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Database: UniProt
Entry: A0A3R8TYU1_9GAMM
LinkDB: A0A3R8TYU1_9GAMM
Original site: A0A3R8TYU1_9GAMM 
ID   A0A3R8TYU1_9GAMM        Unreviewed;       264 AA.
AC   A0A3R8TYU1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   03-MAY-2023, entry version 11.
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=EGJ34_13330 {ECO:0000313|EMBL:RRU11569.1};
OS   Stenotrophomonas sp. 278.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=2479851 {ECO:0000313|EMBL:RRU11569.1, ECO:0000313|Proteomes:UP000274083};
RN   [1] {ECO:0000313|EMBL:RRU11569.1, ECO:0000313|Proteomes:UP000274083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=278 {ECO:0000313|EMBL:RRU11569.1,
RC   ECO:0000313|Proteomes:UP000274083};
RA   D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA   Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT   "Transmission dynamics of multidrug resistant bacteria on intensive care
RT   unit surfaces.";
RL   Submitted (OCT-2018) 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:RRU11569.1}.
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DR   EMBL; RHPP01000076; RRU11569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R8TYU1; -.
DR   OrthoDB; 9808289at2; -.
DR   Proteomes; UP000274083; 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..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        105..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        181..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        215..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        246..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   264 AA;  28569 MW;  10C99F5BCE35678D CRC64;
     MSDLLSALLL GILEGLTEFL PISSTGHLLI AQHWLGERSD FFNIVIQAGA ILAITLVFRQ
     RLWQLATGLH EKANRDYVLK LGTAFLVTAV VGLPVRLAGW ELPETVTPIA WALIIGGIWM
     LLVEARTAKL PDRTEVTWTV AVLVGLAQVV AGVFPGTSRS ASAIFVAMLF GLSRRAAATE
     FVFLVGIPTM FAASAYAFLE LAKDGKLASE NWTDVGVAFV AAIITGFVVV KWLLGYIKQH
     RFTAFAFYRI ALGVGLLLWL PAGS
//
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