ID   HEPS2_BACSU             Reviewed;         348 AA.
AC   P31114;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Heptaprenyl diphosphate synthase component 2;
DE            Short=HepPP synthase subunit 2;
DE            EC=2.5.1.30;
DE   AltName: Full=Spore germination protein C3;
GN   Name=hepT; Synonyms=gerC3, gerCC, hepB; OrderedLocusNames=BSU22740;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Henner D.J.;
RT   "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR,
RT   aro(B,E,F,H), trp(A-F), hisH, and tyrA genes.";
RL   Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
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).
RN   [3]
RP   CHARACTERIZATION OF GERC LOCUS.
RX   PubMed=2121900; DOI=10.1099/00221287-136-7-1335;
RA   Yazdi M.A., Moir A.;
RT   "Characterization and cloning of the gerC locus of Bacillus subtilis 168.";
RL   J. Gen. Microbiol. 136:1335-1342(1990).
RN   [4]
RP   FUNCTION.
RX   PubMed=9720033; DOI=10.1099/00221287-144-8-2125;
RA   Leatherbarrow A.J.H., Yazdi M.A., Curson J.P., Moir A.;
RT   "The gerC locus of Bacillus subtilis, required for menaquinone
RT   biosynthesis, is concerned only indirectly with spore germination.";
RL   Microbiology 144:2125-2130(1998).
CC   -!- FUNCTION: Supplies heptaprenyl diphosphate, the precursor for the side
CC       chain of the isoprenoid quinone menaquinone-7 (MQ-7).
CC       {ECO:0000269|PubMed:9720033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate =
CC         all-trans-heptaprenyl diphosphate + 4 diphosphate;
CC         Xref=Rhea:RHEA:27794, ChEBI:CHEBI:33019, ChEBI:CHEBI:58206,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.30;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of component I and II.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; M80245; AAA20856.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14190.1; -; Genomic_DNA.
DR   PIR; E69630; E69630.
DR   RefSeq; NP_390155.1; NC_000964.3.
DR   RefSeq; WP_010886555.1; NC_000964.3.
DR   AlphaFoldDB; P31114; -.
DR   SMR; P31114; -.
DR   STRING; 224308.BSU22740; -.
DR   PaxDb; 224308-BSU22740; -.
DR   DNASU; 939002; -.
DR   EnsemblBacteria; CAB14190; CAB14190; BSU_22740.
DR   GeneID; 939002; -.
DR   KEGG; bsu:BSU22740; -.
DR   eggNOG; COG0142; Bacteria.
DR   InParanoid; P31114; -.
DR   OrthoDB; 9805316at2; -.
DR   PhylomeDB; P31114; -.
DR   BioCyc; BSUB:BSU22740-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-13770; -.
DR   BRENDA; 2.5.1.30; 658.
DR   SABIO-RK; P31114; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000010; F:trans-hexaprenyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR014119; GerC3_HepT.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   NCBIfam; TIGR02748; GerC3_HepT; 1.
DR   PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR12001:SF87; OCTAPRENYL DIPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Sporulation; Transferase.
FT   CHAIN           1..348
FT                   /note="Heptaprenyl diphosphate synthase component 2"
FT                   /id="PRO_0000124004"
FT   BINDING         73
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         76
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         105
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         121
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         198
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  39516 MW;  0FF9C9199FFE04BE CRC64;
     MLNIIRLLAE SLPRISDGNE NTDVWVNDMK FKMAYSFLND DIDVIERELE QTVRSDYPLL
     SEAGLHLLQA GGKRIRPVFV LLSGMFGDYD INKIKYVAVT LEMIHMASLV HDDVIDDAEL
     RRGKPTIKAK WDNRIAMYTG DYMLAGSLEM MTRINEPKAH RILSQTIVEV CLGEIEQIKD
     KYNMEQNLRT YLRRIKRKTA LLIAVSCQLG AIASGADEKI HKALYWFGYY VGMSYQIIDD
     ILDFTSTEEE LGKPVGGDLL QGNVTLPVLY ALKNPALKNQ LKLINSETTQ EQLEPIIEEI
     KKTDAIEASM AVSEMYLQKA FQKLNTLPRG RARSSLAAIA KYIGKRKF
//