ID   UPPP_STAAU              Reviewed;         291 AA.
AC   Q9KIN5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Undecaprenyl-diphosphatase;
DE            EC=3.6.1.27;
DE   AltName: Full=Bacitracin resistance protein;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase;
GN   Name=uppP; Synonyms=bacA, upk;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCUH29 / NCIMB 40771;
RX   PubMed=10878119; DOI=10.1099/00221287-146-7-1547;
RA   Chalker A.F., Ingraham K.A., Lunsford R.D., Bryant A.P., Bryant J.,
RA   Wallis N.G., Broskey J.P., Pearson S.C., Holmes D.J.;
RT   "The bacA gene, which determines bacitracin susceptibility in Streptococcus
RT   pneumoniae and Staphylococcus aureus, is also required for virulence.";
RL   Microbiology 146:1547-1553(2000).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP) (By similarity). Confers resistance to bacitracin. Is also
CC       required for virulence. {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 membrane {ECO:0000250}; Multi-pass membrane
CC       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; AF228662; AAF81096.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KIN5; -.
DR   SMR; Q9KIN5; -.
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 membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151203"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   291 AA;  32313 MW;  271C912498FDFD9A CRC64;
     MFIIELIKGI ILGVVEGLTE FAPVSSTGHM ILVDDMWLKS SEFLGSQSAF TFKIVIQLGS
     VFAAAWVFRE RFLEILHIGK HKHVEGENDQ QRRSKPRRLN LLHVLVGMVP AGILGLLFDD
     FIEEHLFSVP TVMIGLFVGA IYMIIADKYS VKVKNPQTVD QINYFQAFVI GISQAVAMWP
     GFSRSGSTIS TGVLMKLNHK AASDFTFIMA VPIMLAASGL SLLKHYQDIQ IADIPFYILG
     FLAAFTVGLI AIKTFLHLSN KIKLIPFAIY RIVLVIFIAI LYFGFGIGKG I