Reviewed, UniProtKB/Swiss-Prot P0A2W6 (ACPS_STRPN)

Names and origin

Protein names

Recommended 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
Ordered Locus Names:	SP_1699

Organism

Streptococcus pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

1313 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	120 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein By similarity.
Catalytic activity	CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. HAMAP MF_00101
Cofactor	Magnesium By similarity.
Subunit structure	Homotrimer. HAMAP MF_00101
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the P-Pant transferase superfamily. AcpS family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP macromolecule biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	holo-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 120

120

Holo-[acyl-carrier-protein] synthase HAMAP MF_00101

PRO_0000175713

Sites

Metal binding

8

1

Magnesium By similarity

Metal binding

58

1

Magnesium By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

120

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Helix

12 – 21

10

Helix

25 – 29

5

Helix

32 – 39

8

Helix

43 – 63

21

Helix

73 – 75

3

Beta strand

77 – 80

4

Beta strand

86 – 90

5

Beta strand

95 – 103

9

Beta strand

105 – 115

11

Sequences

	Sequence		Length	Mass (Da)
	P0A2W6-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 7FFB1848AC63DAEE	FASTA	120	13,388
	10 20 30 40 50 60 MIVGHGIDIE ELASIESAVT RHEGFAKRVL TAQEMERFTS LKGRRQIEYL AGRWSAKEAF 70 80 90 100 110 120 SKAMGTGISK LGFQDLEVLN NERGAPYFSQ APFSGKIWLS ISHTDQFVTA SVILEENHES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M. Science 293:498-506(2001) [PubMed: 11463916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4.
[2]	"Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis." Chirgadze N.Y., Briggs S.L., McAllister K.A., Fischl A.S., Zhao G. EMBO J. 19:5281-5287(2000) [PubMed: 11032795] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH 3'-5'-ADP.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE005672 Genomic DNA. Translation: AAK75777.1.

PIR

H95197.

RefSeq

NP_346137.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FTE	X-ray	2.40	A/B/C	1-120	[»]
1FTF	X-ray	2.05	A/B/C	1-120	[»]
1FTH	X-ray	1.90	A/B/C	1-120	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A2W6. 6 interactions.

Genome annotation databases

GeneID

931136.

GenomeReviews

Gene locus SP_1699 in contig AE005672_GR.

KEGG

spn:SP_1699.

TIGR

SP_1699.

Phylogenomic databases

HOGENOM

P0A2W6.

OMA

VHVSITH.

Enzyme and pathway databases

BRENDA

2.7.8.7. 600.

Family and domain databases

HAMAP

MF_00101.
[Tree]

InterPro

IPR008278. 4-PPantetheinyl_Trfase.
IPR002582. ACPS.
IPR004568. PPantethiene-prot_Trfase.
[Graphical view]

Pfam

PF01648. ACPS. 1 hit.
[Graphical view]

ProDom

PD004282. ACPS. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00516. acpS. 1 hit.
TIGR00556. pantethn_trn. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ACPS_STRPN

Accession

Primary (citable) accession number: P0A2W6
Secondary accession number(s): Q9F7T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)