ID A0A1W1UF54_DESTI Unreviewed; 274 AA. AC A0A1W1UF54; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 14-DEC-2022, entry version 16. 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=SAMN00017405_0756 {ECO:0000313|EMBL:SMB79414.1}; OS Desulfonispora thiosulfatigenes DSM 11270. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae; OC Desulfonispora. OX NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB79414.1, ECO:0000313|Proteomes:UP000192731}; RN [1] {ECO:0000313|EMBL:SMB79414.1, ECO:0000313|Proteomes:UP000192731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB79414.1, RC ECO:0000313|Proteomes:UP000192731}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-2017) 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 + 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:0000256|ARBA:ARBA00000759, ECO:0000256|HAMAP- CC Rule:MF_01006}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01006}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. 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 --------------------------------------------------------------------------- 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; FWWT01000005; SMB79414.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1W1UF54; -. DR STRING; 656914.SAMN00017405_0756; -. DR EnsemblBacteria; SMB79414; SMB79414; SAMN00017405_0756. DR Proteomes; UP000192731; 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 PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1. DR Pfam; PF02673; BacA; 1. DR TIGRFAMs; TIGR00753; undec_PP_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:UP000192731}; 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 48..66 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 87..104 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 116..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 154..182 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 188..211 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 223..244 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 256..273 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" SQ SEQUENCE 274 AA; 30963 MW; 559250C37925E95E CRC64; MFLIELLKAV FLGIVEGITE WLPISSTGHM ILVEEFMQLN ATAAFKEMFF VVIQLGAIMA VVLLFFHKLN PFSLRKSKLE KKETMSIWYK VIVGVIPAAV LGLLFDDWLN EQFYNYQTVA IMLIVYGILF IVIENRNRGR YGRVTSFEAL TYKTAFLIGM FQVLSLIPGT SRSGATILGA IILGTSRFIA AEYSFFLSIP VMFGASALKL LKFGLTFTQM EMYILLTGMI VAFVVSIIAI KFLLGYIKNN DFKAFGWYRI ILGILVFGYF IIFG //