ID UPPP_ECO57 Reviewed; 273 AA. AC P60933; P31054; P39203; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 1. DT 27-MAR-2024, entry version 114. 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=Z4410, ECs3940; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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; AE005174; AAG58191.1; -; Genomic_DNA. DR EMBL; BA000007; BAB37363.1; -; Genomic_DNA. DR PIR; D91121; D91121. DR RefSeq; NP_311967.1; NC_002695.1. DR RefSeq; WP_001281927.1; NZ_VOAI01000009.1. DR AlphaFoldDB; P60933; -. DR SMR; P60933; -. DR STRING; 155864.Z4410; -. DR GeneID; 916234; -. DR KEGG; ece:Z4410; -. DR KEGG; ecs:ECs_3940; -. DR PATRIC; fig|386585.9.peg.4109; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_6; -. DR OMA; AWYRIVF; -. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; 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..273 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000151147" FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 45..65 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 116..136 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 190..210 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 222..242 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 252..272 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 273 AA; 29759 MW; 6BFAC099D5163352 CRC64; MSDMHSLLIA AILGVVEGLT EFLPVSSTGH MIIVGHLLGF EGDTAKTFEV VIQLGSILAV VVMFWRRLFG LIGIHFGRPL QHEGESKGRL TLIHILLGMI PAVVLGLLFH DTIKSLFNPI NVMYALVVGG LLLIAAECLK PKEPRAPGLD DMTYRQAFMI GCFQCLALWP GFSRSGATIS GGMLMGVSRY AASEFSFLLA VPMMMGATAL DLYKSWGFLT SGDIPMFAVG FITAFVVALI AIKTFLQLIK RISFIPFAIY RFIVAAAVYV VFF //