ID UPPP_SINFN Reviewed; 268 AA. AC C3MCT9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 83. 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=NGR_c36660; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=19376903; DOI=10.1128/aem.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion RT systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). 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; CP001389; ACP27387.1; -; Genomic_DNA. DR RefSeq; WP_012710131.1; NC_012587.1. DR RefSeq; YP_002828140.1; NC_012587.1. DR AlphaFoldDB; C3MCT9; -. DR SMR; C3MCT9; -. DR STRING; 394.NGR_c36660; -. DR KEGG; rhi:NGR_c36660; -. DR PATRIC; fig|394.7.peg.6518; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_5; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000001054; 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..268 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_1000148823" FT TRANSMEM 5..25 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 84..104 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 106..126 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 184..204 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 248..268 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 268 AA; 28488 MW; F1E6EED402DB9D0D CRC64; MADQSIISAL VLGLIEGLTE FIPVSSTAHV LLAGHFLGFK SPGNTFAVLI QLGAILAILL VYFQKLLSIA LALPTSVKAR RFVFSVLIAF LPAALIGAAA HGFIKAVLFE TPMLICVVLI VGGVILYAID RLPLQPRYTD VFDYPPSLAL KIGLFQCLAM IPGTSRSGAT IAGALLMGTD KRSAAEFSFF LAMPTMLGAF TLDLYKNRDA LSFDDIGVIA IGFIAAFVAG IVVVRSLLDF VSHRGFTPFA IWRIVVGTAG LVGLWLVG //