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Protein

Polyketide biosynthesis protein PksE

Gene

pksE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity.1 Publication

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871By similarity
Active sitei193 – 1931By similarity

GO - Molecular functioni

  1. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
  2. nitronate monooxygenase activity Source: InterPro

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU17120-MONOMER.
UniPathwayiUPA01003.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyketide biosynthesis protein PksE
Including the following 1 domains:
Malonyl CoA-acyl carrier protein transacylase (EC:2.3.1.39)
Short name:
MCT
Gene namesi
Name:pksE
Ordered Locus Names:BSU17120
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU17120. [Micado]

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Polyketide biosynthesis protein PksEPRO_0000388002Add
BLAST

Proteomic databases

PaxDbiO34787.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU17120.

Structurei

3D structure databases

ProteinModelPortaliO34787.
SMRiO34787. Positions 1-283, 480-586.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 312312Acyl transferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000275975.
InParanoidiO34787.
KOiK15329.
OMAiGGMYRGI.
OrthoDBiEOG67X1P6.
PhylomeDBiO34787.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
3.40.366.10. 2 hits.
InterProiIPR004136. 2Npropane_dOase.
IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013785. Aldolase_TIM.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR014179. PfaD_fam.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF03060. NMO. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.
TIGR02814. pfaD_fam. 1 hit.

Sequencei

Sequence statusi: Complete.

O34787-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MITYVFPGQG SQQKGMGQGL FEQYQHLTDQ ADQILGYSIE KLCTEKSYLD
60 70 80 90 100
VNHTEYTQPA LYVVNALSYL KRVEETGRKP DFAAGHSLGE YNALMAAGAF
110 120 130 140 150
DFETGLRLVK KRGELMGRIT GGGMAAVIGL SKEQVTAVLE EHRLYDIDVA
160 170 180 190 200
NENTPQQIVI SGPKKEIEKA RAVFENTKDV KLFHPLNVSG AFHSRYMNEA
210 220 230 240 250
KQVFKQYIDS FQFAPLAIPV ISNVYAEPYH QDRLKDTLSE QMDNTVKWTD
260 270 280 290 300
SIRFLMGRGE MEFAEIGPGT VLTGLIHRIK NEAEPLTYIP KKNPAISAHL
310 320 330 340 350
KEQRNVQAGI TAESLGSAEF KQDYHLTYAY LAGGMYRGIA SKEMVVKLSR
360 370 380 390 400
AGMMGFFGTG GLSLKEVEDA IHAIQGELGK GQAYGINLVH NMKHTESEEK
410 420 430 440 450
MIDLLLRNQV SIVEASAFLS VTPVLVRYRA KGVKRNQNGD VICSNRLIAK
460 470 480 490 500
ISRPEVAESF LSPAPENMLQ KLLGENKITM NEAELLRCIP MADDICVEAD
510 520 530 540 550
SGGHTDGGVA YSLMPAMTSL RDEMMKKYQY RKKIRVGAAG GIGTPEAAMA
560 570 580 590 600
AFMLGADFIL TGSINQCTVE AATSDKVKDL LQQMNVQDTA YAPAGDMFES
610 620 630 640 650
GSKVQVLKKG VFFPARANKL YELYQRYGSI RELDAKMLAQ LEEKYFKRSI
660 670 680 690 700
EDIYKDIALH YPAADIEKAE QNPKHKMALI FRWYFRYSSK LAISGSEHSK
710 720 730 740 750
VDYQIHCGPA LGAFNQWVKG SQLENWRNRH VDEIGKKLMT ETAVLLHERM
760
QSMYQPSHET DNIKIKV
Length:767
Mass (Da):85,743
Last modified:May 5, 2009 - v3
Checksum:iC97C8825E3DE8881
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13584.3.
RefSeqiNP_389593.3. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13584; CAB13584; BSU17120.
GeneIDi939997.
KEGGibsu:BSU17120.
PATRICi18975233. VBIBacSub10457_1808.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13584.3.
RefSeqiNP_389593.3. NC_000964.3.

3D structure databases

ProteinModelPortaliO34787.
SMRiO34787. Positions 1-283, 480-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU17120.

Proteomic databases

PaxDbiO34787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13584; CAB13584; BSU17120.
GeneIDi939997.
KEGGibsu:BSU17120.
PATRICi18975233. VBIBacSub10457_1808.

Organism-specific databases

GenoListiBSU17120. [Micado]

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000275975.
InParanoidiO34787.
KOiK15329.
OMAiGGMYRGI.
OrthoDBiEOG67X1P6.
PhylomeDBiO34787.

Enzyme and pathway databases

UniPathwayiUPA01003.
BioCyciBSUB:BSU17120-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
3.40.366.10. 2 hits.
InterProiIPR004136. 2Npropane_dOase.
IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013785. Aldolase_TIM.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR014179. PfaD_fam.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF03060. NMO. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.
TIGR02814. pfaD_fam. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 99-129.
  3. Cited for: SUBCELLULAR LOCATION.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  4. "The identification of bacillaene, the product of the PksX megacomplex in Bacillus subtilis."
    Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R., Walsh C.T., Clardy J.
    Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BACILLAENE BIOSYNTHESIS.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

Entry informationi

Entry nameiPKSE_BACSU
AccessioniPrimary (citable) accession number: O34787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: January 7, 2015
This is version 94 of the entry and version 3 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.