ID A0A1W1UF54_DESTI Unreviewed; 274 AA. AC A0A1W1UF54; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 05-DEC-2018, entry version 6. 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=SAMN00017405_0756 {ECO:0000313|EMBL:SMB79414.1}; OS Desulfonispora thiosulfatigenes DSM 11270. OC Bacteria; Firmicutes; Clostridia; Clostridiales; 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 CC diphosphate (UPP). Confers resistance to bacitracin. CC {ECO:0000256|HAMAP-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; CC EC=3.6.1.27; Evidence={ECO:0000256|HAMAP-Rule:MF_01006, CC 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 --------------------------------------------------------------------------- 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 Proteomes; UP000192731; 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:UP000192731}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702354}; 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:UP000192731}; 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 48 66 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 87 104 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 116 133 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 154 182 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 188 211 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 223 244 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 256 273 Helical. {ECO:0000256|HAMAP-Rule: FT 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 //