ID UPPP_FLAPJ Reviewed; 261 AA. AC A6H239; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 76. 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}; OrderedLocusNames=FP2358; OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 / OS JIP02/86). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B., RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F., RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(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; AM398681; CAL44413.1; -; Genomic_DNA. DR RefSeq; WP_011964447.1; NC_009613.3. DR RefSeq; YP_001297214.1; NC_009613.3. DR AlphaFoldDB; A6H239; -. DR SMR; A6H239; -. DR STRING; 402612.FP2358; -. DR EnsemblBacteria; CAL44413; CAL44413; FP2358. DR GeneID; 66553466; -. DR KEGG; fps:FP2358; -. DR PATRIC; fig|402612.5.peg.2414; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_10; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000006394; 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 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; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..261 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000303027" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 41..61 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 69..89 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 95..115 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 129..149 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 169..186 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 241..261 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 261 AA; 28818 MW; 2502FC9E60E0FD64 CRC64; MNYIQAIILA IIEGITEFLP VSSTGHMIIA SSFFGIAHED FTKLFTIVIQ LGAILSVVVL YFKRFFQTLD FYFKLLVAFI PAVVLGLLFS KKIDALLESP VTVAVSLLVG GIILLKVDDW FNNSSETEIT YLKAFKIGLF QCIAMIPGVS RSGASIVGGM SQKLARTSAA EFSFFLAVPT MLGATLKKCY DYYKDGFILT HDQINILIIG NIVAFLVALL AIKTFIGFLS KNGFKVFGYY RIVAGIVLLL IHFFIHPLTL I //