ID UPPP1_BURCM Reviewed; 276 AA. AC Q0BHM0; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Undecaprenyl-diphosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein 1 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006}; GN Name=uppP1 {ECO:0000255|HAMAP-Rule:MF_01006}; GN OrderedLocusNames=Bamb_0794; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia OS (strain AMMD)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-244 / AMMD; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., RA Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000440; ABI86353.1; -; Genomic_DNA. DR RefSeq; WP_011656167.1; NZ_CP009798.1. DR AlphaFoldDB; Q0BHM0; -. DR SMR; Q0BHM0; -. DR GeneID; 69545060; -. DR KEGG; bam:Bamb_0794; -. DR PATRIC; fig|339670.21.peg.796; -. DR eggNOG; COG1968; Bacteria. DR Proteomes; UP000000662; Chromosome 1. 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 NCBIfam; TIGR00753; undec_PP_bacA; 1. DR PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1. DR PANTHER; PTHR30622:SF3; UNDECAPRENYL-DIPHOSPHATASE; 1. DR Pfam; PF02673; 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; Transmembrane; Transmembrane helix. FT CHAIN 1..276 FT /note="Undecaprenyl-diphosphatase 1" FT /id="PRO_0000290693" FT TRANSMEM 4..24 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 45..62 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 83..103 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 252..272 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 276 AA; 30303 MW; FAE8690EC2AD0CD9 CRC64; MDWILICKAL ILGVVEGLTE FLPVSSTGHL IVAGSFLNFN DAHAKTFDVV IQFGAILAVC WEYRQRIVSI VTGLPSRPDA QRFTLNVVIA TIPAIALGLL FEKKIKAVLF SPVPVAFALV VGGAIILWAE ARQRERREPP RVQSIDALTP LDALKVGLAQ CFALVPGMSR SGSTIIGGML FGLDRRVATE FSFFLAIPII FGATLYETVK DWQAFTVDSL GLFALGLVAA FVSAFVCVRW LLRFVATHDF TVFAWYRIAF GLFVLLVGYS GWLNWA //