ID   UPPP_AZOBR              Reviewed;         187 AA.
AC   P39438;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Undecaprenyl-diphosphatase;
DE            EC=3.6.1.27;
DE   AltName: Full=Bacitracin resistance protein;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase;
DE   Flags: Fragment;
GN   Name=uppP; Synonyms=bacA, upk;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=8428988; DOI=10.1016/s0021-9258(18)53664-4;
RA   Pelanda R., Vanoni M.A., Perego M., Piubelli L., Galizzi A., Curti B.,
RA   Zanetti G.;
RT   "Glutamate synthase genes of the diazotroph Azospirillum brasilense.
RT   Cloning, sequencing, and analysis of functional domains.";
RL   J. Biol. Chem. 268:3099-3106(1993).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP). Confers resistance to bacitracin (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
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:0000305}.
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DR   EMBL; AF192408; AAA22178.2; -; Genomic_DNA.
DR   AlphaFoldDB; P39438; -.
DR   SMR; P39438; -.
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-EC.
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-KW.
DR   InterPro; IPR003824; UppP.
DR   PANTHER; PTHR30622; PTHR30622; 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..>187
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151083"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         187
SQ   SEQUENCE   187 AA;  19842 MW;  E04C8995BCFDB63A CRC64;
     MLIDQYLDAA LLGLIEGLTE FLPVSSTGHL IIFDTLLGFE GPPGKVFEVV IQLGAILAIC
     TVYFARLWKV VTGLKDDPGA RHFAMAVILA FLPAMVLGAA LHGVIKAVLF NPTVVSIALI
     LGGVAILMAE RLVPAPRYHQ IERFPAPLAL KIGLCQCLAL VPGVSRSGAT ILGSLLMGVD
     RRTAAEF