ID UPPP_LACCB Reviewed; 272 AA. AC B3WCK5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000255|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01006}; GN Name=uppP {ECO:0000255|HAMAP-Rule:MF_01006}; GN OrderedLocusNames=LCABL_10200; OS Lacticaseibacillus casei (strain BL23) (Lactobacillus casei). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lacticaseibacillus. OX NCBI_TaxID=543734; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL23; RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A., RA Deutscher J.; RT "Lactobacillus casei BL23 complete genome sequence."; RL Submitted (JUN-2008) 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 membrane {ECO:0000255|HAMAP-Rule:MF_01006}; CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; FM177140; CAQ66106.1; -; Genomic_DNA. DR AlphaFoldDB; B3WCK5; -. DR SMR; B3WCK5; -. DR KEGG; lcb:LCABL_10200; -. DR HOGENOM; CLU_060296_2_0_9; -. 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 membrane; Cell shape; KW Cell wall biogenesis/degradation; Hydrolase; Membrane; KW Peptidoglycan synthesis; Transmembrane; Transmembrane helix. FT CHAIN 1..272 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_1000197377" FT TRANSMEM 2..22 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 110..130 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 185..205 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 224..244 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 272 AA; 30045 MW; CEB5E09DD91BEAF0 CRC64; MFDIIKAVII GIVEGLTEFL PISSTGHIDL VNHVIKLSQS QDFISMFEYV IQFGAILAVV LLYFNKLNPF SKPTAKARNA TWQLWAKVII AVLPSAVVGL PLNSWMDEHL HTPIVVATTL IVYGILFIIL ENYLKNKSAH ITTLADITYQ TALLIGLFQV LSIVPGTSRS GATILGALLI GTSRYVATEF SFFLAIPTMV GVLIIKIGKY LWQGNGFSGE QWAVLMTGSI VSFLVAIVAI KWLLKFVQTH DFKPFGWYRI ALGAIVLLVM FI //