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Database: UniProt
Entry: F3G691_PSESJ
LinkDB: F3G691_PSESJ
Original site: F3G691_PSESJ 
ID   F3G691_PSESJ            Unreviewed;       276 AA.
AC   F3G691;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=PSYPI_09350 {ECO:0000313|EMBL:EGH42591.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH42591.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH42591.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH42591.1,
RC   ECO:0000313|Proteomes:UP000004986};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH42591.1}.
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DR   EMBL; AEAI01000470; EGH42591.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3G691; -.
DR   PATRIC; fig|629263.4.peg.1543; -.
DR   HOGENOM; CLU_060296_2_0_6; -.
DR   Proteomes; UP000004986; 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   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};
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        45..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        83..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        108..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        187..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        217..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        250..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   276 AA;  30422 MW;  BBA3992F1D36FAD3 CRC64;
     MDLWTAAQAL ILGVVEGLTE FLPISSTGHQ IIVADLIDFG GERAMAFNII IQLGAILAVV
     WEVRRKILDV VVGLPKQQQA QRFTLNLLIA FMPAVVLGVI FADTIHHYLF NAITVATALV
     IGGVIMLWAE RREHTVRTET VDDMSWSDAL KIGLVQCLAM IPGTSRSGST IIGGLLFGLS
     RKAATEFSFF LAMPTMVGAA VYSGYKYRDM FRPDDFAVFA IGFITSFIFA MIAVRGLLKF
     IATHSYAVFA WYRIAFGLLI LATWQFGWID WASAKA
//
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