ID   UBIA_ECOBW              Reviewed;         290 AA.
AC   C5A133;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635};
DE            EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_01635};
DE   AltName: Full=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635};
GN   Name=ubiA {ECO:0000255|HAMAP-Rule:MF_01635}; OrderedLocusNames=BWG_3753;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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       {ECO:0000255|HAMAP-Rule:MF_01635}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01635};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01635}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01635}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01635}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01635}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001396; ACR64065.1; -; Genomic_DNA.
DR   RefSeq; WP_000455227.1; NC_012759.1.
DR   AlphaFoldDB; C5A133; -.
DR   SMR; C5A133; -.
DR   KEGG; ebw:BWG_3753; -.
DR   HOGENOM; CLU_034879_1_0_6; -.
DR   OMA; MVVYPYG; -.
DR   UniPathway; UPA00232; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Magnesium; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT   CHAIN           1..290
FT                   /note="4-hydroxybenzoate octaprenyltransferase"
FT                   /id="PRO_1000215802"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
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   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
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