UPPP_STRPN
ID UPPP_STRPN Reviewed; 281 AA.
AC P60934; Q97SC8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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; OrderedLocusNames=SP_0457;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP FUNCTION.
RC STRAIN=0100993 / NCIMB 40794 / Serotype 3;
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, ECO:0000269|PubMed:10878119}.
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; AE005672; AAK74617.1; -; Genomic_DNA.
DR PIR; H95052; H95052.
DR RefSeq; WP_000280773.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P60934; -.
DR SMR; P60934; -.
DR STRING; 170187.SP_0457; -.
DR EnsemblBacteria; AAK74617; AAK74617; SP_0457.
DR GeneID; 60233099; -.
DR GeneID; 66805644; -.
DR KEGG; spn:SP_0457; -.
DR eggNOG; COG1968; Bacteria.
DR OMA; IEGPFRD; -.
DR PhylomeDB; P60934; -.
DR BioCyc; SPNE170187:G1FZB-472-MON; -.
DR Proteomes; UP000000585; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..281
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000151214"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 281 AA; 31810 MW; 0575353B1BDF97C2 CRC64;
MYLIEILKSI FFGIVEGITE WLPISSTGHL ILAEEFIQYQ NQNEAFMSMF NVVIQLGAIL
AVMVIYFNKL NPFKPTKDKQ EVRKTWRLWL KVLIATLPLL GVFKFDDWFD THFHNMVSVA
LMLIIYGVAF IYLEKRNKAR AIEPSVTELD KLPYTTAFYI GLFQVLALLP GTSRSGATIV
GGLLNGTSRS VVTEFTFYLG IPVMFGASAL KIFKFVKAGE LLSFGQLFLL LVAMGVAFAV
SMVAIRFLTS YVKKHDFTLF GKYRIVLGSV LLLYSFVRLF V