ID A0A1H2F1D4_9BACT Unreviewed; 292 AA.
AC A0A1H2F1D4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|ARBA:ARBA00021581};
DE EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374};
DE AltName: Full=Bacitracin resistance protein {ECO:0000256|ARBA:ARBA00032932};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707};
GN ORFNames=SAMN05444156_1431 {ECO:0000313|EMBL:SDU01142.1};
OS Verrucomicrobium sp. GAS474.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobiaceae; Verrucomicrobium.
OX NCBI_TaxID=1882831 {ECO:0000313|EMBL:SDU01142.1, ECO:0000313|Proteomes:UP000198591};
RN [1] {ECO:0000313|EMBL:SDU01142.1, ECO:0000313|Proteomes:UP000198591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS474 {ECO:0000313|EMBL:SDU01142.1,
RC ECO:0000313|Proteomes:UP000198591};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UppP family.
CC {ECO:0000256|ARBA:ARBA00010621}.
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DR EMBL; LT629781; SDU01142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2F1D4; -.
DR STRING; 1882831.SAMN05444156_1431; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000198591; Chromosome i.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR003824; UppP.
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};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198591};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 292 AA; 30746 MW; 764BA7347D504846 CRC64;
MYPTWLQIAF LGLIQGAAEL LPVSSSAHVI VAEKLMGLDP STPAMTFLLV MLHTGTMAAV
ILYFWKAWKE SYFSSAARFK EVVILVVVAS VATALVGGVL KVVIEKILVA TTGGAKSELE
HLFSSLPLIA GALTAAGIVI LVSGYRTRGQ GEEAGGEVTL PSAGWIGAMQ GICLPFRGFS
RSGATISAGL LLGITRRRAE EFSFALAVAL TPPVLAKELH RFLKAEREAG AGLADLPNLL
LPGLAGMIFS FLAGLLALKF LSRLLEGGKW HYFGWYCLGA AAVVAALAAC GW
//
