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-SEP-2017, entry version 20. DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000256|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein {ECO:0000256|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {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; Proteobacteria; 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. RT elegans Gene Expression and Life History Traits."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl CC diphosphate (UPP). Confers resistance to bacitracin. CC {ECO:0000256|HAMAP-Rule:MF_01006}. CC -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate + CC H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01006, ECO:0000256|SAAS:SAAS00702352}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01006}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01006}. CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the CC inhibition of peptidoglycan synthesis by sequestering undecaprenyl CC diphosphate, thereby reducing the pool of lipid carrier available. CC {ECO:0000256|HAMAP-Rule:MF_01006}. CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|HAMAP- CC Rule:MF_01006, ECO:0000256|SAAS:SAAS00702351}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; EXU81510; EXU81510; AX13_06845. DR PATRIC; fig|1457173.3.peg.381; -. DR Proteomes; UP000020766; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; PTHR30622; 1. DR Pfam; PF02673; BacA; 1. DR TIGRFAMs; TIGR00753; undec_PP_bacA; 1. PE 3: Inferred from homology; KW Antibiotic resistance {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702335}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702333}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702357}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702339}; KW Complete proteome {ECO:0000313|Proteomes:UP000020766}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702354, ECO:0000313|EMBL:EXU81510.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702342}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702374}; KW Reference proteome {ECO:0000313|Proteomes:UP000020766}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702376}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702360}. FT TRANSMEM 97 119 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 125 144 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 196 217 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 229 250 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 262 281 Helical. {ECO:0000256|HAMAP-Rule: FT 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 //