ID UPPP_MICLC Reviewed; 277 AA. AC C5CBT8; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 74. 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=Mlut_11800; OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Micrococcus. OX NCBI_TaxID=465515; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / RC NCTC 2665 / VKM Ac-2230; RX PubMed=19948807; DOI=10.1128/jb.01254-09; RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G., RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R., RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V., RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.; RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple RT free-living actinobacterium."; RL J. Bacteriol. 192:841-860(2010). 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; CP001628; ACS30685.1; -; Genomic_DNA. DR RefSeq; WP_010078676.1; NZ_WBMF01000163.1. DR AlphaFoldDB; C5CBT8; -. DR SMR; C5CBT8; -. DR STRING; 465515.Mlut_11800; -. DR EnsemblBacteria; ACS30685; ACS30685; Mlut_11800. DR KEGG; mlu:Mlut_11800; -. DR PATRIC; fig|465515.4.peg.1121; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_1_0_11; -. DR BRENDA; 3.6.1.27; 3348. DR SABIO-RK; C5CBT8; -. DR Proteomes; UP000000738; 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:SF4; 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..277 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_1000213154" 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 90..110 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 191..211 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 224..244 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 277 AA; 29720 MW; 6989D2EE3A4B66AC CRC64; MTWIEAIILG LVQGLTEFLP ISSSAHIRIV GEFLPSATDP GAAFTAITQL GTELAVLIYF WRDITRIIGR WSAAVTGRIP HSDPDARMGW LIIVGSIPIA VLGLLLEDWI DTEFRSLWIT ATMLIVFGVL LALADRLGRQ TKPLEKLTVR DGVLYGLAQA LALIPGVSRS GGTIAAGLAM GYTRPAATRY AFLLAVPAVF ASGLYKLYTS LTDPGTQGPY GMGETLVATA VAFVVAYAVI AWLMRFISTN SYLPFVWYRI LLGGVLFALL GAGVISA //