ID UPPP_YERE8 Reviewed; 272 AA. AC A1JQW4; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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}; Synonyms=bacA; GN OrderedLocusNames=YE3678; OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / OS 8081). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=393305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 13174 / 8081; RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206; RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J., RA Prentice M.B.; RT "The complete genome sequence and comparative genome analysis of the high RT pathogenicity Yersinia enterocolitica strain 8081."; RL PLoS Genet. 2:2039-2051(2006). 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; AM286415; CAL13705.1; -; Genomic_DNA. DR RefSeq; WP_005174137.1; NC_008800.1. DR RefSeq; YP_001007833.1; NC_008800.1. DR AlphaFoldDB; A1JQW4; -. DR SMR; A1JQW4; -. DR KEGG; yen:YE3678; -. DR PATRIC; fig|393305.7.peg.3916; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_6; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000000642; 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; Transmembrane; Transmembrane helix. FT CHAIN 1..272 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000290780" FT TRANSMEM 5..25 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 45..65 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 88..108 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 115..135 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 152..171 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 251..271 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 272 AA; 29552 MW; 02767B7D315BBBE9 CRC64; MTDMYSLFVA FVLGVVEGLT EFLPVSSTGH MIIVGELLGF TGDKAKTFEV IIQLGSILAV VVVFWRRLFG LIGIHFGKVP HEGKTNGHLT LGHILLAMIP AVGLGLAFHD VIKSLFNPQS VMYALVAGGL LLLAAEWFKP KNPKATGLDD ITYRQAFAIG CFQCLALWPG FSRSGATISG GMLVGVNRYA ASEFSFILAV PMMLGASGLD LYKSLHFLSW GDLPMFAVGF ITAFVVALIA IKTFLSLIKR ISFVPFAIYR FIVAAAVYWV FM //