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Database: UniProt
Entry: G7GI07_9GAMM
LinkDB: G7GI07_9GAMM
Original site: G7GI07_9GAMM 
ID   G7GI07_9GAMM            Unreviewed;       184 AA.
AC   G7GI07;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=ACT4_054_00040 {ECO:0000313|EMBL:GAB03232.1};
OS   Acinetobacter sp. NBRC 100985.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1071390 {ECO:0000313|EMBL:GAB03232.1, ECO:0000313|Proteomes:UP000012044};
RN   [1] {ECO:0000313|EMBL:GAB03232.1, ECO:0000313|Proteomes:UP000012044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100985 {ECO:0000313|EMBL:GAB03232.1,
RC   ECO:0000313|Proteomes:UP000012044};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Acinetobacter sp. NBRC 100985.";
RL   Submitted (NOV-2011) 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:GAB03232.1}.
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DR   EMBL; BAEB01000054; GAB03232.1; -; Genomic_DNA.
DR   RefSeq; WP_007483912.1; NZ_BAEB01000054.1.
DR   AlphaFoldDB; G7GI07; -.
DR   Proteomes; UP000012044; 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; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR14969:SF61; UNDECAPRENYL-DIPHOSPHATASE BCRC; 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        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..166
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   184 AA;  20758 MW;  23730B1C4F7BCBA6 CRC64;
     MSFEDLNIYL FHSVNSFATH SLAFDKVMIF LANDLNTVFI SFLVFLLVIQ WKTYRLLFAK
     TLFIVLLSIA FSDLIEMFYH HPRPFQLDLG HKLIGHGLSS SFPSQHTLTI AVIAFTYLMA
     GYRAIGIVGL LVGVIVGLAR VYVGVHFPFD VIGSFVIGFL LVVSTNYVIK GLLLRRRKIN
     LAVE
//
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