ID W0I2E0_9GAMM Unreviewed; 273 AA.
AC W0I2E0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=bacA {ECO:0000313|EMBL:AHF78603.1};
GN Synonyms=uppP {ECO:0000256|HAMAP-Rule:MF_01006};
GN ORFNames=Sant_3621 {ECO:0000313|EMBL:AHF78603.1};
OS Sodalis praecaptivus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF78603.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF78603.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF78603.1,
RC ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
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}.
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DR EMBL; CP006569; AHF78603.1; -; Genomic_DNA.
DR RefSeq; WP_025423725.1; NZ_CP006569.1.
DR AlphaFoldDB; W0I2E0; -.
DR KEGG; sod:Sant_3621; -.
DR PATRIC; fig|1239307.3.peg.4001; -.
DR HOGENOM; CLU_060296_2_0_6; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000019028; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000019028};
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 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ SEQUENCE 273 AA; 29883 MW; 6D67984BAA25F5C6 CRC64;
MADMHEWVIA FILGVVEGLT EFLPVSSTGH MILVGSLLGF TDDKAKTFEV IIQLGSILAV
VVVFWRRLFG LIGIHFGQVP HEGIGSGRLR LGHILLGMIP AVVLGLVFHE QIKAIFAPQY
VMYALVVGGL LLLAGEWLKP KQPRAAGIDD LTYLQAFLIG CFQCLALWPG FSRSGATISG
GLLVGVSRYA ASEFSFILAV PMMLGATVLD LYKSLPFLAW QDFPMFAIGF VTAFVVALLA
IKFFLQIIKR ISFVPFAIYR FILAAVVYWV LVG
//
