ID   HEPS1_BACSU             Reviewed;         251 AA.
AC   P31112;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Heptaprenyl diphosphate synthase component 1;
DE            Short=HepPP synthase subunit 1;
DE            EC=2.5.1.30;
DE   AltName: Full=Spore germination protein C1;
GN   Name=hepS; Synonyms=gerC1, gerCA, hepA; OrderedLocusNames=BSU22760;
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   -!- SUBUNIT: Heterodimer of component I and II.
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DR   EMBL; M80245; AAA20854.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14192.1; -; Genomic_DNA.
DR   PIR; C69630; C69630.
DR   RefSeq; NP_390157.1; NC_000964.3.
DR   RefSeq; WP_004398550.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P31112; -.
DR   SMR; P31112; -.
DR   STRING; 224308.BSU22760; -.
DR   jPOST; P31112; -.
DR   PaxDb; 224308-BSU22760; -.
DR   DNASU; 938998; -.
DR   EnsemblBacteria; CAB14192; CAB14192; BSU_22760.
DR   GeneID; 938998; -.
DR   KEGG; bsu:BSU22760; -.
DR   eggNOG; COG0142; Bacteria.
DR   InParanoid; P31112; -.
DR   OrthoDB; 2417886at2; -.
DR   PhylomeDB; P31112; -.
DR   BioCyc; BSUB:BSU22760-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-13769; -.
DR   BRENDA; 2.5.1.30; 658.
DR   SABIO-RK; P31112; -.
DR   Proteomes; UP000001570; Chromosome.
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; IEA:UniProtKB-KW.
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   Gene3D; 1.20.120.1450; -; 1.
DR   InterPro; IPR009920; HEPPP_synth_su1.
DR   Pfam; PF07307; HEPPP_synt_1; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Reference proteome; Sporulation; Transferase.
FT   CHAIN           1..251
FT                   /note="Heptaprenyl diphosphate synthase component 1"
FT                   /id="PRO_0000124002"
SQ   SEQUENCE   251 AA;  29122 MW;  25D9FF1B3BF6F482 CRC64;
     MQDIYGTLAN LNTKLKQKLS HPYLAKHISA PKIDEDKLLL FHALFEEADI KNNDRENYIV
     TAMLVQSALD THDEVTTARV IKRDENKNRQ LTVLAGDYFS GLYYSLLSEM KDIYMIRTLA
     TAIKEINEHK IRLYDRSFKD ENDFFESVGI VESALFHRVA EHFNLPRWKK LSSDFFVFKR
     LMNGNDAFLD VIGSFIQLGK TKEEILEDCF KKAKNSIESL LPLNSPIQNI LINRLKTISQ
     DQTYHQKVEE G
//