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Protein

Heptaprenyl diphosphate synthase component 1

Gene

hepS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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.

GO - Molecular functioni

  1. heptaprenyl diphosphate synthase activity Source: UniProtKB-EC
  2. 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

Enzyme and pathway databases

BioCyciBSUB:BSU22760-MONOMER.
MetaCyc:MONOMER-13769.
BRENDAi2.5.1.30. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Heptaprenyl diphosphate synthase component 1 (EC:2.5.1.30)
Short name:
HepPP synthase subunit 1
Alternative name(s):
Spore germination protein C1
Gene namesi
Name:hepS
Synonyms:gerC1, gerCA, hepA
Ordered Locus Names:BSU22760
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU22760. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Heptaprenyl diphosphate synthase component 1PRO_0000124002Add
BLAST

Interactioni

Subunit structurei

Heterodimer of component I and II.

Protein-protein interaction databases

STRINGi224308.BSU22760.

Structurei

3D structure databases

ProteinModelPortaliP31112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000086759.
KOiK00805.
OMAiYIDHCKE.
OrthoDBiEOG6PP9Q3.
PhylomeDBiP31112.

Family and domain databases

InterProiIPR009920. HEPPP_synth_su1.
[Graphical view]
PfamiPF07307. HEPPP_synt_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDIYGTLAN LNTKLKQKLS HPYLAKHISA PKIDEDKLLL FHALFEEADI
60 70 80 90 100
KNNDRENYIV TAMLVQSALD THDEVTTARV IKRDENKNRQ LTVLAGDYFS
110 120 130 140 150
GLYYSLLSEM KDIYMIRTLA TAIKEINEHK IRLYDRSFKD ENDFFESVGI
160 170 180 190 200
VESALFHRVA EHFNLPRWKK LSSDFFVFKR LMNGNDAFLD VIGSFIQLGK
210 220 230 240 250
TKEEILEDCF KKAKNSIESL LPLNSPIQNI LINRLKTISQ DQTYHQKVEE

G
Length:251
Mass (Da):29,122
Last modified:June 30, 1993 - v1
Checksum:i25D9FF1B3BF6F482
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80245 Genomic DNA. Translation: AAA20854.1.
AL009126 Genomic DNA. Translation: CAB14192.1.
PIRiC69630.
RefSeqiNP_390157.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14192; CAB14192; BSU22760.
GeneIDi938998.
KEGGibsu:BSU22760.
PATRICi18976363. VBIBacSub10457_2372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80245 Genomic DNA. Translation: AAA20854.1.
AL009126 Genomic DNA. Translation: CAB14192.1.
PIRiC69630.
RefSeqiNP_390157.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP31112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU22760.

Protocols and materials databases

DNASUi938998.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14192; CAB14192; BSU22760.
GeneIDi938998.
KEGGibsu:BSU22760.
PATRICi18976363. VBIBacSub10457_2372.

Organism-specific databases

GenoListiBSU22760. [Micado]

Phylogenomic databases

HOGENOMiHOG000086759.
KOiK00805.
OMAiYIDHCKE.
OrthoDBiEOG6PP9Q3.
PhylomeDBiP31112.

Enzyme and pathway databases

BioCyciBSUB:BSU22760-MONOMER.
MetaCyc:MONOMER-13769.
BRENDAi2.5.1.30. 658.

Family and domain databases

InterProiIPR009920. HEPPP_synth_su1.
[Graphical view]
PfamiPF07307. HEPPP_synt_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 (DEC-1991) 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(1996) [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(1989) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHEPS1_BACSU
AccessioniPrimary (citable) accession number: P31112
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1993
Last sequence update: June 30, 1993
Last modified: March 31, 2015
This is version 88 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.