ID A0A0Q4DQE3_9FLAO Unreviewed; 272 AA.
AC A0A0Q4DQE3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=ASE55_14155 {ECO:0000313|EMBL:KQM38721.1};
OS Chryseobacterium sp. Leaf201.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1735672 {ECO:0000313|EMBL:KQM38721.1, ECO:0000313|Proteomes:UP000051097};
RN [1] {ECO:0000313|EMBL:KQM38721.1, ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|EMBL:KQM38721.1,
RC ECO:0000313|Proteomes:UP000051097};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM38721.1}.
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DR EMBL; LMKA01000083; KQM38721.1; -; Genomic_DNA.
DR RefSeq; WP_056220124.1; NZ_LMKA01000083.1.
DR AlphaFoldDB; A0A0Q4DQE3; -.
DR STRING; 1735672.ASE55_14155; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000051097; Unassembled WGS sequence.
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; 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};
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006};
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 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 140..165
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 254..271
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ SEQUENCE 272 AA; 30135 MW; B5CE984A2FDC4E5C CRC64;
MDLFKAILIA IIEGLTEYLP ISSTAHMGFT ASLLGLPEDE FLKMFQVSIQ FGAILSVVVA
YWKKFFDLKN LQFYLKLAFA VIPALVLGYL FDDTIEAVLG NQIAISAVLV LGGVVLLFAD
EWFKNPKIDD EKGVTIKKAV IIGFWQCLAM MPGTSRSAAS IIGGMSQGLT RKAAAEFSFF
LAVPTMLAVT VYSVFVKTWG RETGNPQKGY EMIMASQEHI TVFIVGNVVA FIVALIAIKA
FIGVLNKYGF KPWGWYRIFV GIALLIYFQF FK
//