051733};
RN [1] {ECO:0000313|EMBL:KRM60672.1, ECO:0000313|Proteomes:UP000051733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM60672.1,
RC ECO:0000313|Proteomes:UP000051733};
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 Genome Announc. 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR026583-50};
CC Note=For phosphodiesterase activity, probably binds 2 Mn(2+) per
CC subunit. {ECO:0000256|PIRSR:PIRSR026583-50};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KRM60672.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYYY01000061; KRM60672.1; -; Genomic_DNA.
DR RefSeq; WP_057779814.1; NZ_AYYY01000061.1.
DR AlphaFoldDB; A0A0R2A0Z6; -.
DR STRING; 1423813.FC26_GL000148; -.
DR PATRIC; fig|1423813.3.peg.160; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000051733; 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 FunFam; 3.90.1640.10:FF:000002; Cyclic-di-AMP phosphodiesterase; 1.
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; IPR051319; Oligoribo/pAp-PDE_c-di-AMP_PDE.
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; PF24898; GGDEF_GdpP; 1.
DR Pfam; PF21370; PAS_GdpP; 1.
DR PIRSF; PIRSF026583; YybT; 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 Manganese {ECO:0000256|PIRSR:PIRSR026583-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026583};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR026583-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051733};
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..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..312
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 431
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 431
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 456
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 512
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ SEQUENCE 672 AA; 76239 MW; 7C5C2C9ED885B09A CRC64;
MKLFEREKLP FFFRNSRVSW IALFLFVVSA AGIIFAFITN VILGVIVLIL IAFGLYFVMV
ALQRLVLDTN QYLTDLAYHI KRGQQEAFLQ MPIGMIIFNE QREVEWVNPY MVKYFDQQEV
IGKTLDEIDE HLAKKVDENS DQDTPVTIKW GNRRFTMLVQ PALHTIYLME ITKYAKIDER
YQNEKVVIGN IYLDNYAEVT QGMNDSEESN LRNYVTSELN DWAHKYGVFM KVIDTDDYLI
LGHQQTLRQI EADKFSILDT IRENTSKQNA PVTLSVGVAY GDDDLNKLAD LAQSNLDLAL
GRGGDQVVVK ADGQQARFYG GKTNPMEKRT RVRARMISQA LQELMSESDQ IFVQGHRGPD
MDSLGACLGI RRIAKMNGRE CWIVLDDDHI HSDIKRLMHE IDGYQDIKDH IITIREAEEK
ATDQSLLIMV DHSKPSMSMS EQVFNRLQNR VMIIDHHRRG EEFPENPILV YIEPYASSTC
ELITEMLEYQ PRESESLNKL EATAMLTGIQ VDTKSFTSRA GTRTFDAASY LRSAGADGML
IQEFMKENVS SYLDRNHLIS LVQILDDKIA ICTGEDTQSY GSVTTAQAAD SLLQMEGIDA
SFVITRRSDD QVGISARSMG DYNVQVIMEK MGGGGHLSNA ATQISGKQVS EVEQELVAIL
HGDDESEKNE EE
//
