HEPS2_BACSU
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 03-AUG-2022, entry version 131.
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; Firmicutes; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P31114; -.
DR PRIDE; P31114; -.
DR DNASU; 939002; -.
DR EnsemblBacteria; CAB14190; CAB14190; BSU_22740.
DR GeneID; 939002; -.
DR KEGG; bsu:BSU22740; -.
DR eggNOG; COG0142; Bacteria.
DR InParanoid; P31114; -.
DR OMA; GKQMRPM; -.
DR PhylomeDB; P31114; -.
DR BioCyc; BSUB:BSU22740-MON; -.
DR BioCyc; MetaCyc:MON-13770; -.
DR BRENDA; 2.5.1.30; 658.
DR SABIO-RK; P31114; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0036422; F:heptaprenyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
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; -; 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 Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR02748; GerC3_HepT; 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
