ID   UPPP_RALN1              Reviewed;         293 AA.
AC   Q8Y1I9;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 113.
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}; Synonyms=bacA, upk;
GN   OrderedLocusNames=RSc0701; ORFNames=RS01606;
OS   Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01006}.
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   -!- SIMILARITY: Belongs to the UppP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01006}.
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DR   EMBL; AL646052; CAD14231.1; -; Genomic_DNA.
DR   RefSeq; WP_011000656.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y1I9; -.
DR   SMR; Q8Y1I9; -.
DR   STRING; 267608.RSc0701; -.
DR   EnsemblBacteria; CAD14231; CAD14231; RSc0701.
DR   GeneID; 60500219; -.
DR   KEGG; rso:RSc0701; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_2_0_4; -.
DR   Proteomes; UP000001436; Chromosome.
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   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; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..293
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151184"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   293 AA;  32256 MW;  EA353CBD53ACD6B0 CRC64;
     MDIALAIKAL ILGIVEGLTE FLPISSTGHL ILAGQLLDFN DEKGKIFEIV IQFGAILAVC
     WEFRHKIIDV IKGLPNDPRQ QRFALNVIVA TIPAITLALI FGKAIKAHLF NPIVVASAFI
     IGGLVILWAE WRERHRGQTH DPRGNALLEA AKAGAPRVET LDDLRLSDAF KVGLAQCFAL
     IPGTSRSGST IIGGLLFGLS RKVATEFSFF LAIPVIFGAT VYELYKERAL LSTDDLSIFG
     IGFVAAFISA FFCVRWLLRF IASHDFRGFA WYRIVFGVIV LVTAYTHLIA WQA
//