ID   UBIA_COXBN              Reviewed;         287 AA.
AC   A9KGW7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=CBUD_2048;
OS   Coxiella burnetii (strain Dugway 5J108-111).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dugway 5J108-111;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(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}.
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DR   EMBL; CP000733; ABS76725.1; -; Genomic_DNA.
DR   RefSeq; WP_005772835.1; NC_009727.1.
DR   AlphaFoldDB; A9KGW7; -.
DR   SMR; A9KGW7; -.
DR   EnsemblBacteria; ABS76725; ABS76725; CBUD_2048.
DR   KEGG; cbd:CBUD_2048; -.
DR   HOGENOM; CLU_034879_1_0_6; -.
DR   OMA; MVVYPYG; -.
DR   OrthoDB; 1472516at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008555; Chromosome.
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..287
FT                   /note="4-hydroxybenzoate octaprenyltransferase"
FT                   /id="PRO_1000088171"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ   SEQUENCE   287 AA;  32738 MW;  60CF7C03E73D1C45 CRC64;
     MINLRQQMPH YLRLMRFDKP VGIFLLLWPT LWAVWIAAKG APSFKIAVIF IAGSVVMRAA
     GCIVNDFADR HLDKHVQRTQ MRPLASGSVS VTEAMLLFAV LSLIAFTLVL LLNRLTVELA
     VIGILLALVY PFLKRFTHLP QLWLGVAFSW SIPMAFAATV GHVPAVAWLL FFAAVLWPIV
     YDTQYAMIDR EDDVKVGIKS TAILFGRYDR LMIGLLQGSV LLTFGLLGWY LRFNYWFYLG
     LLVALGLMCY QQFLIRHRKP PDCFAAFRNN NWVGFFIFLG ILLTYRN