ID UPPP_PARD8 Reviewed; 266 AA. AC A6LEL8; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 81. 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=BDI_2407; OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM OS 5825 / NCTC 11152). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; OC Parabacteroides. OX NCBI_TaxID=435591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., RA Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). 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; CP000140; ABR44132.1; -; Genomic_DNA. DR RefSeq; WP_008779927.1; NZ_LR215978.1. DR AlphaFoldDB; A6LEL8; -. DR SMR; A6LEL8; -. DR STRING; 435591.BDI_2407; -. DR PaxDb; 435591-BDI_2407; -. DR KEGG; pdi:BDI_2407; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_1_2_10; -. DR BioCyc; PDIS435591:G1G5A-2474-MONOMER; -. DR Proteomes; UP000000566; Chromosome. 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; UNDECAPRENYL-DIPHOSPHATASE; 1. DR PANTHER; PTHR30622:SF2; 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; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..266 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000303032" FT TRANSMEM 41..61 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 80..100 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 180..200 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 245..265 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 266 AA; 28577 MW; 25771B7C03967631 CRC64; MSWFEALILG IVQGLTEYLP VSSSGHLAIG SALFGIEGEE NLAFTIVVHV ATVFSTLVVL WKEIDWIFRG LFKFQMNAET KYVINILISM IPIGIVGVFF KDTVEQIFGS GLLVVGCMLL LTAALLAFSY YAKPRQKESI SMKDAFIIGL AQACAVMPGL SRSGSTIATG LLLGNNKAKL AQFSFLMVIP PILGEALLDV MKMVKGEDVA GDIPALSLAV GFMAAFVSGC VACKWMINIV KKGKLIYFAI YCAIAGLVTI ACTLLK //