ID A0A014KZP4_9ACTN Unreviewed; 278 AA. AC A0A014KZP4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 27-SEP-2017, entry version 19. 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=Z951_41335 {ECO:0000313|EMBL:EXU62476.1}; OS Streptomyces sp. PRh5. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1158056 {ECO:0000313|EMBL:EXU62476.1, ECO:0000313|Proteomes:UP000019949}; RN [1] {ECO:0000313|EMBL:EXU62476.1, ECO:0000313|Proteomes:UP000019949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRh5 {ECO:0000313|EMBL:EXU62476.1, RC ECO:0000313|Proteomes:UP000019949}; RA Zhu D., Yang H., Wang Y., Zhang Z., Yan R.; RT "Whole-genome shotgun assembly and analysis of the genome of RT Streptomyces sp. PRh5, a strain for production of geldanamycin, RT nigericin and nocardamine."; 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:EXU62476.1}. 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; JABQ01000103; EXU62476.1; -; Genomic_DNA. DR RefSeq; WP_037963843.1; NZ_JABQ01000103.1. DR EnsemblBacteria; EXU62476; EXU62476; Z951_41335. DR PATRIC; fig|1158056.3.peg.8282; -. DR Proteomes; UP000019949; 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:UP000019949}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01006, KW ECO:0000256|SAAS:SAAS00702354, ECO:0000313|EMBL:EXU62476.1}; 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 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 46 66 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 93 115 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 121 139 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 192 211 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 223 245 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. FT TRANSMEM 257 276 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01006}. SQ SEQUENCE 278 AA; 29085 MW; F672AC00A27DEDC8 CRC64; MSAISIGQAA VLGIVEGITE FLPVSSTGHL KITEGLMGIP VDDASVVGFT AVIQVGAIAA VLVYFFKDIV RIVSAWGRGL AHREQRYHHD YKFAWWVICA TIPIVIVGLA AKPLIEGPLA SLWVVAGSLV AGSGVMWVAD QMGRHKRGED DTGFKDAMLV GCSQILALLF PGFSRSGATM STALILDLDR VAATRLSFFL GIPALTGAGL YELKDAVGAG VGTAPLVVGT AVSFVVAYAS IAWLLKFVAK HSFNAFVVYR VAIGVLLLGL LGTGALTA //