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P31114 (HEPS2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heptaprenyl diphosphate synthase component 2

Short name=HepPP synthase subunit 2
EC=2.5.1.30
Alternative name(s):
Spore germination protein C3
Gene names
Name:hepT
Synonyms:gerC3, gerCC, hepB
Ordered Locus Names:BSU22740
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Supplies heptaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinone menaquinone-7 (MQ-7). Ref.4

Catalytic activity

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

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Subunit structure

Heterodimer of component I and II.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Heptaprenyl diphosphate synthase component 2
PRO_0000124004

Sites

Metal binding1121Magnesium 1 By similarity
Metal binding1121Magnesium 2 By similarity
Metal binding1161Magnesium 1 By similarity
Metal binding1161Magnesium 2 By similarity
Metal binding2391Magnesium 3 By similarity
Binding site731Isopentenyl diphosphate By similarity
Binding site761Isopentenyl diphosphate By similarity
Binding site1051Isopentenyl diphosphate By similarity
Binding site1211Hexaprenyl diphosphate By similarity
Binding site1221Isopentenyl diphosphate By similarity
Binding site1981Hexaprenyl diphosphate By similarity
Binding site1991Hexaprenyl diphosphate By similarity
Binding site2361Hexaprenyl diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P31114 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 0FF9C9199FFE04BE

FASTA34839,516
        10         20         30         40         50         60 
MLNIIRLLAE SLPRISDGNE NTDVWVNDMK FKMAYSFLND DIDVIERELE QTVRSDYPLL 

        70         80         90        100        110        120 
SEAGLHLLQA GGKRIRPVFV LLSGMFGDYD INKIKYVAVT LEMIHMASLV HDDVIDDAEL 

       130        140        150        160        170        180 
RRGKPTIKAK WDNRIAMYTG DYMLAGSLEM MTRINEPKAH RILSQTIVEV CLGEIEQIKD 

       190        200        210        220        230        240 
KYNMEQNLRT YLRRIKRKTA LLIAVSCQLG AIASGADEKI HKALYWFGYY VGMSYQIIDD 

       250        260        270        280        290        300 
ILDFTSTEEE LGKPVGGDLL QGNVTLPVLY ALKNPALKNQ LKLINSETTQ EQLEPIIEEI 

       310        320        330        340 
KKTDAIEASM AVSEMYLQKA FQKLNTLPRG RARSSLAAIA KYIGKRKF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80245 Genomic DNA. Translation: AAA20856.1.
AL009126 Genomic DNA. Translation: CAB14190.1.
PIRE69630.
RefSeqNP_390155.1. NC_000964.3.

3D structure databases

ProteinModelPortalP31114.
SMRP31114. Positions 34-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU22740.

Protocols and materials databases

DNASU939002.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14190; CAB14190; BSU22740.
GeneID939002.
KEGGbsu:BSU22740.
PATRIC18976359. VBIBacSub10457_2370.

Organism-specific databases

GenoListBSU22740. [Micado]

Phylogenomic databases

HOGENOMHOG000009104.
KOK00805.
OMAFTSTEEE.
OrthoDBEOG6TN43W.
PhylomeDBP31114.

Enzyme and pathway databases

BioCycBSUB:BSU22740-MONOMER.
MetaCyc:MONOMER-13770.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR014119. GerC3_HepT.
IPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
PANTHERPTHR12001. PTHR12001. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
TIGRFAMsTIGR02748. GerC3_HepT. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEPS2_BACSU
AccessionPrimary (citable) accession number: P31114
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList