ID C6Q0G1_9CLOT Unreviewed; 661 AA.
AC C6Q0G1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=CcarbDRAFT_4528 {ECO:0000313|EMBL:EET85030.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET85030.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET85030.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET85030.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) 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|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:EET85030.1}.
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DR EMBL; ACVI01000114; EET85030.1; -; Genomic_DNA.
DR RefSeq; WP_007063413.1; NZ_CP011803.1.
DR AlphaFoldDB; C6Q0G1; -.
DR STRING; 536227.Ccar_20615; -.
DR KEGG; cck:Ccar_20615; -.
DR PATRIC; fig|536227.13.peg.4289; -.
DR eggNOG; COG3887; Bacteria.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000004198; 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; IPR049553; GdpP-like_PAS.
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 Pfam; PF21370; GdpP_PAS; 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:UP000004198};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..150
FT /note="Cyclic-di-AMP phosphodiesterase GdpP-like PAS"
FT /evidence="ECO:0000259|Pfam:PF21370"
FT DOMAIN 350..504
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 526..652
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
SQ SEQUENCE 661 AA; 75127 MW; 36C9AEE115CC573C CRC64;
MDKKYNYFIT GNKVYMIIIA ILISVIIVYR HFYIGIVFIS LYIILVVYNM KNTKVRQTEW
KKFIENFSSQ LDNATRNTLV KMPFPLIMID KKGEILWYNQ KYSYIIKNED ILGKNINGVI
KEINLRQILD GKKNMMKNVK LKENYYDIYS NVVDISDNLE DRIILLYLYD VTQMLKIVKN
LELNKYTIML MEVDNFHDVI KTIEEGQRPL IVAEIERTIN CYAQSLNAMM RKYDDNKYVL
CVQDNYVEKE MEKKFEILDN IREINMGNKL AVTLSIGVGR GGETPLQNEN FAASAKELAL
GRGGDQTVVK NGEKLSFYGG KTKEVEKRTK VRARVIAHAL VELINASSDV FIMGHINPDI
DCLGAAVGIY STIKFLKKDC HIVLEETNSS INLILEKIKN EEDYEKVFIS SKECIDNMKY
NSLLILVDVH SRGYVQDIKV VDAFEKIVII DHHRKSTDFV EGALLSYIEP YASSTSELVT
EMLQYMVEKP KIKIIEAEAL LAGICVDTKN FCFKTGVRTF EAASFLRRLG ADTVDVKKFF
ADDLDTYLKR AEIIKSAEIF NNIAIAVCPN EIEDIVLAAQ AADELLNITG IKASFVFVKI
KDNVCISGRS LGEVNVQVIL ESLGGGGHMT MAGATIKKVT LDEALKKLKD AIGKYIMEGE
E
//
