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
//