ID C2ENV5_9LACO Unreviewed; 673 AA.
AC C2ENV5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cyclic-di-AMP phosphodiesterase {ECO:0000256|PIRNR:PIRNR026583};
DE EC=3.1.4.- {ECO:0000256|PIRNR:PIRNR026583};
GN ORFNames=HMPREF0548_1351 {ECO:0000313|EMBL:EEJ71738.1};
OS Lactobacillus ultunensis DSM 16047.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ71738.1, ECO:0000313|Proteomes:UP000005583};
RN [1] {ECO:0000313|EMBL:EEJ71738.1, ECO:0000313|Proteomes:UP000005583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ71738.1,
RC ECO:0000313|Proteomes:UP000005583};
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 (JAN-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:EEJ71738.1}.
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DR EMBL; ACGU01000064; EEJ71738.1; -; Genomic_DNA.
DR RefSeq; WP_007125848.1; NZ_GG693254.1.
DR AlphaFoldDB; C2ENV5; -.
DR STRING; 525365.HMPREF0548_1351; -.
DR PATRIC; fig|525365.8.peg.2059; -.
DR eggNOG; COG3887; Bacteria.
DR HOGENOM; CLU_018278_0_0_9; -.
DR OrthoDB; 9759476at2; -.
DR Proteomes; UP000005583; 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 InterPro; IPR000160; GGDEF_dom.
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.
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 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 673 AA; 75429 MW; A01DF5E60373B280 CRC64;
MKDFLRKLEL PEFIKDSRLT ASVVIILSLS LIGSVIAMIM NPLFGLAMVL VFILTVAFAV
YGTYILAGNA TNFAVNLSYR IKRSEQEAMI KMPLGILLYD SDHQIQWVNP YLQLYLKDTD
LVGHTIEAVD PDLNKLLNEA IEAKTSENHL VDWDGHRFEM VVQDNLGVIY LLDITRYAKI
EDKYKAERLA IGQIFIDNYD ELSETMHDQE LTSMSSYVQN TLSDYAKKFK AYLKRIDEDH
FLLLVHMQDL AEMEKDKFSV LDKVRQETSR NNTPLTLSMG IAFGSDSLSE IANQAQSNLD
LALGRGGDQV VLRQPGKDAR FYGGKSNPME KRTRVRARMV SQAISELFKD ADRVFVVGHQ
RPDMDSVGSG IGVVKIARLH GVKANFVLDT NKTNYDVGRL VTRMQQKNQD KDIFISPDVA
LAEVTDKSML VMVDHSKYSI TYSQPLYDRL KNRIIVIDHH RRGEEFPENP MLTYVEPYAS
SACELVTEMI EYQQPANGKR VLTDLEATAM LAGIVVDSKE FSLRTGTRTF DAASYLRSIG
ADSAVVSMLL KEDIDSFLER THLVATLKMV KPHMAVLCGP DDQIIDPIIT AQAADTALDL
ENVGASFAIT RRSQNTIGIS ARSMGKINVQ IIMEKLGGGG HLSNAATQIK DVTIEEARAK
LLKAIDEYEE END
//
