ID UPPP_CYTH3 Reviewed; 263 AA. AC Q11WJ0; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 91. 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; GN OrderedLocusNames=CHU_0949; OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC OS 15051 / NCIMB 9469 / D465). OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Cytophaga. OX NCBI_TaxID=269798; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / RC D465; RX PubMed=17400776; DOI=10.1128/aem.00225-07; RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., RA McBride M.J.; RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga RT hutchinsonii."; RL Appl. Environ. Microbiol. 73:3536-3546(2007). 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; CP000383; ABG58226.1; -; Genomic_DNA. DR RefSeq; WP_011584341.1; NZ_FPJX01000005.1. DR AlphaFoldDB; Q11WJ0; -. DR SMR; Q11WJ0; -. DR STRING; 269798.CHU_0949; -. DR KEGG; chu:CHU_0949; -. DR eggNOG; COG1968; Bacteria. DR HOGENOM; CLU_060296_2_0_10; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000001822; 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..263 FT /note="Undecaprenyl-diphosphatase" FT /id="PRO_0000290704" FT TRANSMEM 1..21 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 97..117 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 132..152 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 208..228 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" FT TRANSMEM 238..258 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006" SQ SEQUENCE 263 AA; 29183 MW; DA643E5CE23E3C26 CRC64; MTWLESIILA IVEGVTEFLP VSSTGHMIIT SALMGIKSDP FTKVFEVAIQ FGAILSVVVL YFKRFFKSCD FYFKLFVAFI PTAIVGLLLK KHIDTWLENV WVVASTLLVG GIVLLFVDKW FQKNETEGEE EVSYQTGFLI GCFQCLAMIP GVSRSAATII GGLTQKLTRK AAAEFSFFLA VPTMFAATAK SLYDEKELIL ESTDKIPLLL LGNVVAFIVA MLAIKFFINI LTKYGFKAFG YYRIALGALL LILLAMHVDL QVV //