ID   UPPP2_ENTFL             Reviewed;         276 AA.
AC   Q5WNX2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Undecaprenyl-diphosphatase {ECO:0000255|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01006};
GN   Name=uppP {ECO:0000255|HAMAP-Rule:MF_01006};
GN   Synonyms=bcrD {ECO:0000303|PubMed:15388429};
OS   Enterococcus faecalis (Streptococcus faecalis).
OG   Plasmid pJM01.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=AR01/DGVS;
RX   PubMed=15388429; DOI=10.1128/aac.48.10.3743-3748.2004;
RA   Manson J.M., Keis S., Smith J.M.B., Cook G.M.;
RT   "Acquired bacitracin resistance in Enterococcus faecalis is mediated by an
RT   ABC transporter and a novel regulatory protein, BcrR.";
RL   Antimicrob. Agents Chemother. 48:3743-3748(2004).
RN   [2]
RP   INDUCTION.
RC   STRAIN=AR01/DGVS;
RX   PubMed=18227063; DOI=10.1074/jbc.m709503200;
RA   Gauntlett J.C., Gebhard S., Keis S., Manson J.M., Pos K.M., Cook G.M.;
RT   "Molecular analysis of BcrR, a membrane-bound bacitracin sensor and DNA-
RT   binding protein from Enterococcus faecalis.";
RL   J. Biol. Chem. 283:8591-8600(2008).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP). Confers resistance to bacitracin. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01006};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01006};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01006}.
CC   -!- INDUCTION: Transcription is activated by the regulatory protein BcrR in
CC       the presence of bacitracin. {ECO:0000269|PubMed:15388429,
CC       ECO:0000269|PubMed:18227063}.
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:0000255|HAMAP-Rule:MF_01006}.
CC   -!- SIMILARITY: Belongs to the UppP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01006}.
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DR   EMBL; AY496968; AAS78449.1; -; Genomic_DNA.
DR   RefSeq; WP_002367748.1; NZ_VWNQ01000021.1.
DR   RefSeq; YP_004032990.1; NC_014726.1.
DR   AlphaFoldDB; Q5WNX2; -.
DR   SMR; Q5WNX2; -.
DR   BRENDA; 3.6.1.27; 2095.
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   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Plasmid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..276
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151150"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   276 AA;  30622 MW;  70FC7B0C571ED6B7 CRC64;
     MALDFIEILK VIFLGIVEGI TEWLPISSTG HMLLVDEFIT LNMSEAFKEM FFVVIQLGAI
     LAVVVMFWNK MFPFQFKNKS QSIIKKDTFS LWFKVAVACV PSAIMGILFD DYLDAHLHTP
     VVIAIMLILY GVLFIVIENR NKKRTATTST LADISYKTAL MIGVFQVLSL IPGTSRSGAT
     IIGALLIGVS RVAAAEFTFF LAVPTMLGAS AFKLLKFGFD FTSAELLTLV IGMAVAFAVS
     VFVIKFLMSY IKKHDFKVFG WYRIVLGILV LLITAI