MENA_BACSU
ID MENA_BACSU Reviewed; 311 AA.
AC P39582;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=ywaB;
GN OrderedLocusNames=BSU38490; ORFNames=ipa-6d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; X73124; CAA51562.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15875.1; -; Genomic_DNA.
DR PIR; S39661; S39661.
DR RefSeq; NP_391728.1; NC_000964.3.
DR RefSeq; WP_009968370.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39582; -.
DR SMR; P39582; -.
DR IntAct; P39582; 1.
DR STRING; 224308.BSU38490; -.
DR PaxDb; P39582; -.
DR PRIDE; P39582; -.
DR EnsemblBacteria; CAB15875; CAB15875; BSU_38490.
DR GeneID; 937356; -.
DR KEGG; bsu:BSU38490; -.
DR PATRIC; fig|224308.179.peg.4166; -.
DR eggNOG; COG1575; Bacteria.
DR InParanoid; P39582; -.
DR OMA; QWIEGAR; -.
DR PhylomeDB; P39582; -.
DR BioCyc; BSUB:BSU38490-MON; -.
DR BioCyc; MetaCyc:MON-13813; -.
DR UniPathway; UPA00079; UER00168.
DR Proteomes; UP000001570; 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:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:0032194; P:ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate; IBA:GO_Central.
DR GO; GO:0042371; P:vitamin K biosynthetic process; IBA:GO_Central.
DR CDD; cd13962; PT_UbiA_UBIAD1; 1.
DR Gene3D; 1.10.357.140; -; 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 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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="1,4-dihydroxy-2-naphthoate octaprenyltransferase"
FT /id="PRO_0000096413"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 182..202
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 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01937"
SQ SEQUENCE 311 AA; 33838 MW; A5880C89AC5E8F55 CRC64;
MNQTNKGEGQ TAPQKESMGQ ILWQLTRPHT LTASFVPVLL GTVLAMFYVK VDLLLFLAML
FSCLWIQIAT NLFNEYYDFK RGLDTAESVG IGGAIVRHGM KPKTILQLAL ASYGIAILLG
VYICASSSWW LALIGLVGMA IGYLYTGGPL PIAYTPFGEL FSGICMGSVF VLISFFIQTD
KINMQSILIS IPIAILVGAI NLSNNIRDIE EDKKGGRKTL AILMGHKGAV TLLAASFAVA
YIWVVGLVIT GAASPWLFVV FLSVPKPVQA VKGFVQNEMP MNMIVAMKST AQTNTFFGFL
LSIGLLISYF R
