ID UPPP_ALKOO Reviewed; 279 AA. AC A8MFV5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 80. 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=Clos_0946; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OS OhILAs)). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=350688; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.; RT "Complete genome of Alkaliphilus oremlandii OhILAs."; RL Submitted (OCT-2007) 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; CP000853; ABW18493.1; -; Genomic_DNA. DR RefSeq; WP_012158805.1; NC_009922.1. DR AlphaFoldDB; A8MFV5; -. DR SMR; A8MFV5; -. DR STRING; 350688.Clos_0946; -. DR KEGG; aoe:Clos_0946; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_9; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000000269; 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 membrane; Cell shape; KW Cell wall biogenesis/degradation; Hydrolase; Membrane; KW Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..279 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_1000062785" FT TRANSMEM 3..23 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 188..208 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 220..240 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 279 AA; 31372 MW; 6FEB7A7909EA2AAD CRC64; MSIIELLKVI FLGIVEGITE WLPISSTGHM ILVEEFIQLN ASAAFKEMFF VVVQLGAIMA VVLLYFNKLN PFALSKTKRE KRETMRIWYK VVVGIIPAGV MGLLFDDWLN EHLYNYWTVA AMLIVYGVLF IIIENRNKHR YAKINSFSEL SYSTAFLIGL FQVLSLIPGT SRSGATIIGA IILGTSRYIA AEYSFFMSIP IMFGASAVKL LKFGFNFTSI EIITLVTGMV VAFVVSIIAI RLLMAYIKNN DFKAFGWYRI FLGVVVIGYF LITNGKVLS //