UPPP_ECOLI
ID UPPP_ECOLI Reviewed; 273 AA.
AC P60932; P31054; P39203; Q2M9E8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Undecaprenyl-diphosphatase;
DE EC=3.6.1.27;
DE AltName: Full=Bacitracin resistance protein;
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase;
GN Name=uppP; Synonyms=bacA, upk; OrderedLocusNames=b3057, JW3029;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157, AND RESISTANCE TO BACITRACIN.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=8389741; DOI=10.1128/jb.175.12.3784-3789.1993;
RA Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M.;
RT "Amplification of the bacA gene confers bacitracin resistance to
RT Escherichia coli.";
RL J. Bacteriol. 175:3784-3789(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-273.
RX PubMed=3009457; DOI=10.1016/s0021-9258(19)84582-9;
RA Cudny H., Lupski J.R., Godson G.N., Deutscher M.P.;
RT "Cloning, sequencing, and species relatedness of the Escherichia coli cca
RT gene encoding the enzyme tRNA nucleotidyltransferase.";
RL J. Biol. Chem. 261:6444-6449(1986).
RN [5]
RP PRELIMINARY CONCEPTUAL TRANSLATION.
RA Rudd K.E.;
RL Unpublished observations (NOV-1994).
RN [6]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=15138271; DOI=10.1074/jbc.m401701200;
RA El Ghachi M., Bouhss A., Blanot D., Mengin-Lecreulx D.;
RT "The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate
RT phosphatase activity.";
RL J. Biol. Chem. 279:30106-30113(2004).
RN [7]
RP FUNCTION.
RX PubMed=15778224; DOI=10.1074/jbc.m412277200;
RA El Ghachi M., Derbise A., Bouhss A., Mengin-Lecreulx D.;
RT "Identification of multiple genes encoding membrane proteins with
RT undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia
RT coli.";
RL J. Biol. Chem. 280:18689-18695(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC (UPP). Confers resistance to bacitracin. {ECO:0000269|PubMed:15778224}.
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:0000269|PubMed:15138271};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15138271,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15138271, ECO:0000269|PubMed:15919996}.
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 -!- SIMILARITY: Belongs to the UppP family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an undecaprenol kinase.
CC {ECO:0000305|PubMed:8389741}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L12966; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M12788; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U28379; AAA89137.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76093.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77108.1; -; Genomic_DNA.
DR EMBL; L12966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M12788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G65093; G65093.
DR RefSeq; NP_417529.1; NC_000913.3.
DR RefSeq; WP_001281927.1; NZ_LN832404.1.
DR PDB; 6CB2; X-ray; 2.00 A; A=1-273.
DR PDBsum; 6CB2; -.
DR AlphaFoldDB; P60932; -.
DR SMR; P60932; -.
DR BioGRID; 4261190; 288.
DR DIP; DIP-48044N; -.
DR IntAct; P60932; 1.
DR STRING; 511145.b3057; -.
DR BindingDB; P60932; -.
DR ChEMBL; CHEMBL4295581; -.
DR SwissLipids; SLP:000001810; -.
DR jPOST; P60932; -.
DR PaxDb; P60932; -.
DR PRIDE; P60932; -.
DR EnsemblBacteria; AAC76093; AAC76093; b3057.
DR EnsemblBacteria; BAE77108; BAE77108; BAE77108.
DR GeneID; 947551; -.
DR KEGG; ecj:JW3029; -.
DR KEGG; eco:b3057; -.
DR PATRIC; fig|1411691.4.peg.3674; -.
DR EchoBASE; EB1616; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_6; -.
DR InParanoid; P60932; -.
DR OMA; IEGPFRD; -.
DR PhylomeDB; P60932; -.
DR BioCyc; EcoCyc:EG11665-MON; -.
DR BioCyc; MetaCyc:EG11665-MON; -.
DR BRENDA; 3.6.1.27; 2026.
DR PRO; PR:P60932; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016462; F:pyrophosphatase activity; IDA:EcoCyc.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IDA:EcoliWiki.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IDA:EcoCyc.
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; IDA:EcoCyc.
DR HAMAP; MF_01006; Undec_diphosphatase; 1.
DR InterPro; IPR003824; UppP.
DR PANTHER; PTHR30622; PTHR30622; 1.
DR Pfam; PF02673; BacA; 1.
DR TIGRFAMs; TIGR00753; undec_PP_bacA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Cell shape; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..273
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000151146"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 158
FT /note="F -> I (in Ref. 4)"
FT /evidence="ECO:0000305"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:6CB2"
FT TURN 21..25
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 43..63
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:6CB2"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 119..139
FT /evidence="ECO:0007829|PDB:6CB2"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 189..214
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 224..248
FT /evidence="ECO:0007829|PDB:6CB2"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6CB2"
FT HELIX 255..272
FT /evidence="ECO:0007829|PDB:6CB2"
SQ SEQUENCE 273 AA; 29759 MW; 6BFAC099D5163352 CRC64;
MSDMHSLLIA AILGVVEGLT EFLPVSSTGH MIIVGHLLGF EGDTAKTFEV VIQLGSILAV
VVMFWRRLFG LIGIHFGRPL QHEGESKGRL TLIHILLGMI PAVVLGLLFH DTIKSLFNPI
NVMYALVVGG LLLIAAECLK PKEPRAPGLD DMTYRQAFMI GCFQCLALWP GFSRSGATIS
GGMLMGVSRY AASEFSFLLA VPMMMGATAL DLYKSWGFLT SGDIPMFAVG FITAFVVALI
AIKTFLQLIK RISFIPFAIY RFIVAAAVYV VFF
