ID   UPPP_STRMU              Reviewed;         281 AA.
AC   Q8CWZ1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SMU_244;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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 membrane {ECO:0000255|HAMAP-Rule:MF_01006};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; AE014133; AAN58014.1; -; Genomic_DNA.
DR   RefSeq; NP_720708.1; NC_004350.2.
DR   RefSeq; WP_002262750.1; NC_004350.2.
DR   AlphaFoldDB; Q8CWZ1; -.
DR   SMR; Q8CWZ1; -.
DR   STRING; 210007.SMU_244; -.
DR   EnsemblBacteria; AAN58014; AAN58014; SMU_244.
DR   KEGG; smu:SMU_244; -.
DR   PATRIC; fig|210007.7.peg.211; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_2_0_9; -.
DR   OMA; IEGPFRD; -.
DR   PhylomeDB; Q8CWZ1; -.
DR   Proteomes; UP000002512; 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 membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..281
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151213"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        86..106
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        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        196..216
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   281 AA;  31363 MW;  91F653A107674654 CRC64;
     MLFFEIIKAI IFGIVEGITE WLPISSTGHL ILVEEFIHFN NANAAFTNMF NVVIQLGAIL
     AVVVIYFDRL NPFKSGKTAR EVQITWQLWA KVILSALPAA VIGLIFDDWL DAHFQNFFSV
     ALMLILYGIA FIYVERRHQG VEPQVTHLVS LPYKTAFFIG LFQVLSLIPG TSRSGATILG
     GILLGTSRQV ATEFTFFLGI PIMFGASLVK VLKFIVSGTI LTGSQLFILL VAMLVAFAVS
     LYVIRFLTDY VKNHDFTFFG KYRIGLGILL LFYGLMKVLF G