ID Q181R1_CLOD6 Unreviewed; 664 AA.
AC Q181R1;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 10-JUN-2026, entry version 107.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN OrderedLocusNames=CD630_36590 {ECO:0000313|EMBL:CAJ70567.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Peptostreptococcaceae; Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ70567.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ70567.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ70567.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2] {ECO:0000313|EMBL:CAJ70567.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ70567.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=21349987; DOI=10.1099/jmm.0.030452-0;
RA Monot M., Boursaux-Eude C., Thibonnier M., Vallenet D., Moszer I.,
RA Medigue C., Martin-Verstraete I., Dupuy B.;
RT "Reannotation of the genome sequence of Clostridium difficile strain 630.";
RL J. Med. Microbiol. 60:1193-1199(2011).
RN [3] {ECO:0000313|EMBL:CAJ70567.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ70567.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=24568651; DOI=10.1186/1471-2164-15-160;
RA Pettit L.J., Browne H.P., Yu L., Smits W.K., Fagan R.P., Barquist L.,
RA Martin M.J., Goulding D., Duncan S.H., Flint H.J., Dougan G.,
RA Choudhary J.S., Lawley T.D.;
RT "Functional genomics reveals that Clostridium difficile Spo0A coordinates
RT sporulation, virulence and metabolism.";
RL BMC Genomics 15:160-160(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 -!- 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}.
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DR EMBL; AM180355; CAJ70567.1; -; Genomic_DNA.
DR RefSeq; WP_003429268.1; NC_009089.1.
DR AlphaFoldDB; Q181R1; -.
DR STRING; 272563.CD630_36590; -.
DR EnsemblBacteria; CAJ70567; CAJ70567; CD630_36590.
DR GeneID; 66356130; -.
DR KEGG; cdf:CD630_36590; -.
DR KEGG; pdc:CDIF630_03987; -.
DR PATRIC; fig|272563.120.peg.3869; -.
DR eggNOG; COG3887; Bacteria.
DR OrthoDB; 9759476at2; -.
DR PhylomeDB; Q181R1; -.
DR BioCyc; PDIF272563:G12WB-3850-MONOMER; -.
DR Proteomes; UP000001978; 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 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:UP000001978};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..314
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT BINDING 357
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 363
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 430
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 430
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 454
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
FT BINDING 509
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR026583-50"
SQ SEQUENCE 664 AA; 75924 MW; 5746D31E164E3C90 CRC64;
MSNKQTFKLN MPEINLYIIV IGISSIILLY YNLYVGCLFF CIFVYMVFHN WRTTNIRRHE
WTEYIQNLSL DIDETTKKAI INLPIPLCIL EFDGNISWYN GKFYDMIGQK DLLDKNIEDI
VKNLNLRKVL NENKEMYTEI NYKEKEYTII YNVIKNDQEK NPKYLMILYW IDKTEYLKVK
QNYDDEKNAM MLIQVDGYDE VLKSAAEDKR ALINVEVEKI LSALELNSNG ALRRTSKDKF
FLVMHKKELK KLEAEKFSIL DTIRHIDYGN NLPVTISIGI GIDGDTLNEN LKLATGALDL
ALGRGGDQAV VKTKDKFVFY GGKSKAVEKK TKVKSRLIGH ALREVIQQSD QVYIMGHKYP
DMDAMGAAVG VYDICKSCNK TANIVLQSVN ESIEIFINKI NENNYYKKLF IGKEEAIDNC
TKNTLVVVVD THRPNYTECE ELLKLSEKVV VIDHHRRGVE FINDAVLLFH EIYVSSTCEM
VTELVQYMDE DVTINKLTAE GLLAGISLDT KNFAFKTGVR TFEAASYLRK VGADTIEVKK
FFNSDVKDFI IKAEIIQSTK IINNRICLAY SSTEIDSINV IIAQTADELL NIKEVEASFV
LGEKDDTIFI SARSLGQINV HVLMEKLGGG GHIDIAGAQL KNVSLKEAYK MVNKIIEEYL
EEEE
//
