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   27-MAR-2024, entry version 148.
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; Pseudomonadota; 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RL   Unpublished observations (NOV-1994).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; 5OON; X-ray; 2.60 A; A=1-273.
DR   PDB; 6CB2; X-ray; 2.00 A; A=1-273.
DR   PDB; 6FMT; X-ray; 3.00 A; A=1-273.
DR   PDB; 6FMV; X-ray; 2.30 A; A=1-273.
DR   PDB; 6FMW; X-ray; 2.60 A; A=1-273.
DR   PDBsum; 5OON; -.
DR   PDBsum; 6CB2; -.
DR   PDBsum; 6FMT; -.
DR   PDBsum; 6FMV; -.
DR   PDBsum; 6FMW; -.
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; 511145-b3057; -.
DR   EnsemblBacteria; AAC76093; AAC76093; b3057.
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; AWYRIVF; -.
DR   OrthoDB; 9808289at2; -.
DR   PhylomeDB; P60932; -.
DR   BioCyc; EcoCyc:EG11665-MONOMER; -.
DR   BioCyc; MetaCyc:EG11665-MONOMER; -.
DR   BRENDA; 3.6.1.27; 2026.
DR   PRO; PR:P60932; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
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   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   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           5..20
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   TURN            21..24
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           43..63
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           65..71
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           92..115
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           119..139
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           154..164
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           174..184
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           189..214
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   TURN            215..218
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           221..223
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           224..248
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:6FMV"
FT   HELIX           255..272
FT                   /evidence="ECO:0007829|PDB:6FMV"
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
//