ID   UPPP_ANADE              Reviewed;         292 AA.
AC   Q2IMA5;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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}; OrderedLocusNames=Adeh_0157;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP000251; ABC79934.1; -; Genomic_DNA.
DR   RefSeq; WP_011419217.1; NC_007760.1.
DR   AlphaFoldDB; Q2IMA5; -.
DR   SMR; Q2IMA5; -.
DR   STRING; 290397.Adeh_0157; -.
DR   EnsemblBacteria; ABC79934; ABC79934; Adeh_0157.
DR   KEGG; ade:Adeh_0157; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_1_0_7; -.
DR   OMA; IEGPFRD; -.
DR   Proteomes; UP000001935; 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.
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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..292
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000250224"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   292 AA;  30535 MW;  52EEE77BB4BB72FC CRC64;
     MSLVSAALFG LVQALTEFLP VSSTAHLLVF GELLGHSLDD RRFRAFVTII QAGTTLAVLI
     YFRADIARLV AASTRGLVRG KPLGTPEARL GWYILLGTLP AALAGKLLER RIEALGNWVI
     AGSLVGLGLV LLAAERLASH RRRVEDVGPG DALLIGVAQA LALVPGSSRS GTTITGGMLL
     GFTREAAARF SFLLSVPITL AAGAYKLWST VPDLRGEVAW TVATVVGTVV SAVAGYLVID
     WLLAWLRTRT TYVFVVWRIA AGAAIAALIL SGVLPAGAEA PPPPPPALHA AP