UPPP1_BACLD
ID UPPP1_BACLD Reviewed; 270 AA.
AC Q65LE3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Undecaprenyl-diphosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein 1 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006};
GN Name=uppP1 {ECO:0000255|HAMAP-Rule:MF_01006};
GN OrderedLocusNames=BLi01213, BL03255;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU40121.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU22775.1; -; Genomic_DNA.
DR RefSeq; WP_003180571.1; NC_006322.1.
DR AlphaFoldDB; Q65LE3; -.
DR SMR; Q65LE3; -.
DR STRING; 279010.BL03255; -.
DR EnsemblBacteria; AAU22775; AAU22775; BL03255.
DR GeneID; 66216650; -.
DR KEGG; bld:BLi01213; -.
DR KEGG; bli:BL03255; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_1_2_9; -.
DR OMA; VGGRWAQ; -.
DR OrthoDB; 1826154at2; -.
DR BioCyc; BLIC279010:BLI_RS06025-MON; -.
DR Proteomes; UP000000606; 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.
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..270
FT /note="Undecaprenyl-diphosphatase 1"
FT /id="PRO_0000151105"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 270 AA; 29692 MW; 0E2E9E2729AB6B17 CRC64;
MDFLVLIKYI LLGLLQGFTE PIPVSSSGHL VLAQHFLGLN IEGFSFELLM NAGSLIAVLL
VYKNDIFRLA VNGLSYVTTK NEKGKADFRF IIYLIIATIP AGVIGVLFDD EISAFFKDGV
RITAVTLLIT GLALFLIRNL RGRKSDGEIR LRDAVIIGFS QMVALVPGIS RSGATIVPAM
ALGLKSETAL RFSFLLYIPV SLGGTILSIT DIFHDPRLGE LFLPYLFAFI ASVIATYFSL
RWFMNIMAKG NLVYFSIYCF VIGIAVLIFA
