UPPP_LIMF3
ID UPPP_LIMF3 Reviewed; 276 AA.
AC B2GDY8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=LAF_1534;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008937; BAG27870.1; -; Genomic_DNA.
DR RefSeq; WP_004562945.1; NC_010610.1.
DR AlphaFoldDB; B2GDY8; -.
DR SMR; B2GDY8; -.
DR EnsemblBacteria; BAG27870; BAG27870; LAF_1534.
DR GeneID; 61201126; -.
DR KEGG; lfe:LAF_1534; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_9; -.
DR OMA; IEGPFRD; -.
DR OrthoDB; 1826154at2; -.
DR Proteomes; UP000001697; 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 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_1000197378"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 276 AA; 30754 MW; 486324C8C3E20737 CRC64;
MLEILKAVIL GIVEGITEFL PISSTGHLVL VDEFIKLNEP KKFIDMFNVV IQLGAIMAVV
VLYFHKLNPW SPKKSRLERS QTWTLWKKVI IAVIPSVIIG LPLNDWMDAH LMNWLVVSIA
LIVYGVLFIV IENHNQNLRP RFDSLNTLPY KVAILIGCFQ ILSLIPGTSR SGATILGAIL
IGTSRYVAAE FSFFLAIPTM FGASLLKLYK FFAHGGTLAG NQGLILAVGV IVSFVVAYAS
IRFLLNYIKT KDFKAFGWYR IILGVIVIAY FALLAH