ID A0A089LXC0_9BACL Unreviewed; 666 AA.
AC A0A089LXC0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=PSTEL_26775 {ECO:0000313|EMBL:AIQ66181.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ66181.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ66181.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ66181.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009286; AIQ66181.1; -; Genomic_DNA.
DR RefSeq; WP_038699807.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LXC0; -.
DR STRING; 169760.PSTEL_26775; -.
DR KEGG; pste:PSTEL_26775; -.
DR HOGENOM; CLU_018278_0_0_9; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000029507; 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 Reference proteome {ECO:0000313|Proteomes:UP000029507};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..313
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 666 AA; 74603 MW; 155D05E20D6AAF7F CRC64;
MPKFLQRRWH GYHTVWAFLL LLVLVIAVSI YNWVLGVVCL FLAGTLCITM LKTELSFRRN
LVEYINSLTF RIKRVEGEAV STLPLGIILY GEDRNVEWSN RYAGEIFARK SLVGDLLPDL
LPDLGPVMVP PVKREVGKDG VQKDIRLEIG VDQRYYQAVL VPSERLLYLF EITDLVDLRQ
RYEEEKLALG ILLMDNLDEA AQGMDDQQRT SLIAKVTSEI TDWARQFDVY LRRLSSERYL
MLLNHRSLQA LEESRFVILD EVREMTADLK VPMTLSIGLA FGAESASELG ALAQSSLDMA
LGRGGDQAAV KAGQRLSFYG GKTNAAEKRT RVRARVIAHA LRDLMQESDR VIIMGHRNPD
IDAVGASIGL LRAAQMYNVE ADIVLDGPNP SITRMLEQLK RDEELYSSFI STEQALQVMT
EHTLLIVVDT HKASMTMEPR LVQYASRIVV VDHHRRGEEF INEAVLVYLE PYASSTCELV
TELLQYIHEK VKLSTLEATM LLAGITVDTK HFALHTGSRT FEAAGFLRRL GADTVLIQRM
LKEDLQEYIS KAEIIKHARM VYDHIALVVT EAGMKIPQLL IAQTADTLLG MTNVLASFVI
SERTDGLIGI SARSLGRMNV QVVMEKLGGG GHLTNAAAQL EGTCKDAEAR LLEVLAEIES
KEGLFE
//