ID   MENA_ECOLI              Reviewed;         308 AA.
AC   P32166; Q2M8M6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   04-NOV-2026, entry version 171.
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, ECO:0000269|PubMed:9573170};
GN   Name=menA {ECO:0000255|HAMAP-Rule:MF_01937,
GN   ECO:0000303|PubMed:9573170}; Synonyms=yiiW;
GN   OrderedLocusNames=b3930, JW3901;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=K12;
RX   PubMed=9573170; DOI=10.1128/jb.180.10.2782-2787.1998;
RA   Suvarna K., Stevenson D., Meganathan R., Hudspeth M.E.S.;
RT   "Menaquinone (vitamin K2) biosynthesis: localization and characterization
RT   of the menA gene from Escherichia coli.";
RL   J. Bacteriol. 180:2782-2787(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [3]
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   [4]
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   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
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: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC       demethylmenaquinone (DMK). Attaches octaprenylpyrophosphate, a
CC       membrane-bound 40-carbon side chain to DHNA. The conversion of DHNA to
CC       DMK proceeds in three stages: the removal of the carboxyl group of DHNA
CC       as CO(2), the attachment of the isoprenoid side chain, and a quinol-to-
CC       quinone oxidation, which is thought to be spontaneous.
CC       {ECO:0000269|PubMed:9573170}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an all-trans-polyprenyl diphosphate + 1,4-dihydroxy-2-
CC         naphthoate + 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         ECO:0000269|PubMed:9573170};
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, ECO:0000269|PubMed:9573170}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01937, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000269|PubMed:15919996}.
CC   -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01937, ECO:0000305}.
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DR   EMBL; U56082; AAB01207.1; -; Genomic_DNA.
DR   EMBL; L19201; AAB03062.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76912.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77380.1; -; Genomic_DNA.
DR   PIR; S40873; S40873.
DR   RefSeq; NP_418365.1; NC_000913.3.
DR   RefSeq; WP_000139496.1; NZ_CP009789.1.
DR   AlphaFoldDB; P32166; -.
DR   SMR; P32166; -.
DR   BioGRID; 4261778; 7.
DR   FunCoup; P32166; 474.
DR   STRING; 511145.b3930; -.
DR   PaxDb; 511145-b3930; -.
DR   DNASU; 948418; -.
DR   EnsemblBacteria; AAC76912; AAC76912; b3930.
DR   GeneID; 75169372; -.
DR   GeneID; 75204603; -.
DR   GeneID; 948418; -.
DR   KEGG; ecj:JW3901; -.
DR   KEGG; eco:b3930; -.
DR   KEGG; ecoc:C3026_21240; -.
DR   PATRIC; fig|1411691.4.peg.2775; -.
DR   EchoBASE; EB1826; -.
DR   eggNOG; COG1575; Bacteria.
DR   HOGENOM; CLU_043611_1_1_6; -.
DR   InParanoid; P32166; -.
DR   OMA; AAAFICF; -.
DR   OrthoDB; 9767568at2; -.
DR   PhylomeDB; P32166; -.
DR   BioCyc; EcoCyc:DMK-MONOMER; -.
DR   BioCyc; MetaCyc:DMK-MONOMER; -.
DR   BRENDA; 2.5.1.74; 2026.
DR   UniPathway; UPA00079; UER00168.
DR   PRO; PR:P32166; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P32166; -.
DR   GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate polyprenyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0042371; P:vitamin K biosynthetic process; IBA:GO_Central.
DR   CDD; cd13962; PT_UbiA_UBIAD1; 1.
DR   FunFam; 1.10.357.140:FF:000016; 1,4-dihydroxy-2-naphthoate octaprenyltransferase; 1.
DR   Gene3D; 1.10.357.140; UbiA prenyltransferase; 1.
DR   HAMAP; MF_01937; MenA_1; 1.
DR   InterPro; IPR004657; MenA.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR044878; UbiA_sf.
DR   InterPro; IPR026046; UBIAD1.
DR   NCBIfam; NF004754; menA; 1.
DR   NCBIfam; TIGR00751; menA; 1.
DR   NCBIfam; NF004750; PRK06080.1-2; 1.
DR   NCBIfam; NF004751; PRK06080.1-3; 1.
DR   PANTHER; PTHR13929; 1,4-DIHYDROXY-2-NAPHTHOATE OCTAPRENYLTRANSFERASE; 1.
DR   PANTHER; PTHR13929:SF0; UBIA PRENYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   PIRSF; PIRSF005355; UBIAD1; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Menaquinone biosynthesis;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..308
FT                   /note="1,4-dihydroxy-2-naphthoate octaprenyltransferase"
FT                   /id="PRO_0000096414"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        42
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        64..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        119..123
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        145..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        170..176
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        198..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        228..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        248..250
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        251..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        271..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT   TOPO_DOM        308
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996"
SQ   SEQUENCE   308 AA;  33594 MW;  FECD9E85BAA40E2E CRC64;
     MTEQQISRTQ AWLESLRPKT LPLAFAAIIV GTALAWWQGH FDPLVALLAL ITAGLLQILS
     NLANDYGDAV KGSDKPDRIG PLRGMQKGVI TQQEMKRALI ITVVLICLSG LALVAVACHT
     LADFVGFLIL GGLSIIAAIT YTVGNRPYGY IGLGDISVLV FFGWLSVMGS WYLQAHTLIP
     ALILPATACG LLATAVLNIN NLRDINSDRE NGKNTLVVRL GEVNARRYHA CLLMGSLVCL
     ALFNLFSLHS LWGWLFLLAA PLLVKQARYV MREMDPVAMR PMLERTVKGA LLTNLLFVLG
     IFLSQWAA
//