GenomeNet

Database: UniProt
Entry: R5AIB9_9FIRM
LinkDB: R5AIB9_9FIRM
Original site: R5AIB9_9FIRM 
ID   R5AIB9_9FIRM            Unreviewed;       669 AA.
AC   R5AIB9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   ORFNames=BN453_00079 {ECO:0000313|EMBL:CCX39116.1};
OS   Firmicutes bacterium CAG:102.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262998 {ECO:0000313|EMBL:CCX39116.1, ECO:0000313|Proteomes:UP000018112};
RN   [1] {ECO:0000313|EMBL:CCX39116.1, ECO:0000313|Proteomes:UP000018112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:102 {ECO:0000313|EMBL:CCX39116.1,
RC   ECO:0000313|Proteomes:UP000018112};
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|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:CCX39116.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAWG010000008; CCX39116.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5AIB9; -.
DR   STRING; 1262998.BN453_00079; -.
DR   Proteomes; UP000018112; 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; 3.30.70.270; -; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 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   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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:UP000018112};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          189..317
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   669 AA;  73647 MW;  1755447CD8DB237D CRC64;
     MDDMSENAKS EQYQEKTGRE SNPIGVAAVI LLLCICFLID ARVGFGALIG AAAGFFAWSL
     LKDNGTRKEE NADDRVAFLD TTVLQHNFPL PQNMPIPYAV LDIRGHILMY NEKFAKEFPN
     MELILPVVDQ LKKAGIGKHA VVVVEEKHYD AMLNQCEVVE ENGAVGNVLN MTLVDISKQY
     ELEERLDRNE TVIGMLFLDN YEDVMDSLAE DRQPLLSAIV DRKLTQFAAD ANGVMRKLQM
     DRYILLLSKG DLEALKEKKF DIMNTIREIN VGEHIPVTMS MGVGIGGGSL EDAMQSAKAA
     LDLALGRGGD QVLIKEGEKY LFYGAKAGEV GRNGRIRARV KADALWELMG ASSSIMVMGH
     RNGDLDSLGS SMGICAIARA MGKKCRIVMN EVSTGIKCIS EQMTQDEYYQ TAFMKEKDAL
     KEMDDKTLVI VVDTHRTSMV EGPSVLEAAK KIVVFDHHRK SAQDFIEQAV LLYHEPYASS
     TSELITEMIQ HIGKKIKLRS IEADALLAGI TVDTKNFAVK TGAITFESAG FLRRNGADSI
     RVRMLFQNDI DSYKAKATAV RDAELYLGSM ALSVCPANRE NSTLTAAQAA DDLMNVTGVK
     ASFVCCKVDD VVYVSARSFG DVNVQRIMEK LGGGGHFTVS GAQLKDCSAE EAKERVRSAI
     DEYLKEETT
//
DBGET integrated database retrieval system