ID UPPP_RHIME Reviewed; 268 AA. AC Q92SP2; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 105. 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=R00328; ORFNames=SMc00408; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., RA Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium RT meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(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; AL591688; CAC41765.1; -; Genomic_DNA. DR RefSeq; NP_384434.1; NC_003047.1. DR RefSeq; WP_010968508.1; NC_003047.1. DR AlphaFoldDB; Q92SP2; -. DR SMR; Q92SP2; -. DR EnsemblBacteria; CAC41765; CAC41765; SMc00408. DR GeneID; 61601808; -. DR KEGG; sme:SMc00408; -. DR PATRIC; fig|266834.11.peg.1699; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_5; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000001976; 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 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..268 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000151187" FT TRANSMEM 5..25 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 268 AA; 28479 MW; 14810C607D7FF3C7 CRC64; MADQSIISAL VLGLIEGLTE FIPVSSTAHV LLAGHFLGFK SPGNTFAVLI QLGAILAILL VYFQKLLAIA LALPTSVKAR RFVFSVLLAF LPAALIGAAA HGFIKSVLFE TPMLICVVLI VGGIILYAID RLPLTPRYTD VFDYPPSLAL KIGLFQCLAM IPGTSRSGAT IAGALLMGTD KRSAAEFSFF LAMPTMVGAF ALDLYKNRDA LSFDDVGLIA AGFIAAFIAG IFVVRSLLDF VSHRGFTPFA IWRILVGTAG LVGLWLLG //