UBIA_ECOLI
ID UBIA_ECOLI Reviewed; 290 AA.
AC P0AGK1; P26601; Q2M6R4; Q4JHR7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000303|PubMed:4552989};
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:4552989};
DE AltName: Full=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000303|PubMed:8155731};
DE AltName: Full=PHB octaprenyl transferase {ECO:0000303|PubMed:1644192};
GN Name=ubiA {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000303|PubMed:4552989};
GN Synonyms=cyr; OrderedLocusNames=b4040, JW4000;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1644758; DOI=10.1128/jb.174.16.5309-5316.1992;
RA Nichols B.P., Green J.M.;
RT "Cloning and sequencing of Escherichia coli ubiC and purification of
RT chorismate lyase.";
RL J. Bacteriol. 174:5309-5316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=1644192; DOI=10.1016/0014-5793(92)80710-x;
RA Siebert M., Bechthold A., Melzer M., May U., Berger U., Schroeder G.,
RA Schroeder J., Severin K., Heide L.;
RT "Ubiquinone biosynthesis. Cloning of the genes coding for chorismate
RT pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from
RT Escherichia coli.";
RL FEBS Lett. 307:347-350(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1512213; DOI=10.1128/jb.174.17.5762.1992;
RA Nishimura K., Nakahigashi K., Inokuchi H.;
RT "Location of the ubiA gene on the physical map of Escherichia coli.";
RL J. Bacteriol. 174:5762-5762(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Wolter F.P.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL21;
RA Zhang D., Shrestha B., Tan T.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC STRAIN=K12;
RX PubMed=8409922; DOI=10.1099/00221287-139-8-1795;
RA Wu G., Williams H.D., Gibson F., Poole R.K.;
RT "Mutants of Escherichia coli affected in respiration: the cloning and
RT nucleotide sequence of ubiA, encoding the membrane-bound p-
RT hydroxybenzoate:octaprenyltransferase.";
RL J. Gen. Microbiol. 139:1795-1805(1993).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=4552989; DOI=10.1128/jb.110.1.18-25.1972;
RA Young I.G., Leppik R.A., Hamilton J.A., Gibson F.;
RT "Biochemical and genetic studies on ubiquinone biosynthesis in Escherichia
RT coli K-12:4-hydroxybenzoate octaprenyltransferase.";
RL J. Bacteriol. 110:18-25(1972).
RN [11]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8155731; DOI=10.1016/0005-2760(94)90193-7;
RA Melzer M., Heide L.;
RT "Characterization of polyprenyldiphosphate:4-hydroxybenzoate
RT polyprenyltransferase from Escherichia coli.";
RL Biochim. Biophys. Acta 1212:93-102(1994).
RN [12]
RP INDUCTION.
RX PubMed=7765507; DOI=10.1271/bbb.58.1814;
RA Suzuki K., Ueda M., Yuasa M., Nakagawa T., Kawamukai M., Matsuda H.;
RT "Evidence that Escherichia coli ubiA product is a functional homolog of
RT yeast COQ2, and the regulation of ubiA gene expression.";
RL Biosci. Biotechnol. Biochem. 58:1814-1819(1994).
RN [13]
RP POSSIBLE GENETIC INTERACTION WITH DNAG.
RX PubMed=9093842; DOI=10.1093/genetics/145.4.867;
RA Britton R.A., Lupski J.R.;
RT "Isolation and characterization of suppressors of two Escherichia coli dnaG
RT mutations, dnaG2903 and parB.";
RL Genetics 145:867-875(1997).
RN [14]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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 prenylation of para-hydroxybenzoate (PHB) with
CC an all-trans polyprenyl group. Mediates the second step in the final
CC reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the
CC condensation of the polyisoprenoid side chain with PHB, generating the
CC first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate
CC (PubMed:4552989). Geranyldiphosphate (GPP), all-trans-
CC farnesyldiphosphate (FPP) and all-trans-solanesyldiphosphate (SPP) are
CC also accepted as side chain precursors (PubMed:8155731).
CC {ECO:0000269|PubMed:4552989, ECO:0000269|PubMed:8155731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-octaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:27782, ChEBI:CHEBI:1617, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57711; EC=2.5.1.39;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635,
CC ECO:0000269|PubMed:4552989};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635,
CC ECO:0000269|PubMed:4552989, ECO:0000269|PubMed:8155731};
CC Note=Can also use Mn(2+) and Co(2+) with lower efficiency.
CC {ECO:0000269|PubMed:8155731};
CC -!- ACTIVITY REGULATION: The reaction is stimulated by 0.01% CHAPS, but
CC strongly inhibited by sodiumdeoxycholate, Tween 80 and Triton X-100.
CC {ECO:0000269|PubMed:8155731}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=255 uM for GPP {ECO:0000269|PubMed:8155731};
CC KM=22 uM for FPP {ECO:0000269|PubMed:8155731};
CC KM=31 uM for SPP {ECO:0000269|PubMed:8155731};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:8155731};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:4552989}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01635, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:4552989,
CC ECO:0000269|PubMed:8155731}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01635}.
CC -!- INDUCTION: Expression is slightly repressed by glucose.
CC {ECO:0000269|PubMed:7765507}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to convert 4-hydroxybenzoate
CC into 3-octaprenyl-4-hydroxybenzoate and is ubiquinone-deficient.
CC {ECO:0000269|PubMed:4552989}.
CC -!- MISCELLANEOUS: The sdgG mutation, which suppresses a conditional
CC mutation in dnaG (DNA primase), has been localized to one of the ubiA,
CC ubiC or yjbI genes. {ECO:0000305|PubMed:9093842}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000305}.
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DR EMBL; M93136; AAA24712.1; -; Genomic_DNA.
DR EMBL; M93413; AAA24717.1; -; Genomic_DNA.
DR EMBL; X66619; CAA47182.1; -; Genomic_DNA.
DR EMBL; X57434; CAA40682.1; -; Genomic_DNA.
DR EMBL; X69522; CAA49270.1; -; Genomic_DNA.
DR EMBL; DQ087228; AAY88960.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43134.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77010.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78042.1; -; Genomic_DNA.
DR EMBL; M96268; AAA17028.1; -; Unassigned_DNA.
DR EMBL; X63407; CAA45003.1; -; Genomic_DNA.
DR PIR; JC2316; JC2316.
DR RefSeq; NP_418464.1; NC_000913.3.
DR RefSeq; WP_000455227.1; NZ_SSZK01000016.1.
DR AlphaFoldDB; P0AGK1; -.
DR SMR; P0AGK1; -.
DR BioGRID; 4259714; 333.
DR STRING; 511145.b4040; -.
DR jPOST; P0AGK1; -.
DR PaxDb; P0AGK1; -.
DR PRIDE; P0AGK1; -.
DR EnsemblBacteria; AAC77010; AAC77010; b4040.
DR EnsemblBacteria; BAE78042; BAE78042; BAE78042.
DR GeneID; 948540; -.
DR KEGG; ecj:JW4000; -.
DR KEGG; eco:b4040; -.
DR PATRIC; fig|1411691.4.peg.2668; -.
DR EchoBASE; EB1344; -.
DR eggNOG; COG0382; Bacteria.
DR HOGENOM; CLU_034879_1_0_6; -.
DR InParanoid; P0AGK1; -.
DR OMA; MVVYPYG; -.
DR PhylomeDB; P0AGK1; -.
DR BioCyc; EcoCyc:4OHBENZOATE-OCTAPRENYLTRANSFER-MON; -.
DR BioCyc; MetaCyc:4OHBENZOATE-OCTAPRENYLTRANSFER-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:P0AGK1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:EcoCyc.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Magnesium; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT CHAIN 1..290
FT /note="4-hydroxybenzoate octaprenyltransferase"
FT /id="PRO_0000162890"
FT TOPO_DOM 1..22
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 44..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 67..99
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 120..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 162
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 184..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 255..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TOPO_DOM 289..290
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 290 AA; 32512 MW; F10FED1D7A30E115 CRC64;
MEWSLTQNKL LAFHRLMRTD KPIGALLLLW PTLWALWVAT PGVPQLWILA VFVAGVWLMR
AAGCVVNDYA DRKFDGHVKR TANRPLPSGA VTEKEARALF VVLVLISFLL VLTLNTMTIL
LSIAALALAW VYPFMKRYTH LPQVVLGAAF GWSIPMAFAA VSESVPLSCW LMFLANILWA
VAYDTQYAMV DRDDDVKIGI KSTAILFGQY DKLIIGILQI GVLALMAIIG ELNGLGWGYY
WSILVAGALF VYQQKLIANR EREACFKAFM NNNYVGLVLF LGLAMSYWHF
