ID UPPP_PSEU2 Reviewed; 276 AA. AC Q4ZS30; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 90. 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=Psyr_3008; OS Pseudomonas syringae pv. syringae (strain B728a). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=205918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B728a; RX PubMed=16043691; DOI=10.1073/pnas.0504930102; RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., RA Kyrpides N.C., Ivanova N., Lindow S.E.; RT "Comparison of the complete genome sequences of Pseudomonas syringae pv. RT syringae B728a and pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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 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; CP000075; AAY38042.1; -; Genomic_DNA. DR RefSeq; WP_003400617.1; NC_007005.1. DR RefSeq; YP_236080.1; NC_007005.1. DR AlphaFoldDB; Q4ZS30; -. DR SMR; Q4ZS30; -. DR STRING; 205918.Psyr_3008; -. DR KEGG; psb:Psyr_3008; -. DR PATRIC; fig|205918.7.peg.3069; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_6; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000000426; 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; Transmembrane; Transmembrane helix. FT CHAIN 1..276 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000227633" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 85..105 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 109..129 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 183..203 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 218..238 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 254..274 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 276 AA; 30456 MW; FEA293950B302CD9 CRC64; MDLWTAAQAL ILGVVEGLTE FLPISSTGHQ IIVADLIDFG GERAMAFNII IQLGAILAVV WEFRRKILDV VVGLPKQQQA QRFTLNLLIA FMPAVVLGVI FADTIHHYLF NAITVATALV IGGVIMLWAE RREHTVRTET VDDMSWSDAL KIGLVQCLAM IPGTSRSGST IIGGLLFGLS RKAATEFSFF LAMPTMVGAA VYSGYKYRDM FRPDDFAVFA IGFVTSFIFA MIAVRGLLKF IATHSYAVFA WYRIAFGLLI LATWQFGWID WASAKA //