ID A0A014P5Q8_9BURK Unreviewed; 282 AA. AC A0A014P5Q8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 27-NOV-2024, entry version 37. DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|ARBA:ARBA00021581, ECO:0000256|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374, ECO:0000256|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein {ECO:0000256|ARBA:ARBA00032932, ECO:0000256|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707, ECO:0000256|HAMAP-Rule:MF_01006}; GN Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006}; GN ORFNames=AX13_06845 {ECO:0000313|EMBL:EXU81510.1}; OS Comamonas aquatica DA1877. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU81510.1, ECO:0000313|Proteomes:UP000020766}; RN [1] {ECO:0000313|EMBL:EXU81510.1, ECO:0000313|Proteomes:UP000020766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU81510.1, RC ECO:0000313|Proteomes:UP000020766}; RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P., RA Caudy A.A., Walhout A.J.; RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans RT Gene Expression and Life History Traits."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate CC (UPP). Confers resistance to bacitracin. {ECO:0000256|HAMAP- CC Rule:MF_01006}. CC -!- CATALYTIC ACTIVITY: CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di- CC trans,octa-cis-undecaprenyl phosphate + phosphate + H(+); 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:0000256|ARBA:ARBA00000759, ECO:0000256|HAMAP- CC Rule:MF_01006}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651, CC ECO:0000256|HAMAP-Rule:MF_01006}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-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 {ECO:0000256|HAMAP-Rule:MF_01006}. CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|ARBA:ARBA00010621, CC ECO:0000256|HAMAP-Rule:MF_01006}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EXU81510.1}. 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; JBOK01000002; EXU81510.1; -; Genomic_DNA. DR RefSeq; WP_043378369.1; NZ_JBOK01000002.1. DR AlphaFoldDB; A0A014P5Q8; -. DR STRING; 225991.MA05_01750; -. DR PATRIC; fig|1457173.3.peg.381; -. DR Proteomes; UP000020766; Unassembled WGS sequence. 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:SF4; UNDECAPRENYL-DIPHOSPHATASE; 1. DR Pfam; PF02673; BacA; 1. PE 3: Inferred from homology; KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP- KW Rule:MF_01006}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01006}; Cell shape {ECO:0000256|HAMAP-Rule:MF_01006}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01006}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006}; KW Reference proteome {ECO:0000313|Proteomes:UP000020766}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01006}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01006}. FT TRANSMEM 97..119 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 125..144 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 196..217 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 229..250 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 262..281 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" SQ SEQUENCE 282 AA; 30552 MW; 77D928B420F87E40 CRC64; MNATFGWLDA LILGLVQGLT EFLPISSSAH LRILGPLLPG GADPGAAFTA ITQLGTELAV LIYFRKDVLR MLVAWFASLP VIGSRRPGEA LHPDAKLAWL VILGTIPICV LGLLLRSWIE TTFRTLALTA VMLIVFGLLL GWAEKRSTQT RQIGQLGLRD GIVLGFAQAM ALIPGVSRSG GTITAGLLLG MTREAAARFS FLLAIPAVLL SGFYQLLFKR DPMSGEQWML TFMATAIAFV VGYAVIVWFM RLISNKGFGF FVIYRVLLGL AILAGLHFGF IQ //