ID A0A0J1FZA6_9FIRM Unreviewed; 689 AA.
AC A0A0J1FZA6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=RHS_5479 {ECO:0000313|EMBL:KLU68694.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU68694.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU68694.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU68694.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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|PIRNR:PIRNR026583}.
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:KLU68694.1}.
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DR EMBL; JNGB01000142; KLU68694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FZA6; -.
DR PATRIC; fig|1504536.3.peg.1390; -.
DR Proteomes; UP000036477; 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; IPR014528; GdpP/PdeA.
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 PIRSF; PIRSF026583; YybT; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR026583};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR026583};
KW Membrane {ECO:0000256|PIRNR:PIRNR026583, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 374..529
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 562..680
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
SQ SEQUENCE 689 AA; 77446 MW; FB45D50CFC3470C2 CRC64;
MGVQSMKKIN RKIKYSGRLK SYMQWPLALV VFLLLMNIAV FAVDTKAGIA AALFSVVYIV
LIIGVFVLYK PRIMTELVSF ATQYGQIQKK MLQKFAIPYG LLDTEGKIIW MNEAFCNAVG
KDPKYHKNIL NLFPEISVNV LPKNEDIQTI EVHFDGEDYR AQLQRVSIEE LADSVNIVEV
PEDQNYLIAV YLFDTTELNQ YIRENKEQKL VAGLIYIDNY DEALESVEEV RRSLLMALID
RKINKYITSL DGIVKKIEKD KYFIAIRQRS LTTLESNRFS LLEEVKSVNI GNDMSVTLSI
GIGVNGNGYV QNYDFSRIAI ELALGRGGDQ AVVKDNEKIS YYGGKSQQME KSTRVKARVK
AHALREFIDS KEDVVVMGHK ITDIDSFGAS IGVYRAARLM NKKAHIVIED VNSSIRPWMN
MFLNNKDYES DMFVNHAQAE EIVDNNTVVV VVDTNRPSMA ECSSILEQTK TIVVLDHHRQ
SSEVIKNAVL SYIEPYASST CEMVAEILQY FVDGIKLKNI EADCIYAGII IDTNNFVAKT
GVRTFEAAAF LRRCGADVTR VRKMLRNDMS AYKARAEAVR HAELFLNCYA FSICPSENIE
SPTVVGAQAA NELLNIIGVK ASFVFTPFNK QVYISARSID EVNVQIITER MGGGGHLNIA
GAQLKDTTVE EAISKLKDVI IKMTEEGAI
//
