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P31114

- HEPS2_BACSU

UniProt

P31114 - HEPS2_BACSU

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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

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
Complete GO annotation...

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.
InParanoidiP31114.
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

        10         20         30         40         50
MLNIIRLLAE SLPRISDGNE NTDVWVNDMK FKMAYSFLND DIDVIERELE
60 70 80 90 100
QTVRSDYPLL SEAGLHLLQA GGKRIRPVFV LLSGMFGDYD INKIKYVAVT
110 120 130 140 150
LEMIHMASLV HDDVIDDAEL RRGKPTIKAK WDNRIAMYTG DYMLAGSLEM
160 170 180 190 200
MTRINEPKAH RILSQTIVEV CLGEIEQIKD KYNMEQNLRT YLRRIKRKTA
210 220 230 240 250
LLIAVSCQLG AIASGADEKI HKALYWFGYY VGMSYQIIDD ILDFTSTEEE
260 270 280 290 300
LGKPVGGDLL QGNVTLPVLY ALKNPALKNQ LKLINSETTQ EQLEPIIEEI
310 320 330 340
KKTDAIEASM AVSEMYLQKA FQKLNTLPRG RARSSLAAIA KYIGKRKF
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.
WP_010886555.1. 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.
WP_010886555.1. 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.
InParanoidi P31114.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 102 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