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P96618 (ACPS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Holo-[acyl-carrier-protein] synthase

Short name=Holo-ACP synthase
EC=2.7.8.7
Alternative name(s):
4'-phosphopantetheinyl transferase AcpS
Gene names
Name:acpS
Synonyms:ydcB
Ordered Locus Names:BSU04620
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl carrier protein of secondary metabolism. Ref.3

Catalytic activity

CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. Ref.3

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00101

Subunit structure

Homotrimer. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00101.

Sequence similarities

Belongs to the P-Pant transferase superfamily. AcpS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121121Holo-[acyl-carrier-protein] synthase HAMAP-Rule MF_00101
PRO_0000175613

Sites

Metal binding81Magnesium
Metal binding581Magnesium

Experimental info

Mutagenesis21I → A: 6% of wild-type activity. Ref.4
Mutagenesis51I → R: Loss of activity; no trimer formation. Ref.4
Mutagenesis1131Q → E: 14% of wild-type activity. Ref.4
Mutagenesis1131Q → R: Loss of activity; no trimer formation. Ref.4

Secondary structure

...................... 121
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P96618 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 6C10401DA7116701

FASTA12113,718
        10         20         30         40         50         60 
MIYGIGLDIT ELKRIASMAG RQKRFAERIL TRSELDQYYE LSEKRKNEFL AGRFAAKEAF 

        70         80         90        100        110        120 
SKAFGTGIGR QLSFQDIEIR KDQNGKPYII CTKLSQAAVH VSITHTKEYA AAQVVIERLS 


S 

« Hide

References

« Hide 'large scale' references
[1]"A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome."
Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.
Submitted (MAR-1997) 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]"4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis."
Mootz H.D., Finking R., Marahiel M.A.
J. Biol. Chem. 276:37289-37298(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[4]"Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites."
Parris K.D., Lin L., Tam A., Mathew R., Hixon J., Stahl M., Fritz C.C., Seehra J., Somers W.S.
Structure 8:883-895(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ILE-2; ILE-5 AND GLN-113, X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH COENZYME A AND WITH HOLO-(ACYL-CARRIER-PROTEIN), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB001488 Genomic DNA. Translation: BAA19299.1.
AL009126 Genomic DNA. Translation: CAB12269.1.
PIRH69772.
RefSeqNP_388343.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F7LX-ray1.50A2-121[»]
1F7TX-ray1.80A/B/C/D/E/F2-121[»]
1F80X-ray2.30A/B/C3-121[»]
ProteinModelPortalP96618.
SMRP96618. Positions 2-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP96618. 1 interaction.
STRING224308.BSU04620.

Chemistry

BindingDBP96618.
ChEMBLCHEMBL4734.

Proteomic databases

PaxDbP96618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12269; CAB12269; BSU04620.
GeneID938194.
KEGGbsu:BSU04620.
PATRIC18972508. VBIBacSub10457_0482.

Organism-specific databases

GenoListBSU04620. [Micado]

Phylogenomic databases

eggNOGCOG0736.
HOGENOMHOG000014315.
KOK00997.
OMAVHVSITH.
OrthoDBEOG6384R9.
ProtClustDBPRK00070.

Enzyme and pathway databases

BioCycBSUB:BSU04620-MONOMER.
SABIO-RKP96618.

Family and domain databases

Gene3D3.90.470.20. 1 hit.
HAMAPMF_00101. AcpS.
InterProIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR002582. ACPS.
IPR004568. PPantethiene-prot_Trfase_dom.
[Graphical view]
PfamPF01648. ACPS. 1 hit.
[Graphical view]
ProDomPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56214. SSF56214. 1 hit.
TIGRFAMsTIGR00516. acpS. 1 hit.
TIGR00556. pantethn_trn. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP96618.
PROP96618.

Entry information

Entry nameACPS_BACSU
AccessionPrimary (citable) accession number: P96618
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 110 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

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