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Database: UniProt
Entry: G7H0I7_9ACTN
LinkDB: G7H0I7_9ACTN
Original site: G7H0I7_9ACTN 
ID   G7H0I7_9ACTN            Unreviewed;       279 AA.
AC   G7H0I7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ECO:0000313|EMBL:GAB09362.1};
GN   ORFNames=GOARA_036_00940 {ECO:0000313|EMBL:GAB09362.1};
OS   Gordonia araii NBRC 100433.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB09362.1, ECO:0000313|Proteomes:UP000035088};
RN   [1] {ECO:0000313|EMBL:GAB09362.1, ECO:0000313|Proteomes:UP000035088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB09362.1,
RC   ECO:0000313|Proteomes:UP000035088};
RA   Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia araii NBRC 100433.";
RL   Submitted (NOV-2011) 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:GAB09362.1}.
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DR   EMBL; BAEE01000036; GAB09362.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7H0I7; -.
DR   STRING; 1073574.GOARA_036_00940; -.
DR   Proteomes; UP000035088; 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:SF4; 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        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        114..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        187..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        226..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        257..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   279 AA;  29851 MW;  AF7D3C9CE1ED9AA1 CRC64;
     MVEMTWLQTI VLSVVQGLTE FLPISSSGHL RIVSELFFGD DAGASFTAVS QLGTEAAVLV
     FFARDIWRIV LAWFAGLRNP DARGSDYRIG WAVIVATIPI GIIGFFFADQ VRTAARNLWI
     TATVLILFSG VFWLAERYGT QQRSLEKVTM RDAIVMGLAQ CLALIPGVSR SGASASAGLF
     VGLEREAAFR LSFLLAIPAV TASGLFSLPD AFEPAGKGLA ASGPQLIVAV IIAFVVGYAA
     IAWLLKFVSQ HSMNWFGAYR VALGLFIIGL LASGTIAAQ
//
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