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Database: UniProt
Entry: A0A2D8RH30_9GAMM
LinkDB: A0A2D8RH30_9GAMM
Original site: A0A2D8RH30_9GAMM 
ID   A0A2D8RH30_9GAMM        Unreviewed;       233 AA.
AC   A0A2D8RH30;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=undecaprenyl-diphosphate phosphatase {ECO:0000256|ARBA:ARBA00012374};
DE            EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707};
GN   ORFNames=CME36_18295 {ECO:0000313|EMBL:MAM89254.1};
OS   Hahellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae.
OX   NCBI_TaxID=2048971 {ECO:0000313|EMBL:MAM89254.1, ECO:0000313|Proteomes:UP000225829};
RN   [1] {ECO:0000313|Proteomes:UP000225829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC         trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00000759};
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:MAM89254.1}.
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DR   EMBL; NZNF01000041; MAM89254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D8RH30; -.
DR   Proteomes; UP000225829; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd03392; PAP2_like_2; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR14969:SF13; AT30094P; 1.
DR   PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        60..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..202
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   233 AA;  25367 MW;  DB839DE2B4C05343 CRC64;
     MLLTMFVLAG LAWIFIWVTG EVVGGDSHAL DEQLLMSMRS AADPSDPLGP HWVEELMRDI
     TGLGGVGVLT FLTLVVVGFL ILQNKGKVAL VVVVTIGSGI ALSLLMKMGF DRPRPELVPH
     ESYVYTTSFP SGHSMMSAVV YLSLASLLAR VQQNRRVKIY LVAVAMVLTM MIGVSRVYMG
     VHWPTDVLAG WMAGAFWALL CYMVTRHLQH SGAVEPEGLD VDPDAAKTPL TVR
//
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