ID   MENA_MYCTO              Reviewed;         292 AA.
AC   P9WIP2; L0T6Z2; O06400; P65650;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
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}; OrderedLocusNames=MT0558;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44781.1; -; Genomic_DNA.
DR   PIR; A70546; A70546.
DR   RefSeq; WP_003402865.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIP2; -.
DR   SMR; P9WIP2; -.
DR   EnsemblBacteria; AAK44781; AAK44781; MT0558.
DR   GeneID; 45424498; -.
DR   KEGG; mtc:MT0558; -.
DR   PATRIC; fig|83331.31.peg.589; -.
DR   HOGENOM; CLU_043611_1_0_11; -.
DR   UniPathway; UPA00079; UER00168.
DR   Proteomes; UP000001020; 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_0000427970"
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