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Protein

Polyketide biosynthesis malonyl CoA-acyl carrier protein transacylase PksC

Gene

pksC

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

Functioni

Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK).2 Publications

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].1 Publication

Pathway: bacillaene biosynthesis

This protein is involved in the pathway bacillaene biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway bacillaene biosynthesis and in Antibiotic biosynthesis.

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU17100-MONOMER.
UniPathwayiUPA01003.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyketide biosynthesis malonyl CoA-acyl carrier protein transacylase PksC (EC:2.3.1.39)
Short name:
AT
Gene namesi
Name:pksC
Ordered Locus Names:BSU17100
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU17100. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Polyketide biosynthesis malonyl CoA-acyl carrier protein transacylase PksCPRO_0000388004Add
BLAST

Proteomic databases

PaxDbiO34825.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009411.

Structurei

3D structure databases

ProteinModelPortaliO34825.
SMRiO34825. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
InParanoidiO34825.
KOiK15327.
OMAiCLENPYS.
OrthoDBiEOG6W19KW.
PhylomeDBiO34825.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.

Sequencei

Sequence statusi: Complete.

O34825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITYVFPGQG SQKQGMGSGL FDEFKELTDQ ADEILGYSIK RLCLENPYSN
60 70 80 90 100
LNKTQFTQPA LYVVNALSYL KKIRDEEVKP DFVAGHSLGE YNALFAAEAF
110 120 130 140 150
DFETGLQLVR KRGELMSLIS NGGMAAVMGL NEEQVAKALK EYHLHDVDIA
160 170 180 190 200
NVNAPYQIVI SGKKDEIEKA ASLFETMTEV TMVLPLNVSG AFHSRYMNKA
210 220 230 240 250
KEEFEEFLHA FYFSPPSIPV ISNVYAKPYT YEFMKQTLAD QINHSVKWTD
260 270 280
SISYLMKKGH MEFEEVGPGN VLTGLIHRIK KDAEAMPR
Length:288
Mass (Da):32,464
Last modified:January 1, 1998 - v1
Checksum:iAFAE397EAB2FD3C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13582.1.
PIRiA69678.
RefSeqiNP_389591.1. NC_000964.3.
WP_003231821.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13582; CAB13582; BSU17100.
GeneIDi939504.
KEGGibsu:BSU17100.
PATRICi18975227. VBIBacSub10457_1805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13582.1.
PIRiA69678.
RefSeqiNP_389591.1. NC_000964.3.
WP_003231821.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO34825.
SMRiO34825. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009411.

Proteomic databases

PaxDbiO34825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13582; CAB13582; BSU17100.
GeneIDi939504.
KEGGibsu:BSU17100.
PATRICi18975227. VBIBacSub10457_1805.

Organism-specific databases

GenoListiBSU17100. [Micado]

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
InParanoidiO34825.
KOiK15327.
OMAiCLENPYS.
OrthoDBiEOG6W19KW.
PhylomeDBiO34825.

Enzyme and pathway databases

UniPathwayiUPA01003.
BioCyciBSUB:BSU17100-MONOMER.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 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. "Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis."
    Calderone C.T., Kowtoniuk W.E., Kelleher N.L., Walsh C.T., Dorrestein P.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:8977-8982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  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 nameiPKSC_BACSU
AccessioniPrimary (citable) accession number: O34825
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: January 1, 1998
Last modified: June 24, 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
  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.