ID E6VX83_PSEA9 Unreviewed; 263 AA.
AC E6VX83;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|ARBA:ARBA00021581, ECO:0000256|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374, ECO:0000256|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein {ECO:0000256|ARBA:ARBA00032932, ECO:0000256|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707, ECO:0000256|HAMAP-Rule:MF_01006};
GN Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006};
GN OrderedLocusNames=Daes_1576 {ECO:0000313|EMBL:ADU62589.1};
OS Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS (Desulfovibrio aespoeensis).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU62589.1, ECO:0000313|Proteomes:UP000002191};
RN [1] {ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA Hazen T., Woyke T.;
RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU62589.1, ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RX PubMed=24874683;
RA Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA Goodwin L., Shapiro N.;
RT "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL Genome Announc. 2:e00509-14(2014).
CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC (UPP). Confers resistance to bacitracin. {ECO:0000256|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:0000256|ARBA:ARBA00000759, ECO:0000256|HAMAP-
CC Rule:MF_01006};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01006}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01006}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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 {ECO:0000256|HAMAP-Rule:MF_01006}.
CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|ARBA:ARBA00010621,
CC ECO:0000256|HAMAP-Rule:MF_01006}.
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DR EMBL; CP002431; ADU62589.1; -; Genomic_DNA.
DR RefSeq; WP_013514516.1; NC_014844.1.
DR AlphaFoldDB; E6VX83; -.
DR STRING; 643562.Daes_1576; -.
DR KEGG; das:Daes_1576; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_7; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000002191; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; 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:SF3; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR Pfam; PF02673; BacA; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW Rule:MF_01006}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01006};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01006}; Cell shape {ECO:0000256|HAMAP-Rule:MF_01006};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01006};
KW Kinase {ECO:0000313|EMBL:ADU62589.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006};
KW Transferase {ECO:0000313|EMBL:ADU62589.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01006};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01006}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 215..233
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ SEQUENCE 263 AA; 28612 MW; 5450A72B321D1854 CRC64;
MASWYVAVIL GIVEGLTEFL PVSSTGHLIL TSHLLGFTGP KAETFTIVIQ LGAILAVLTL
YLDRFIGLLR FDPQKNFSGP RGLWLLFLTS LPASLLGLAA HKYIKAYLFS PFTVACALAA
GAVMILVVES VDKQEKAATL DEITPWQALG IGLFQCLALW PGFSRSAATI MGGMLLGLRR
TVAAEYSFIA AVPIMVAATG YDFLKNYELF VADDLFFLAV GFGVSFIAAW AAIKGFIYLL
GRLTLRPFAV YRLTLVPLIF LFL
//
