ID R5TY95_9FIRM Unreviewed; 681 AA.
AC R5TY95;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=BN683_01007 {ECO:0000313|EMBL:CCZ63926.1};
OS Roseburia sp. CAG:50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262949 {ECO:0000313|EMBL:CCZ63926.1, ECO:0000313|Proteomes:UP000018378};
RN [1] {ECO:0000313|EMBL:CCZ63926.1, ECO:0000313|Proteomes:UP000018378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:50 {ECO:0000313|Proteomes:UP000018378};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ63926.1}.
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DR EMBL; CBAK010000026; CCZ63926.1; -; Genomic_DNA.
DR AlphaFoldDB; R5TY95; -.
DR Proteomes; UP000018378; 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:UP000018378};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..520
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 553..668
FT /note="DHHA1"
FT /evidence="ECO:0000259|Pfam:PF02272"
SQ SEQUENCE 681 AA; 77501 MW; 0E5E2E9D54EF751D CRC64;
MRQDVKLKGK LKGYTQTPLV LTALFGAMDV WMYVLNIKAG VLGSVFVGIY FFVMLFVYWR
NKPILMNELI DFATQYGTVQ KRLLNEFEVP YAVMDATGKL LWMNRQFEAL SEKNKGYHKS
ITTIFPQITR ELMEKEDELE LVVEREECVY RASVHKIHFT DILHESSSIE LTEKVQYLQV
IYLFDETQLT RYRIENQEMQ MVPALVYIDN YDEVLDTVEE VKKSLLVALV DRKVTKFFAS
IDGLVKKTEN DKYFVVFQHK YLEKMEEEKF SLLEDVKSIK VGNEMSVTLS MGIGYVGNDY
TKNYEYSRMA IDLALGRGGD QVVVKTRDKI SYFGGSNRQV DKSTRVKARV KALALREIMI
TRDKFFVMGH KIADIDSFGA AIGIYCAARQ LGKKAQIVID EVNTTLRPLK ECFTPENGYP
DDMFIPSQLA LDEIDSHTAL IVVDTNRPSY TECPNLLNRA KAIVVFDHHR QCEDVVKNAV
LSYTEPYASS TCEMIAEVLQ YFDEDIKLST QEADAIYAGI LIDTNNFVSK TGVRTFEAAA
YLRRCGAEVT RVRKMLRNDM DAYKARAEAV RHAEVFHNMF AISVCPADNI ESPTVACAQA
ANELLNIIGI KASFVLTEYH DRIYISARSI DEINVQLVME RLGGGGHMNS AGAQLTGCTL
EDAKRTIENT LDEMIREGDI K
//
