ID A0A1Q9VYY7_9MICO Unreviewed; 290 AA.
AC A0A1Q9VYY7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
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=BJF88_07190 {ECO:0000313|EMBL:OLT55215.1};
OS Cellulosimicrobium sp. CUA-896.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=1517881 {ECO:0000313|EMBL:OLT55215.1, ECO:0000313|Proteomes:UP000185790};
RN [1] {ECO:0000313|EMBL:OLT55215.1, ECO:0000313|Proteomes:UP000185790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUA-896 {ECO:0000313|EMBL:OLT55215.1,
RC ECO:0000313|Proteomes:UP000185790};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT55215.1}.
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DR EMBL; MKKH01000003; OLT55215.1; -; Genomic_DNA.
DR RefSeq; WP_075827445.1; NZ_MKKH01000003.1.
DR AlphaFoldDB; A0A1Q9VYY7; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000185790; 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 Reference proteome {ECO:0000313|Proteomes:UP000185790};
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 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 226..249
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ SEQUENCE 290 AA; 30749 MW; A1626F120F34F65B CRC64;
MNAWEAVLLG LVQGLTEFLP ISSSAHLRIV GELLGSDPGA AFTAITQIGT ETAVLLYFRR
DIARICAAWW RSLRGDHGSD WRSRTGRADH DAAMAWFIAL GSIPIVVLGL LFQESIENTF
RNLYLTALML AVFALVLGWA DRVGAKRRTL RELTPRQAVA FGFAQALALV PGVSRSGGTI
TAGLLMGFTR EAAARYSFLL AIPAVLGSGF YQLVKSAGEP EPGAPGAGAT LIATLVAFVV
GYLVIIAFLK IVSTFSYAPF VVYRLGLAAL VVLLLLVGVL EPGGTAASTP
//