ID A0A014KZP4_9ACTN Unreviewed; 278 AA. AC A0A014KZP4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 24-JUL-2024, entry version 32. 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=Z951_41335 {ECO:0000313|EMBL:EXU62476.1}; OS Streptomyces sp. PRh5. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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 Streptomyces RT sp. PRh5, a strain for production of geldanamycin, nigericin and RT nocardamine."; RL Submitted (JAN-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A014KZP4; -. DR PATRIC; fig|1158056.3.peg.8282; -. DR OrthoDB; 9808289at2; -. DR Proteomes; UP000019949; 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: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 NCBIfam; TIGR00753; undec_PP_bacA; 1. DR PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1. DR PANTHER; PTHR30622:SF3; UNDECAPRENYL-DIPHOSPHATASE; 1. DR Pfam; PF02673; 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 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 46..66 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 93..115 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 121..139 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 192..211 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 223..245 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006" FT TRANSMEM 257..276 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule: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 //