ID   UPPP_CORGB              Reviewed;         293 AA.
AC   A4QEA1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
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};
GN   OrderedLocusNames=cgR_1575;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(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 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}.
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DR   EMBL; AP009044; BAF54567.1; -; Genomic_DNA.
DR   RefSeq; WP_011897266.1; NC_009342.1.
DR   AlphaFoldDB; A4QEA1; -.
DR   SMR; A4QEA1; -.
DR   KEGG; cgt:cgR_1575; -.
DR   HOGENOM; CLU_060296_1_0_11; -.
DR   PhylomeDB; A4QEA1; -.
DR   Proteomes; UP000006698; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..293
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000303025"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   293 AA;  31627 MW;  F90A9F77D16D067A CRC64;
     MNEEITLLAA AADPAATENI GWVQTIVLSI VQGLTEFLPI SSSGHLRIIS ELFWGADAGA
     SFTAVVQLGT EAAVLVFFAK EIWQIITGWF AGVFNKERRG FEYRMGWMII VATIPVVILG
     VLGKDLIREA LRNMWITASV LILFSLVFIL AEKMGKKERD YDKLTMKDAI IMGLAQCLAL
     IPGVSRSGGT ISAGLFLGLK REVATKFSFL LAIPAVLGSG LYSLPDAFAP SSGQAASGLQ
     LTVGTLFAFV VGYISIAWLM KFVANHSFSW FAAYRIPAGL LVMLLLALGM LNP
//