ID UPPP_DESAH Reviewed; 276 AA. AC C0QC99; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 68. 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=HRM2_40590; OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 / OS HRM2) (Desulfobacterium autotrophicum). OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulforapulum. OX NCBI_TaxID=177437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2; RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x; RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., RA Meyerdierks A., Gottschalk G., Amann R.; RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate RT reducer oxidizing organic carbon completely to carbon dioxide."; RL Environ. Microbiol. 11:1038-1055(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; CP001087; ACN17116.1; -; Genomic_DNA. DR RefSeq; WP_015905849.1; NC_012108.1. DR AlphaFoldDB; C0QC99; -. DR SMR; C0QC99; -. DR STRING; 177437.HRM2_40590; -. DR KEGG; dat:HRM2_40590; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_1_2_7; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000000442; 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..276 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_1000213148" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 120..140 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 154..174 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 227..247 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 255..275 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 276 AA; 29045 MW; 1B244DBC95736543 CRC64; MELYQGVVLG VLQGLTEFLP VSSSGHLVLG QNFFGITEPA LSFDISVHLG TLFAVALVFF KEIKAMVVSL GRLVQNLGSL KNFKQVVKAD GDVRLAALII VGSIPTAVIG LILKNYVHAL FSSLVIVGSM LMVTGTFLWL TRHSTPGGKK VEQIGFGTAL FIGVCQGVAV IPGISRSGAT IAAGLFSGVE RETAARYSFL LSMPAIAGAE ILSLKESFAT GAGFDTVTLL STLTAFIVGT LALVALLKIV KKGRFYLFAP YCWVVGLISI IAGFVA //