O86785 (ACPS_STRCO) Reviewed, UniProtKB/Swiss-Prot

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:	SCO4744
ORF Names:	SC6G4.22c

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	123 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00101
Catalytic activity	CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]. HAMAP-Rule MF_00101
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the P-Pant transferase superfamily. AcpS family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 123

123

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

PRO_0000175711

Sites

Metal binding

9

1

Magnesium By similarity

Metal binding

57

1

Magnesium By similarity

Secondary structure

1

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123

Helix Strand Turn

Details...

Beta strand

2 – 12

11

Helix

13 – 22

10

Helix

26 – 30

5

Helix

33 – 36

4

Beta strand

41 – 43

3

Helix

46 – 62

17

Helix

71 – 73

3

Beta strand

74 – 78

5

Beta strand

84 – 88

5

Helix

90 – 99

10

Beta strand

103 – 111

9

Beta strand

114 – 123

10

Sequences

	Sequence		Length	Mass (Da)
	O86785 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: C8301B17E510E56D	FASTA	123	12,566
	10 20 30 40 50 60 MSIIGVGIDV AEVERFGAAL ERTPALAGRL FLESELLLPG GERRGVASLA ARFAAKEALA 70 80 90 100 110 120 KALGAPAGLL WTDAEVWVEA GGRPRLRVTG TVAARAAELG VASWHVSLSH DAGIASAVVI AEG

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL939121 Genomic DNA. Translation: CAA20400.1.

PIR

T35573.

RefSeq

NP_628902.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JBZ	X-ray	1.62	A	1-123	[»]
2JCA	X-ray	1.98	A/B/C	1-123	[»]
2WDO	X-ray	1.56	A	1-123	[»]
2WDS	X-ray	1.35	A	1-123	[»]
2WDY	X-ray	1.40	A	1-123	[»]

ProteinModelPortal

O86785.

SMR

O86785. Positions 1-123.

ModBase

Search...

Protein-protein interaction databases

STRING

100226.SCO4744.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAA20400; CAA20400; CAA20400.

GeneID

1100185.

KEGG

sco:SCO4744.

PATRIC

23739312. VBIStrCoe124346_4816.

Phylogenomic databases

eggNOG

NOG129113.

HOGENOM

HOG000014315.

KO

K00997.

OMA

APAGMNW.

ProtClustDB

PRK00070.

Family and domain databases

Gene3D

3.90.470.20. 1 hit.

HAMAP

MF_00101. AcpS.

InterPro

IPR008278. 4-PPantetheinyl_Trfase_SF.
IPR002582. ACPS.
IPR004568. PPantethiene-prot_Trfase_dom.
[Graphical view]

Pfam

PF01648. ACPS. 1 hit.
[Graphical view]

ProDom

PD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF56214. 4-PPT_transf. 1 hit.

TIGRFAMs

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

ProtoNet

Search...

Other

EvolutionaryTrace

O86785.

Entry information

Entry name

ACPS_STRCO

Accession

Primary (citable) accession number: O86785

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program