ID   UPPP_SYNJA              Reviewed;         276 AA.
AC   Q2JXZ9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=CYA_0087;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABC98318.1; -; Genomic_DNA.
DR   RefSeq; WP_011429010.1; NC_007775.1.
DR   AlphaFoldDB; Q2JXZ9; -.
DR   SMR; Q2JXZ9; -.
DR   STRING; 321327.CYA_0087; -.
DR   EnsemblBacteria; ABC98318; ABC98318; CYA_0087.
DR   KEGG; cya:CYA_0087; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_1_0_3; -.
DR   OMA; IEGPFRD; -.
DR   OrthoDB; 1826154at2; -.
DR   Proteomes; UP000008818; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..276
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000250275"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        152..172
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        226..246
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   276 AA;  30083 MW;  39E5D9E10B5E0183 CRC64;
     MLADIWYPNW WQALVLGMVQ GITEFLPISS TAHLRVFPAL LGWPDAGASF AAVIQLGSLG
     AVLIYFASDL RQLLLGSWKA WQKRDFQEES WRLLMGILVG TLPIVIAGWA VKAIWGSPPR
     QLWVVAAAAI GLALALGWAE RVGKRRRDLH SLGIGDGLWV GLAQALALIP GVSRSGVTLT
     AALLLDLQRS AAARYSFLLG IPALFLAGVA EFIAEFRAEA LLSQGLGTLS AFVFSYGSID
     WLIRFLQRSS TWVFIVYRIG FGLFIFLGLA LGFLQP