ID A0A2G6BQ27_9BACT Unreviewed; 278 AA. AC A0A2G6BQ27; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 05-DEC-2018, entry version 5. 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=CR982_06010 {ECO:0000313|EMBL:PID27300.1}; OS Candidatus Cloacimonetes bacterium. OC Bacteria; Candidatus Cloacimonetes. OX NCBI_TaxID=2030808 {ECO:0000313|EMBL:PID27300.1, ECO:0000313|Proteomes:UP000231330}; RN [1] {ECO:0000313|EMBL:PID27300.1, ECO:0000313|Proteomes:UP000231330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DOLZORAL124_31_13 {ECO:0000313|EMBL:PID27300.1}; RA Dudek N.K., Sun C.L., Burstein D., Kantor R.S., Aliaga Goltsman D.S., RA Bik E.M., Thomas B.C., Banfield J.F., Relman D.A.; RT "Novel microbial diversity and functional potential in the marine RT mammal oral microbiome."; RL Submitted (OCT-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 -!- 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:PID27300.1}. 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; PDON01000061; PID27300.1; -; Genomic_DNA. DR Proteomes; UP000231330; 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. 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:UP000231330}; 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 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 43 61 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 93 115 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 127 145 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 196 216 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 228 252 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 258 277 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. SQ SEQUENCE 278 AA; 30643 MW; D82D73BBE1F4ED4E CRC64; MSEIVKSIIM GIVQGATEFL PISSSGHLAL MHKFLNFQTE SNLFFDVMLH LATLIAVIIF FRDKIKDIIV GFFYGVKTLG KGGTFRESFL ESLYSRLSLL IIVGSIPTAA IGLIFKDLFE SYNSNLIVVG SALIVTSILL LLYEISRKGY KDENKLSFKD VFIIGIVQGI AIIPGISRSG STIAAAKLLR VKKETAASFS FLLSIPAVGG AFLLKLKDLF QENLSFDFAT VAAGFLASFI TGYLCLAMLL WLIRKANLKI FILYCFIMGS YALYYALN //