ID R8AMS6_PLESH Unreviewed; 174 AA.
AC R8AMS6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PLESHI_15448 {ECO:0000313|EMBL:EON87649.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON87649.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON87649.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON87649.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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:EON87649.1}.
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DR EMBL; AQQO01000359; EON87649.1; -; Genomic_DNA.
DR RefSeq; WP_010864685.1; NZ_KB944511.1.
DR AlphaFoldDB; R8AMS6; -.
DR STRING; 703.SAMEA2665130_02652; -.
DR PATRIC; fig|1315976.3.peg.2953; -.
DR HOGENOM; CLU_072573_10_2_6; -.
DR OrthoDB; 9780507at2; -.
DR Proteomes; UP000014012; 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; 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:UP000014012};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 61..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..171
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 174 AA; 19518 MW; 98F723B28519FB5F CRC64;
MALSRLSPRW RLQQLDLALS TFCLCHRFNH QVARVCRLVS RTGDGPWYLL LALVLLRWEP
VHGTAFFTAL LLAFAIELPL YWLLKNAIRR HRPLDLPCFI VPSDKYSLPS GHTAAAFLVC
GLIAAYYPLW LLPALCWAAL IGLSRVLLGV HYLTDIVAGA LLGLSCAKLA LEWL
//