P96618 (ACPS_BACSU) 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
Synonyms:	ydcB
Ordered Locus Names:	BSU04620

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	121 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 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. 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 By similarity. HAMAP MF_00101
Subunit structure	Homotrimer.
Subcellular location	Cytoplasm By similarity HAMAP MF_00101.
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 Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 121

121

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

PRO_0000175613

Sites

Metal binding

8

1

Magnesium

Metal binding

58

1

Magnesium

Experimental info

Mutagenesis

2

1

I → A: 6% of wild-type activity. Ref.4

Mutagenesis

5

1

I → R: Loss of activity; no trimer formation. Ref.4

Mutagenesis

113

1

Q → E: 14% of wild-type activity. Ref.4

Mutagenesis

113

1

Q → R: Loss of activity; no trimer formation. Ref.4

Secondary structure

1

.

.

.

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.

.

.

.

.

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.

.

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.

.

.

.

.

121

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Helix

12 – 21

10

Helix

25 – 29

5

Helix

32 – 38

7

Helix

43 – 63

21

Helix

74 – 76

3

Beta strand

78 – 81

4

Beta strand

87 – 91

5

Turn

92 – 94

3

Beta strand

95 – 105

11

Beta strand

107 – 117

11

Sequences

	Sequence		Length	Mass (Da)
	P96618 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 6C10401DA7116701	FASTA	121	13,718
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9384377] [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: 11489886] [Abstract] Cited for: CHARACTERIZATION.
[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: 10997907] [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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB001488 Genomic DNA. Translation: BAA19299.1.
AL009126 Genomic DNA. Translation: CAB12269.1.

PIR

H69772.

RefSeq

NP_388343.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F7L	X-ray	1.50	A	2-121	[»]
1F7T	X-ray	1.80	A/B/C/D/E/F	2-121	[»]
1F80	X-ray	2.30	A/B/C	3-121	[»]

ProteinModelPortal

P96618.

SMR

P96618. Positions 2-119.

ModBase

Search...

Protein-protein interaction databases

IntAct

P96618. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000004077; EBBACP00000004077; EBBACG00000004069.

GeneID

938194.

GenomeReviews

Gene locus BSU04620 in contig AL009126_GR.

KEGG

bsu:BSU04620.

NMPDR

fig|224308.1.peg.462.

PATRIC

18972508. VBIBacSub10457_0482.

Organism-specific databases

GenoList

BSU04620. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001692.

HOGENOM

HBG734479.

OMA

VHVSITH.

PhylomeDB

P96618.

ProtClustDB

PRK00070.

Enzyme and pathway databases

BioCyc

BSUB:BSU04620-MONOMER.

Family and domain databases

HAMAP

MF_00101. AcpS.
[Tree]

InterPro

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

Gene3D

G3DSA:3.90.470.20. G3DSA:3.90.470.20. 1 hit.

KO

K00997.

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...

Entry information

Entry name

ACPS_BACSU

Accession

Primary (citable) accession number: P96618

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program