ID D7CM81_SYNLT Unreviewed; 259 AA.
AC D7CM81;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, 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=Slip_1037 {ECO:0000313|EMBL:ADI01816.1};
OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophothermus.
OX NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI01816.1, ECO:0000313|Proteomes:UP000000378};
RN [1] {ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX DOI=10.4056/sigs.1233249;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1T).";
RL Stand. Genomic Sci. 3:267-275(2010).
RN [2] {ECO:0000313|EMBL:ADI01816.1, ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX PubMed=21304731;
RA Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1).";
RL Stand. Genomic Sci. 3:268-275(2010).
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 membrane {ECO:0000256|HAMAP-Rule:MF_01006};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01006}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; CP002048; ADI01816.1; -; Genomic_DNA.
DR RefSeq; WP_013175218.1; NC_014220.1.
DR AlphaFoldDB; D7CM81; -.
DR STRING; 643648.Slip_1037; -.
DR KEGG; slp:Slip_1037; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_1_0_9; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000000378; 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:SF2; 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};
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:ADI01816.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006};
KW Reference proteome {ECO:0000313|Proteomes:UP000000378};
KW Transferase {ECO:0000313|EMBL:ADI01816.1};
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 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ SEQUENCE 259 AA; 27673 MW; 41D49711CAD3CDF0 CRC64;
MNYLDAVILG IVQGLTEFLP VSSSGHLVIF QKLLGFQQPG VTFEVMLHLG TLVAVIAAFW
SDVWGIIKKP MSRIVYLIIL GTIPAGLIGV FLKPLFEQAF ESLTVVGVGL IITGFLLVLG
EKLGTRAWWG KEVEQTSVGD ALFIGLLQGL AITPGISRSG STISAGLLRG LDREFAARFS
FLLSIPAILG AGILEGKDIL DSGIAGHSLA PYIVGTVTAA VSSYTAIRIV MGLVKRGRLS
LFSYYCWTVG ILILAFFRG
//
