ID UPPP_CAMJE Reviewed; 267 AA. AC Q9PIS4; Q0PBT4; Q46111; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 124. 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, upk; GN OrderedLocusNames=Cj0205; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-138. RC STRAIN=386-IP; RX PubMed=7489896; DOI=10.1016/0378-1119(95)00515-8; RA Bustamante V.H., Puente J.L., Sanchez-Lopez F., Bobadilla M., Calva E.; RT "Identification of Campylobacter jejuni and C.coli using the rpoB gene and RT a cryptic DNA fragment from C.jejuni."; RL Gene 165:1-8(1995). 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; AL111168; CAL34374.1; -; Genomic_DNA. DR EMBL; X76062; CAA53663.1; -; Genomic_DNA. DR PIR; D81439; D81439. DR PIR; S38664; S38664. DR RefSeq; WP_002836742.1; NZ_SZUC01000006.1. DR RefSeq; YP_002343663.1; NC_002163.1. DR AlphaFoldDB; Q9PIS4; -. DR SMR; Q9PIS4; -. DR STRING; 192222.Cj0205; -. DR PaxDb; 192222-Cj0205; -. DR EnsemblBacteria; CAL34374; CAL34374; Cj0205. DR GeneID; 904549; -. DR KEGG; cje:Cj0205; -. DR PATRIC; fig|192222.6.peg.202; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_7; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000000799; 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..267 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000151128" FT TRANSMEM 4..24 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 69..89 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 173..193 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 239..259 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT CONFLICT 21 FT /note="I -> V (in Ref. 2; CAA53663)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="F -> L (in Ref. 2; CAA53663)" FT /evidence="ECO:0000305" SQ SEQUENCE 267 AA; 29751 MW; 41496EE123753DDA CRC64; MENLYALILG IIEGLTEFLP ISSTGHMILG TTILGIDIDE FWKSFLIIIQ LGSILAVIFV FWRKLFQGLD IWLKLAVGFF PTGVIGLFVA KYLNALFNGW VVVGMLIFGG VVFILIELAH KNKQYRINSL EEISFKQAFC IGIFQSLAMI PGTSRSGASI IGGLLLEFNR KVAAEFSFLL AIPTMIIATA YSIYKEPELL GNANSLIPLG IGFITAFIVA VLVIKFFLKF ISKFDFIPFG IYRIILGFVF FYLYYSGILN AGSEFKL //