ID G5S2B8_SALET Unreviewed; 423 AA.
AC G5S2B8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LTSEURB_5438 {ECO:0000313|EMBL:EHC98617.1};
OS Salmonella enterica subsp. enterica serovar Urbana str. R8-2977.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913084 {ECO:0000313|EMBL:EHC98617.1, ECO:0000313|Proteomes:UP000004776};
RN [1] {ECO:0000313|EMBL:EHC98617.1, ECO:0000313|Proteomes:UP000004776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-2977 {ECO:0000313|EMBL:EHC98617.1,
RC ECO:0000313|Proteomes:UP000004776};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC98617.1}.
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DR EMBL; AFCW01002014; EHC98617.1; -; Genomic_DNA.
DR AlphaFoldDB; G5S2B8; -.
DR PATRIC; fig|913084.3.peg.4014; -.
DR Proteomes; UP000004776; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR CDD; cd03397; PAP2_acid_phosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR001011; Acid_Pase_classA_bac.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..423
FT /note="undecaprenyl-diphosphate phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003483847"
FT DOMAIN 173..292
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 423 AA; 46440 MW; D32E65BF3669CEBB CRC64;
MKLHITVLAS SLALAMPALA KDIPLSQAES IAKSVTPDSA SVAFNDLEAQ WLTQLRKALQ
GDTAALTRDA LAQMRQNSIQ ADNAWLQASG YDFHTTENQQ MGITLLSAFN TLPEAVLKDN
LATVTAINHD ADVNTRHQAL ADAESVEYLY FLSDAMGPRL GRAFLAAYDK GELGKAAALI
KASEVSTGAA KKYFHYPRPY QVPGNTIHLT PDDVVVKDGH PYTAGGGAFP SGHTNTGYTD
ALLMAEMIPE RFDALVIRGA RYGYSRLVLG VHYPLDVMGA RMVAQRNVAH YLNDPYYRTL
FNEARAQLRE ALVKECGTTI VECAASAGKD DPYRDPAMHT FYRFTMTYNL PQQKGEHQPL
KIPKGADVLL QTALPNLSPA QRQALMEETA LPAGYPLSGE TEDQQFWQRL DLSAAYEMAR
KTR
//
