UPPP2_BURPS
ID UPPP2_BURPS Reviewed; 276 AA.
AC Q63RM9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Undecaprenyl-diphosphatase 2 {ECO:0000255|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein 2 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 2 {ECO:0000255|HAMAP-Rule:MF_01006};
GN Name=uppP2 {ECO:0000255|HAMAP-Rule:MF_01006}; OrderedLocusNames=BPSL2643;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC (UPP). Confers resistance to bacitracin. {ECO:0000255|HAMAP-
CC Rule:MF_01006}.
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:0000255|HAMAP-Rule:MF_01006};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01006}.
CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition
CC of peptidoglycan synthesis by sequestering undecaprenyl diphosphate,
CC thereby reducing the pool of lipid carrier available.
CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000255|HAMAP-
CC Rule:MF_01006}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571965; CAH36651.1; -; Genomic_DNA.
DR RefSeq; WP_004185904.1; NZ_CP009538.1.
DR RefSeq; YP_109239.1; NC_006350.1.
DR AlphaFoldDB; Q63RM9; -.
DR SMR; Q63RM9; -.
DR STRING; 272560.BPSL2643; -.
DR EnsemblBacteria; CAH36651; CAH36651; BPSL2643.
DR GeneID; 56594830; -.
DR KEGG; bps:BPSL2643; -.
DR PATRIC; fig|272560.51.peg.2704; -.
DR eggNOG; COG1968; Bacteria.
DR OMA; IEGPFRD; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01006; Undec_diphosphatase; 1.
DR InterPro; IPR003824; UppP.
DR PANTHER; PTHR30622; PTHR30622; 1.
DR Pfam; PF02673; BacA; 1.
DR TIGRFAMs; TIGR00753; undec_PP_bacA; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..276
FT /note="Undecaprenyl-diphosphatase 2"
FT /id="PRO_0000151127"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 276 AA; 30284 MW; 608BFAFD49296177 CRC64;
MDWILICKAL ALGIVEGLTE FLPVSSTGHL IVAGSFLRFH PEQAKTFDVV IQFGAILAVC
WEYRRRIIDV VTGLPAQREA RRFTMNVVIA TVPAVALALL FEKTIKSVLF APVPVAVALV
VGGAAILWVE GRQRERSEPA RVQSIDALTP FDALKVGLAQ CCALIPGMSR SGSTIIGGML
FGLERRVATE FSFFLAIPVI FGATLYETAK DWRAFNVDSV GLFAIGLVAA FVSAFACVRW
LLRYVASHDF TAFAWYRIAF GLFVLLVGYS GWIEWT
