ID   B1LNN5_ECOSM            Unreviewed;       312 AA.
AC   B1LNN5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=1,4-dihydroxy-2-naphthoate octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01937};
DE            Short=DHNA-octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01937};
DE            EC=2.5.1.74 {ECO:0000256|HAMAP-Rule:MF_01937};
GN   Name=menA {ECO:0000256|HAMAP-Rule:MF_01937,
GN   ECO:0000313|EMBL:ACB18241.1};
GN   OrderedLocusNames=EcSMS35_4372 {ECO:0000313|EMBL:ACB18241.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB18241.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB18241.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to
CC       demethylmenaquinone (DMK). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01937};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC       menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01937}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01937}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01937}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01937}.
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DR   EMBL; CP000970; ACB18241.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1LNN5; -.
DR   KEGG; ecm:EcSMS35_4372; -.
DR   HOGENOM; CLU_043611_1_1_6; -.
DR   UniPathway; UPA00079; UER00168.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   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; TIGR00751; menA; 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   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01937};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01937};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01937};
KW   Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW   Rule:MF_01937};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01937, ECO:0000313|EMBL:ACB18241.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01937};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01937}.
FT   TRANSMEM        24..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        48..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        128..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        154..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        232..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        256..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
FT   TRANSMEM        294..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01937"
SQ   SEQUENCE   312 AA;  34008 MW;  4F381C518D026A55 CRC64;
     MARIMTEQQI SRTQAWLESL RPKTLPLAFA AIIVGTALAW WQGHFDPLVA LLALITAGLL
     QILSNLANDY GDAVKGSDKP DRIGPLRGMQ KGVITQQEMK RALIITVVLI CLSGLALVAV
     ACHTLADFVG FLILGGLSII AAITYTVGNR PYGYIGLGDI SVLVFFGWLS VMGSWYLQAH
     TLIPALILPA TACGLLATAV LNINNLRDIN SDRENGKNTL VVRLGAVNAR RYHACLLMGS
     LVCLALFNLF SLHSLWGWLF LLAAPLLVKQ ARYVMREMDP VAMRPMLERT VKGALLTNLL
     FVLGIFLSQW AA
//