ID   UPPP_MYCLE              Reviewed;         282 AA.
AC   Q9CC42; Q49783; Q49788;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=ML1297; ORFNames=B2126_C2_190/B2126_C3_227;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17193.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00017; AAA17200.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00017; AAA17193.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL583921; CAC31678.1; -; Genomic_DNA.
DR   PIR; C87071; C87071.
DR   PIR; S72853; S72853.
DR   PIR; S72860; S72860.
DR   RefSeq; NP_301931.1; NC_002677.1.
DR   AlphaFoldDB; Q9CC42; -.
DR   SMR; Q9CC42; -.
DR   STRING; 272631.gene:17575131; -.
DR   KEGG; mle:ML1297; -.
DR   PATRIC; fig|272631.5.peg.2399; -.
DR   Leproma; ML1297; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_1_0_11; -.
DR   OrthoDB; 9808289at2; -.
DR   Proteomes; UP000000806; Chromosome.
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   NCBIfam; TIGR00753; undec_PP_bacA; 1.
DR   PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR   PANTHER; PTHR30622:SF4; UNDECAPRENYL-DIPHOSPHATASE; 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..282
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151164"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        228..248
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"
FT   CONFLICT        116
FT                   /note="S -> P (in Ref. 1; AAA17193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   282 AA;  30273 MW;  845022213C3A60B9 CRC64;
     MTAVSAMSWW QVIVLAVVQG LTEFLPVSSS GHLAIVSRIL FTGDAGASFT AVSQLGTEVA
     VLVYFGRDIV RILHAWCRGL TVTLHRTADY WLGWYVIIGT IPICILGLVC KDEIRSGIRP
     LWVVATALVA FSGVIAFAEY VGRQNRCIEQ LNWRDALVVG VAQTLALIPG VSRSGSTISA
     GLFLGLDREL AARFGFLLAI PAVFASGLFS IPDAFHPITE GMSATGAQLL VATVIAFVVG
     LVAVSWLLRF LVQHNLYWFV GYRIVVGVGV LILLAVKTVA AT
//