ID   MENA_MYCBO              Reviewed;         292 AA.
AC   P65651; A0A1R3XVR1; O06400; X2BFB9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=1,4-dihydroxy-2-naphthoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01937};
DE            Short=DHNA-octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01937};
DE            EC=2.5.1.74 {ECO:0000255|HAMAP-Rule:MF_01937};
GN   Name=menA {ECO:0000255|HAMAP-Rule:MF_01937};
GN   OrderedLocusNames=BQ2027_MB0548C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC       demethylmenaquinone (DMK). {ECO:0000255|HAMAP-Rule:MF_01937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl
CC         diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate;
CC         Xref=Rhea:RHEA:26478, Rhea:RHEA-COMP:9563, Rhea:RHEA-COMP:9564,
CC         ChEBI:CHEBI:11173, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:55437, ChEBI:CHEBI:58914; EC=2.5.1.74;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01937};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC       menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01937}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01937};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01937}.
CC   -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01937}.
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DR   EMBL; LT708304; SIT99144.1; -; Genomic_DNA.
DR   RefSeq; NP_854209.1; NC_002945.3.
DR   RefSeq; WP_003402865.1; NC_002945.4.
DR   AlphaFoldDB; P65651; -.
DR   SMR; P65651; -.
DR   GeneID; 45424498; -.
DR   PATRIC; fig|233413.5.peg.596; -.
DR   OMA; QWIEGAR; -.
DR   UniPathway; UPA00079; UER00168.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate octaprenyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13962; PT_UbiA_UBIAD1; 1.
DR   HAMAP; MF_01937; MenA_1; 1.
DR   InterPro; IPR004657; MenA.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR026046; UBIAD1.
DR   PANTHER; PTHR13929; PTHR13929; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   PIRSF; PIRSF005355; UBIAD1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Menaquinone biosynthesis; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..292
FT                   /note="1,4-dihydroxy-2-naphthoate octaprenyltransferase"
FT                   /id="PRO_0000096416"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
SQ   SEQUENCE   292 AA;  30014 MW;  FF73431AB309D817 CRC64;
     MASFAQWVSG ARPRTLPNAI APVVAGTGAA AWLHAAVWWK ALLALAVAVA LVIGVNYAND
     YSDGIRGTDD DRVGPVRLVG SRLATPRSVL TAAMTSLALG ALAGLVLALL SAPWLIAVGA
     ICIAGAWLYT GGSKPYGYAG FGELAVFVFF GPVAVLGTQY TQALRVDWVG LAQAVATGAL
     SCSVLVANNL RDIPTDARAD KITLAVRLGD ARTRMLYQGL LAVAGVLTFV LMLATPWCVV
     GLVAAPLALR AAGPVRSGRG GRELIPVLRD TGLAMLVWAL AVAGALAFGQ LS