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Database: UniProt
Entry: C8PB08_9LACO
LinkDB: C8PB08_9LACO
Original site: C8PB08_9LACO 
ID   C8PB08_9LACO            Unreviewed;       671 AA.
AC   C8PB08;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE            EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN   ORFNames=HMPREF0520_0278 {ECO:0000313|EMBL:EEW51957.1};
OS   Lactobacillus iners DSM 13335.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=525328 {ECO:0000313|EMBL:EEW51957.1, ECO:0000313|Proteomes:UP000004115};
RN   [1] {ECO:0000313|EMBL:EEW51957.1, ECO:0000313|Proteomes:UP000004115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13335 {ECO:0000313|EMBL:EEW51957.1,
RC   ECO:0000313|Proteomes:UP000004115};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (SEP-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|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. 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:EEW51957.1}.
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DR   EMBL; ACLN01000004; EEW51957.1; -; Genomic_DNA.
DR   RefSeq; WP_006729285.1; NZ_GG700805.1.
DR   AlphaFoldDB; C8PB08; -.
DR   GeneID; 69785655; -.
DR   PATRIC; fig|525328.13.peg.348; -.
DR   HOGENOM; CLU_018278_0_0_9; -.
DR   OrthoDB; 9759476at2; -.
DR   Proteomes; UP000004115; 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   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; IPR029787; Nucleotide_cyclase.
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   Pfam; PF21370; GdpP_PAS; 1.
DR   PIRSF; PIRSF026583; YybT; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 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:UP000004115};
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..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          187..315
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   671 AA;  75116 MW;  979DB78B8108F0EE CRC64;
     MKDFLRKLEL PAFVKDSRLT ASLIIVLSLS FVGFIVGLLI SPLYGLAMLL LFILTCTFSI
     YGIYVLAINT NNYASNLSYR IKRGEQEAMI KMPLGILLYD EDQQIQWVNP YLQLFLKNND
     MIGTSLKNLD EQLYKSINDA IRDKDTNNRV IRVGKHKCEI VVQNDLGVVY ILDITKYAAI
     ERRYQDQRLS IGLIFIDNYD ELSQAMGDQN LTDMSSYIQN ALNEYAKRFN AYLKRIDEDH
     YLLLSHMIDL HKMEADRFSI LDKVRKESSR CNTPLTLSVG IAFGSESLND ISEQAQSNLD
     LALGRGGDQV VVRQIGKDAH FYGGKSNPME KRTRVRARVV SQALQELFKD ADHVFVQGHK
     SPDLDAIGSA IGIVKIARIH GVKANVILDL SELNYDVERL IKKMQEAGVD QETFISPDEA
     VQIATDNSLL VLTDHSKYSI TYNQSIYDKM KNRLVVIDHH RRGEEFPENP MLVYIEPYAS
     STCELVTEMI EYQPQGGDGV LNYLEATAML AGITVDSKEF SLRTGTRTFD AASYLRSIGA
     DSQVVSYLLK ESIDNYLKRS YLVSTVDMVH SNMAILSGND SEIYDAIIIA QAADTALSLE
     GVSASFAIAR RSNSMIGISA RSTGKINVQV IMEKLGGGGH LSNAATQLDN ISVSEAKERL
     LQAIDSYLQE N
//
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