UPPP_CAMJE
ID UPPP_CAMJE Reviewed; 267 AA.
AC Q9PIS4; Q0PBT4; Q46111;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Cj0205;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-138.
RC STRAIN=386-IP;
RX PubMed=7489896; DOI=10.1016/0378-1119(95)00515-8;
RA Bustamante V.H., Puente J.L., Sanchez-Lopez F., Bobadilla M., Calva E.;
RT "Identification of Campylobacter jejuni and C.coli using the rpoB gene and
RT a cryptic DNA fragment from C.jejuni.";
RL Gene 165:1-8(1995).
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; AL111168; CAL34374.1; -; Genomic_DNA.
DR EMBL; X76062; CAA53663.1; -; Genomic_DNA.
DR PIR; D81439; D81439.
DR PIR; S38664; S38664.
DR RefSeq; WP_002836742.1; NC_002163.1.
DR RefSeq; YP_002343663.1; NC_002163.1.
DR AlphaFoldDB; Q9PIS4; -.
DR SMR; Q9PIS4; -.
DR STRING; 192222.Cj0205; -.
DR PaxDb; Q9PIS4; -.
DR PRIDE; Q9PIS4; -.
DR EnsemblBacteria; CAL34374; CAL34374; Cj0205.
DR GeneID; 904549; -.
DR KEGG; cje:Cj0205; -.
DR PATRIC; fig|192222.6.peg.202; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_7; -.
DR OMA; IEGPFRD; -.
DR Proteomes; UP000000799; 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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..267
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000151128"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT CONFLICT 21
FT /note="I -> V (in Ref. 2; CAA53663)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="F -> L (in Ref. 2; CAA53663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29751 MW; 41496EE123753DDA CRC64;
MENLYALILG IIEGLTEFLP ISSTGHMILG TTILGIDIDE FWKSFLIIIQ LGSILAVIFV
FWRKLFQGLD IWLKLAVGFF PTGVIGLFVA KYLNALFNGW VVVGMLIFGG VVFILIELAH
KNKQYRINSL EEISFKQAFC IGIFQSLAMI PGTSRSGASI IGGLLLEFNR KVAAEFSFLL
AIPTMIIATA YSIYKEPELL GNANSLIPLG IGFITAFIVA VLVIKFFLKF ISKFDFIPFG
IYRIILGFVF FYLYYSGILN AGSEFKL
