ID   G2FBJ9_9GAMM            Unreviewed;       184 AA.
AC   G2FBJ9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=TevJSym_ab00320 {ECO:0000313|EMBL:EGW55680.1};
OS   endosymbiont of Tevnia jerichonana (vent Tica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55680.1, ECO:0000313|Proteomes:UP000005167};
RN   [1] {ECO:0000313|EMBL:EGW55680.1, ECO:0000313|Proteomes:UP000005167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGW55680.1}.
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DR   EMBL; AFZB01000002; EGW55680.1; -; Genomic_DNA.
DR   RefSeq; WP_006473718.1; NZ_AFZB01000002.1.
DR   AlphaFoldDB; G2FBJ9; -.
DR   eggNOG; COG0671; Bacteria.
DR   Proteomes; UP000005167; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        131..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..172
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   184 AA;  20438 MW;  7969B5507ED2C8F7 CRC64;
     MSPDQSLIIW INQGWASPFL DWLLSWVSDK YSFSFPLLLL LLWTAVSREL SAGLRWWLAL
     ILMVALGDAL GAQLKDLFAQ ARPCFSFFEP LRLIEGGQCG ASLKGMPSNH ALNSFAATAF
     LFVTRPAWKG WRLFLLVSAI LVALSRIYLA KHFPSQVVMG AAIGTLWGLA AACLYDRIRC
     RGSD
//