ID UPPP1_CORJK Reviewed; 281 AA. AC Q4JXD8; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Undecaprenyl-diphosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein 1 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006}; GN Name=uppP1 {ECO:0000255|HAMAP-Rule:MF_01006}; GN OrderedLocusNames=jk0367; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=306537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K411; RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., RA Rupp O., Schneiker S., Viehoever P., Puehler A.; RT "Complete genome sequence and analysis of the multiresistant nosocomial RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the RT human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). 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; CR931997; CAI36519.1; -; Genomic_DNA. DR RefSeq; WP_005296312.1; NC_007164.1. DR AlphaFoldDB; Q4JXD8; -. DR SMR; Q4JXD8; -. DR STRING; 306537.jk0367; -. DR GeneID; 3433526; -. DR KEGG; cjk:jk0367; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_1_0_11; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000000545; 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..281 FT /note="Undecaprenyl-diphosphatase 1" FT /id="PRO_0000227615" FT TRANSMEM 95..115 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 119..139 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 195..215 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 256..276 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 281 AA; 30422 MW; 0CFF3F6080F25A31 CRC64; MTDPATTMSW VQVIVLSVVQ GLTEFLPVSS SGHLRIVSQL FWGEDAGASF TAVIQLGTEL AVLVFFAKDI WRILTAWFAG LADKSKRNFD YRMGWMVIAG TIPVGLAGVL LKDLIRENFR NLWITATVLI LFSLVFILAE RRGKKTRGFE ELTMKDAVLM GLWQCLALIP GVSRSGGTIS GGLFLNLDRE VATRFSFLLA IPAVLASGLF SLPDAFDPQA GQAASGLQLL VGSGIGFVVG YISIAWLLKF VSNHSFAWFA AYRIPLGLLV MALLGTGVMA A //