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Database: UniProt
Entry: A0A1B8QA40_9GAMM
LinkDB: A0A1B8QA40_9GAMM
Original site: A0A1B8QA40_9GAMM 
ID   A0A1B8QA40_9GAMM        Unreviewed;       196 AA.
AC   A0A1B8QA40;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=A9306_01250 {ECO:0000313|EMBL:OBX75980.1};
OS   Moraxella atlantae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=34059 {ECO:0000313|EMBL:OBX75980.1, ECO:0000313|Proteomes:UP000092616};
RN   [1] {ECO:0000313|EMBL:OBX75980.1, ECO:0000313|Proteomes:UP000092616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 59586 {ECO:0000313|EMBL:OBX75980.1,
RC   ECO:0000313|Proteomes:UP000092616};
RA   Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome of Moraxella atlantae CCUG 59586.";
RL   Submitted (JUN-2016) 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:OBX75980.1}.
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DR   EMBL; LZNA01000067; OBX75980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8QA40; -.
DR   Proteomes; UP000092616; 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:SF60; UNDECAPRENYL-DIPHOSPHATASE YBJG-RELATED; 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:UP000092616};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..190
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   196 AA;  22251 MW;  5F9E76D52DB3F743 CRC64;
     MQQFYDYLER KPRLHHLHQR LLKWDARLTI RANRWSHREL IGQFFKVISR LGDGWFWAAA
     VITMIGVLAV QGRAPLSITL ATLVILLTSY SGYRLYRFLK RHTVRPRPYQ VHQVIVLKER
     PLDVFSFPSG HTLQAVLFTL LIGSQTPVLL WVVAPFTALV ALSRLVLGLH YPTDVLVGAG
     IGASFAMAAQ LVLTLV
//
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