HEPS1_BACSU
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 03-AUG-2022, entry version 108.
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; 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 -!- SUBUNIT: Heterodimer of component I and II.
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; 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; P31112; -.
DR PRIDE; P31112; -.
DR DNASU; 938998; -.
DR EnsemblBacteria; CAB14192; CAB14192; BSU_22760.
DR GeneID; 938998; -.
DR KEGG; bsu:BSU22760; -.
DR eggNOG; COG0142; Bacteria.
DR OMA; CDIYGGY; -.
DR PhylomeDB; P31112; -.
DR BioCyc; BSUB:BSU22760-MON; -.
DR BioCyc; MetaCyc:MON-13769; -.
DR BRENDA; 2.5.1.30; 658.
DR SABIO-RK; P31112; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0036422; F:heptaprenyl diphosphate synthase 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 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
