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Protein

Holo-[acyl-carrier-protein] synthase

Gene

acpS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].1 PublicationUniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Magnesium
Metal bindingi58 – 581Magnesium

GO - Molecular functioni

  1. holo-[acyl-carrier-protein] synthase activity Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-HAMAP
  2. macromolecule biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU04620-MONOMER.
SABIO-RKP96618.

Names & Taxonomyi

Protein namesi
Recommended name:
Holo-[acyl-carrier-protein] synthaseUniRule annotation (EC:2.7.8.7UniRule annotation)
Short name:
Holo-ACP synthaseUniRule annotation
Alternative name(s):
4'-phosphopantetheinyl transferase AcpSUniRule annotation
Gene namesi
Name:acpSUniRule annotation
Synonyms:ydcB
Ordered Locus Names:BSU04620
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU04620. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21I → A: 6% of wild-type activity. 1 Publication
Mutagenesisi5 – 51I → R: Loss of activity; no trimer formation. 1 Publication
Mutagenesisi113 – 1131Q → E: 14% of wild-type activity. 1 Publication
Mutagenesisi113 – 1131Q → R: Loss of activity; no trimer formation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121Holo-[acyl-carrier-protein] synthasePRO_0000175613Add
BLAST

Proteomic databases

PaxDbiP96618.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

IntActiP96618. 1 interaction.
STRINGi224308.BSU04620.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Helixi12 – 2110Combined sources
Helixi25 – 295Combined sources
Helixi32 – 387Combined sources
Helixi43 – 6321Combined sources
Beta strandi68 – 714Combined sources
Helixi74 – 763Combined sources
Beta strandi78 – 814Combined sources
Beta strandi87 – 915Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 10511Combined sources
Beta strandi107 – 11711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F7LX-ray1.50A1-121[»]
1F7TX-ray1.80A/B/C/D/E/F2-121[»]
1F80X-ray2.30A/B/C2-121[»]
ProteinModelPortaliP96618.
SMRiP96618. Positions 2-119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96618.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0736.
HOGENOMiHOG000014315.
InParanoidiP96618.
KOiK00997.
OMAiWISISHS.
OrthoDBiEOG6384R9.
PhylomeDBiP96618.

Family and domain databases

Gene3Di3.90.470.20. 1 hit.
HAMAPiMF_00101. AcpS.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR002582. ACPS.
IPR004568. Ppantetheine-prot_Trfase_dom.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
[Graphical view]
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56214. SSF56214. 1 hit.
TIGRFAMsiTIGR00516. acpS. 1 hit.
TIGR00556. pantethn_trn. 1 hit.

Sequencei

Sequence statusi: Complete.

P96618-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIYGIGLDIT ELKRIASMAG RQKRFAERIL TRSELDQYYE LSEKRKNEFL
60 70 80 90 100
AGRFAAKEAF SKAFGTGIGR QLSFQDIEIR KDQNGKPYII CTKLSQAAVH
110 120
VSITHTKEYA AAQVVIERLS S
Length:121
Mass (Da):13,718
Last modified:May 1, 1997 - v1
Checksum:i6C10401DA7116701
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19299.1.
AL009126 Genomic DNA. Translation: CAB12269.1.
PIRiH69772.
RefSeqiNP_388343.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12269; CAB12269; BSU04620.
GeneIDi938194.
KEGGibsu:BSU04620.
PATRICi18972508. VBIBacSub10457_0482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19299.1.
AL009126 Genomic DNA. Translation: CAB12269.1.
PIRiH69772.
RefSeqiNP_388343.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F7LX-ray1.50A1-121[»]
1F7TX-ray1.80A/B/C/D/E/F2-121[»]
1F80X-ray2.30A/B/C2-121[»]
ProteinModelPortaliP96618.
SMRiP96618. Positions 2-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP96618. 1 interaction.
STRINGi224308.BSU04620.

Chemistry

BindingDBiP96618.
ChEMBLiCHEMBL4734.

Proteomic databases

PaxDbiP96618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12269; CAB12269; BSU04620.
GeneIDi938194.
KEGGibsu:BSU04620.
PATRICi18972508. VBIBacSub10457_0482.

Organism-specific databases

GenoListiBSU04620. [Micado]

Phylogenomic databases

eggNOGiCOG0736.
HOGENOMiHOG000014315.
InParanoidiP96618.
KOiK00997.
OMAiWISISHS.
OrthoDBiEOG6384R9.
PhylomeDBiP96618.

Enzyme and pathway databases

BioCyciBSUB:BSU04620-MONOMER.
SABIO-RKP96618.

Miscellaneous databases

EvolutionaryTraceiP96618.
PROiP96618.

Family and domain databases

Gene3Di3.90.470.20. 1 hit.
HAMAPiMF_00101. AcpS.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR002582. ACPS.
IPR004568. Ppantetheine-prot_Trfase_dom.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
[Graphical view]
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56214. SSF56214. 1 hit.
TIGRFAMsiTIGR00516. acpS. 1 hit.
TIGR00556. pantethn_trn. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACPS_BACSU
AccessioniPrimary (citable) accession number: P96618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: January 7, 2015
This is version 116 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.