ID   UPPP1_PSEPF             Reviewed;         276 AA.
AC   Q3KD12;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Undecaprenyl-diphosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein 1 {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006};
GN   Name=uppP1 {ECO:0000255|HAMAP-Rule:MF_01006}; OrderedLocusNames=Pfl01_2602;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA74343.1; -; Genomic_DNA.
DR   RefSeq; WP_011334017.1; NC_007492.2.
DR   AlphaFoldDB; Q3KD12; -.
DR   SMR; Q3KD12; -.
DR   STRING; 205922.Pfl01_2602; -.
DR   EnsemblBacteria; ABA74343; ABA74343; Pfl01_2602.
DR   KEGG; pfo:Pfl01_2602; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_2_0_6; -.
DR   OMA; IEGPFRD; -.
DR   Proteomes; UP000002704; Chromosome.
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; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..276
FT                   /note="Undecaprenyl-diphosphatase 1"
FT                   /id="PRO_0000227630"
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        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   276 AA;  30315 MW;  95C1D6E85B689355 CRC64;
     MDLWTALQAL ILGVVEGLTE FLPISSTGHQ IIVADLLDFG GERAMAFNII IQLGAILAVV
     WEFRRKILDV VIGLPTQPSA RRFTANLLIA FLPAVVLGVI FADLIHHYLF NPITVAAALV
     VGGIVMLWAE QRQHEVHAET VDEIRWTDAL KIGFAQCLAM IPGTSRSGST IIGGLLFGLS
     RKTATEFSFF LAMPTMVGAA VYSGYKYRDL FVPADFPVFA IGFVTAFIFA MIAVRGLLKF
     IGSHSYAAFA WYRIVFGLVI LATWQFGWVD WTAAQP