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Reviewed, UniProtKB/Swiss-Prot P24224 (ACPS_ECOLI)

Last modified June 16, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: dpj
Ordered Locus Names: b2563, JW2547
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length126 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein. HAMAP MF_00101

Catalytic activity

CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. HAMAP MF_00101

Cofactor

Magnesium. HAMAP MF_00101

Subunit structure

Homodimer. HAMAP MF_00101

Subcellular location

Cytoplasm Probable.

Sequence similarities

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

Mass spectrometry

Molecular mass is 13950 Da from positions 2 - 126. Determined by ESI. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 126125Holo-[acyl-carrier-protein] synthase HAMAP MF_00101
PRO_0000175643

Sites

Metal binding91Magnesium By similarity
Metal binding581Magnesium By similarity

Experimental info

Mutagenesis51G → D: 5-fold reduction in catalytic activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P24224-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A80628315E69731E

FASTA12614,052
        10         20         30         40         50         60 
MAILGLGTDI VEIARIEAVI ARSGDRLARR VLSDNEWAIW KTHHQPVRFL AKRFAVKEAA 

        70         80         90        100        110        120 
AKAFGTGIRN GLAFNQFEVF NDELGKPRLR LWGEALKLAE KLGVANMHVT LADERHYACA 


TVIIES 

« Hide

References

« Hide 'large scale' references
[1]"Locating essential Escherichia coli genes by using mini-Tn10 transposons: the pdxJ operon."
Takiff H.E., Baker T., Copeland T., Chen S.-M., Court D.L.
J. Bacteriol. 174:1544-1553(1992) [PubMed: 1537799] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Suppression of insertions in the complex pdxJ operon of Escherichia coli K-12 by lon and other mutations."
Lam H.-M., Tancula E., Dempsey W.B., Winkler M.E.
J. Bacteriol. 174:1554-1567(1992) [PubMed: 1537800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]Nashimoto H., Saito N.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase."
Lambalot R.H., Walsh C.T.
J. Biol. Chem. 270:24658-24661(1995) [PubMed: 7559576] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26, CHARACTERIZATION, MASS SPECTROMETRY.
Strain: K12.
[7]"Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli."
Flugel R.S., Hwangbo Y., Lambalot R.H., Cronan J.E. Jr., Walsh C.T.
J. Biol. Chem. 275:959-968(2000) [PubMed: 10625633] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF GLY-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases

M76470 Genomic DNA. Translation: AAA21846.1.
M74526 Genomic DNA. Translation: AAA24316.1.
D64044 Genomic DNA. No translation available.
U36841 Genomic DNA. Translation: AAA79825.1.
U00096 Genomic DNA. Translation: AAC75616.1.
AP009048 Genomic DNA. Translation: BAE76739.1.
PIRB42294.
RefSeqAP_003149.1.
NP_417058.1.

3D structure databases

HSSPHSSP built from PDB template 1F7L based on UniProtKB P96618.
ModBaseSearch...

Genome annotation databases

GeneID947037.
GenomeReviewsGene locus JW2547 in contig AP009048_GR.
Gene locus b2563 in contig U00096_GR.
KEGGecj:JW2547.
eco:b2563.

Organism-specific databases

EchoBASEEB0243.
EcoGeneEG10247. acpS.
CMRSearch...

Phylogenomic databases

HOGENOMP24224.
OMAP24224. MGVVNLP.

Enzyme and pathway databases

BioCycEcoCyc:HOLO-ACP-SYNTH-MON.

Family and domain databases

HAMAPMF_00101.
[Tree]
InterProIPR008278. 4-PPantetheinyl_Trfase.
IPR002582. ACPS.
IPR004568. PPantethiene-prot_Trfase.
[Graphical view]
PfamPF01648. ACPS. 1 hit.
[Graphical view]
ProDomPD004282. ACPS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00516. acpS. 1 hit.
TIGR00556. pantethn_trn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACPS_ECOLI
AccessionPrimary (citable) accession number: P24224
Secondary accession number(s): Q2MAG7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents