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Database: UniProt
Entry: R9M4K8_9FIRM
LinkDB: R9M4K8_9FIRM
Original site: R9M4K8_9FIRM 
ID   R9M4K8_9FIRM            Unreviewed;       664 AA.
AC   R9M4K8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   ORFNames=C816_01759 {ECO:0000313|EMBL:EOS65905.1};
OS   Oscillibacter sp. 1-3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillibacter.
OX   NCBI_TaxID=1235797 {ECO:0000313|EMBL:EOS65905.1, ECO:0000313|Proteomes:UP000014108};
RN   [1] {ECO:0000313|EMBL:EOS65905.1, ECO:0000313|Proteomes:UP000014108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-3 {ECO:0000313|EMBL:EOS65905.1,
RC   ECO:0000313|Proteomes:UP000014108};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Oscillibacter bacterium 1-3.";
RL   Submitted (APR-2013) 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:EOS65905.1}.
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DR   EMBL; ASTC01000013; EOS65905.1; -; Genomic_DNA.
DR   RefSeq; WP_016322063.1; NZ_KE159707.1.
DR   AlphaFoldDB; R9M4K8; -.
DR   STRING; 1235797.C816_01759; -.
DR   PATRIC; fig|1235797.3.peg.1917; -.
DR   eggNOG; COG3887; Bacteria.
DR   HOGENOM; CLU_018278_0_0_9; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000014108; 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   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   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:UP000014108};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          189..317
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   664 AA;  72995 MW;  AD9E6C28D8F1BFE5 CRC64;
     MNNKKLSRML EPNLKLYFLC MALFCLLALA VNPLLALAEA CVTAALYAYF SQANKKRRQG
     ILQYIDSVTG SVDTASKSTL IHSPLPIMVF RPDTGEVIWS NEDFLQLAGV REHLFEMRVE
     DAVPNCPVQW LLEGKQECPE RVAMNGRRFR VYGSLVRAKS RSGEQNLVAT TYWVDVTESD
     ALREAYTATR PVLALLMVDN YEDLMKACAD TQRSGILAQI DEKLDQWAAG SDGILLKTER
     DRYLFLFEER HYDHFVEEKF SVLDTIRDIK AAEGVPPTLS IGIGKDGATL SELLKNANLS
     LEMALSRGGD QAVVRGKVDF AFYGGRAKAT EKRTKVKSRV MANALSELMA DAGQIYVMGH
     SYADMDAVGA AVGICCAARK RGKQAQIVMD LEHNASEALL ERVRSMPEYA DTFISGGEAF
     LKMQPGALLV VVDTNRPELV DSPQVLDACN RVAVIDHHRR AATYIENAAF SFHEPYASSA
     SELVTELLQY LIEPADLMRG EAEALLAGIV LDTKHFTLRT GGRTFEAAAF LRRAGADTAD
     VQRLFQNDLN DMVSRYDIVR RAELYRGDIA VSVVPQEGVD RVAAAQAADE LLTLKGVKAS
     FVLYRNGENV LMSARSLGEV NVQVVLEALG GGGNSTTAGG CVENGDILDV RTRLVAAIDA
     YFEK
//
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