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Database: UniProt
Entry: A0A261QMY0_9GAMM
LinkDB: A0A261QMY0_9GAMM
Original site: A0A261QMY0_9GAMM 
ID   A0A261QMY0_9GAMM        Unreviewed;       251 AA.
AC   A0A261QMY0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
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=CE195_10635 {ECO:0000313|EMBL:OZI14146.1};
OS   Sodalis-like symbiont of Philaenus spumarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=1189304 {ECO:0000313|EMBL:OZI14146.1, ECO:0000313|Proteomes:UP000216612};
RN   [1] {ECO:0000313|EMBL:OZI14146.1, ECO:0000313|Proteomes:UP000216612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=spu {ECO:0000313|Proteomes:UP000216612};
RA   Chouaia B.;
RT   "Metabolic interaction between xylem feeders and their symbionts.";
RL   Submitted (JUN-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:OZI14146.1}.
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DR   EMBL; NKXM01000597; OZI14146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261QMY0; -.
DR   Proteomes; UP000216612; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd01610; PAP2_like; 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:SF54; PHOSPHATIDYLGLYCEROPHOSPHATASE B; 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:UP000216612};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..227
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   251 AA;  28930 MW;  DCEFD6AA86A74DCE CRC64;
     MVEIAKRTGI SALLLMVLPL LLWASGWQWQ PENDYRWLKG WYWLTQTVTS PWGTLTSALL
     ISWFLWCLRY RLKPALGLVA ILTATLLIGQ GMKSFIKERA QEPRPYVLWL EKHYAIDDRA
     FYAMPRKARS AAVARELKEQ QVIPPWLQKH WRAATDFSFP SGHTIFAVSW ALLAVGLLWP
     RRYRFSTVVL MVWASGVMVS RMVLGMHWPR DVVVGVAVSW LVITLGCWLV QRWIGALTPM
     PEEAPDIRSR G
//
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