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P31114

- HEPS2_BACSU

UniProt

P31114 - HEPS2_BACSU

Protein

Heptaprenyl diphosphate synthase component 2

Gene

hepT

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Supplies heptaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinone menaquinone-7 (MQ-7).1 Publication

    Catalytic activityi

    (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate.

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731Isopentenyl diphosphateBy similarity
    Binding sitei76 – 761Isopentenyl diphosphateBy similarity
    Binding sitei105 – 1051Isopentenyl diphosphateBy similarity
    Metal bindingi112 – 1121Magnesium 1By similarity
    Metal bindingi112 – 1121Magnesium 2By similarity
    Metal bindingi116 – 1161Magnesium 1By similarity
    Metal bindingi116 – 1161Magnesium 2By similarity
    Binding sitei121 – 1211Hexaprenyl diphosphateBy similarity
    Binding sitei122 – 1221Isopentenyl diphosphateBy similarity
    Binding sitei198 – 1981Hexaprenyl diphosphateBy similarity
    Binding sitei199 – 1991Hexaprenyl diphosphateBy similarity
    Binding sitei236 – 2361Hexaprenyl diphosphateBy similarity
    Metal bindingi239 – 2391Magnesium 3By similarity

    GO - Molecular functioni

    1. heptaprenyl diphosphate synthase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. transferase activity, transferring alkyl or aryl (other than methyl) groups Source: UniProtKB

    GO - Biological processi

    1. isoprenoid biosynthetic process Source: UniProtKB-KW
    2. menaquinone biosynthetic process Source: UniProtKB
    3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Isoprene biosynthesis, Sporulation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU22740-MONOMER.
    MetaCyc:MONOMER-13770.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heptaprenyl diphosphate synthase component 2 (EC:2.5.1.30)
    Short name:
    HepPP synthase subunit 2
    Alternative name(s):
    Spore germination protein C3
    Gene namesi
    Name:hepT
    Synonyms:gerC3, gerCC, hepB
    Ordered Locus Names:BSU22740
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU22740. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348Heptaprenyl diphosphate synthase component 2PRO_0000124004Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of component I and II.

    Protein-protein interaction databases

    STRINGi224308.BSU22740.

    Structurei

    3D structure databases

    ProteinModelPortaliP31114.
    SMRiP31114. Positions 34-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPP/GGPP synthase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000009104.
    KOiK00805.
    OMAiFTSTEEE.
    OrthoDBiEOG6TN43W.
    PhylomeDBiP31114.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR014119. GerC3_HepT.
    IPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PANTHERiPTHR12001. PTHR12001. 1 hit.
    PfamiPF00348. polyprenyl_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.
    TIGRFAMsiTIGR02748. GerC3_HepT. 1 hit.
    PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P31114-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNIIRLLAE SLPRISDGNE NTDVWVNDMK FKMAYSFLND DIDVIERELE    50
    QTVRSDYPLL SEAGLHLLQA GGKRIRPVFV LLSGMFGDYD INKIKYVAVT 100
    LEMIHMASLV HDDVIDDAEL RRGKPTIKAK WDNRIAMYTG DYMLAGSLEM 150
    MTRINEPKAH RILSQTIVEV CLGEIEQIKD KYNMEQNLRT YLRRIKRKTA 200
    LLIAVSCQLG AIASGADEKI HKALYWFGYY VGMSYQIIDD ILDFTSTEEE 250
    LGKPVGGDLL QGNVTLPVLY ALKNPALKNQ LKLINSETTQ EQLEPIIEEI 300
    KKTDAIEASM AVSEMYLQKA FQKLNTLPRG RARSSLAAIA KYIGKRKF 348
    Length:348
    Mass (Da):39,516
    Last modified:July 1, 1993 - v1
    Checksum:i0FF9C9199FFE04BE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80245 Genomic DNA. Translation: AAA20856.1.
    AL009126 Genomic DNA. Translation: CAB14190.1.
    PIRiE69630.
    RefSeqiNP_390155.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14190; CAB14190; BSU22740.
    GeneIDi939002.
    KEGGibsu:BSU22740.
    PATRICi18976359. VBIBacSub10457_2370.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80245 Genomic DNA. Translation: AAA20856.1 .
    AL009126 Genomic DNA. Translation: CAB14190.1 .
    PIRi E69630.
    RefSeqi NP_390155.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P31114.
    SMRi P31114. Positions 34-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU22740.

    Protocols and materials databases

    DNASUi 939002.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14190 ; CAB14190 ; BSU22740 .
    GeneIDi 939002.
    KEGGi bsu:BSU22740.
    PATRICi 18976359. VBIBacSub10457_2370.

    Organism-specific databases

    GenoListi BSU22740. [Micado ]

    Phylogenomic databases

    HOGENOMi HOG000009104.
    KOi K00805.
    OMAi FTSTEEE.
    OrthoDBi EOG6TN43W.
    PhylomeDBi P31114.

    Enzyme and pathway databases

    BioCyci BSUB:BSU22740-MONOMER.
    MetaCyc:MONOMER-13770.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR014119. GerC3_HepT.
    IPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    PANTHERi PTHR12001. PTHR12001. 1 hit.
    Pfami PF00348. polyprenyl_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    TIGRFAMsi TIGR02748. GerC3_HepT. 1 hit.
    PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, aro(B,E,F,H), trp(A-F), hisH, and tyrA genes."
      Henner D.J.
      Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Characterization and cloning of the gerC locus of Bacillus subtilis 168."
      Yazdi M.A., Moir A.
      J. Gen. Microbiol. 136:1335-1342(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF GERC LOCUS.
    4. "The gerC locus of Bacillus subtilis, required for menaquinone biosynthesis, is concerned only indirectly with spore germination."
      Leatherbarrow A.J.H., Yazdi M.A., Curson J.P., Moir A.
      Microbiology 144:2125-2130(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiHEPS2_BACSU
    AccessioniPrimary (citable) accession number: P31114
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3