P80643 (ACP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl carrier protein
Short name=ACP

Gene names

Name:	acpA
Synonyms:	acpP
Ordered Locus Names:	BSU15920

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	77 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Carrier of the growing fatty acid chain in fatty acid biosynthesis. HAMAP MF_01217
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01217
Subcellular location	Cytoplasm By similarity HAMAP MF_01217.
Post-translational modification	4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group. HAMAP MF_01217
Sequence similarities	Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	Phosphopantetheine
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro phosphopantetheine 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 – 77

77

Acyl carrier protein HAMAP MF_01217

PRO_0000180104

Amino acid modifications

Modified residue

37

1

O-(pantetheine 4'-phosphoryl)serine HAMAP MF_01217

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

77

Helix Strand Turn

Details...

Helix

3 – 14

12

Turn

15 – 21

7

Beta strand

25 – 27

3

Beta strand

29 – 33

5

Helix

37 – 50

14

Helix

57 – 62

6

Helix

66 – 76

11

Sequences

	Sequence		Length	Mass (Da)
	P80643 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 75E745DE3C6A0951	FASTA	77	8,591
	10 20 30 40 50 60 MADTLERVTK IIVDRLGVDE ADVKLEASFK EDLGADSLDV VELVMELEDE FDMEISDEDA 70 EKIATVGDAV NYIQNQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes." Morbidoni H.R., de Mendoza D., Cronan J.E. Jr. J. Bacteriol. 178:4794-4800(1996) [PubMed: 8759840] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-77, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14. Strain: 168.
[2]	"The effect of Srb, a homologue of the mammalian SRP receptor alpha-subunit, on Bacillus subtilis growth and protein translocation." Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K. Gene 172:17-24(1996) [PubMed: 8654983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"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.
[4]	"Role of the D-alanyl carrier protein in the biosynthesis of D-alanyl-lipoteichoic acid." Heaton M.P., Neuhaus F.C. J. Bacteriol. 176:681-690(1994) [PubMed: 8300523] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-17.
[5]	"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: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOLO-(ACYL-CARRIER-PROTEIN) IN COMPLEX WITH HOLO-(ACYL-CARRIER-PROTEIN) SYNTHASE.
[6]	"Solution structure of B. subtilis acyl carrier protein." Xu G.Y., Tam A., Lin L., Hixon J., Fritz C.C., Powers R. Structure 9:277-287(2001) [PubMed: 11525165] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U59433 Genomic DNA. Translation: AAC44308.1.
D64116 Genomic DNA. Translation: BAA10975.1.
AL009126 Genomic DNA. Translation: CAB13465.1.

PIR

JC4822.
T46634.

RefSeq

NP_389474.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F80	X-ray	2.30	D/E/F	2-77	[»]
1HY8	NMR	-	A	2-77	[»]
2X2B	X-ray	2.69	A	1-77	[»]

ProteinModelPortal

P80643.

SMR

P80643. Positions 1-76.

ModBase

Search...

Protein-protein interaction databases

IntAct

P80643. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000002503; EBBACP00000002503; EBBACG00000002498.

GeneID

938486.

GenomeReviews

Gene locus BSU15920 in contig AL009126_GR.

KEGG

bsu:BSU15920.

NMPDR

fig|224308.1.peg.1594.

PATRIC

18974989. VBIBacSub10457_1686.

Organism-specific databases

GenoList

BSU15920. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000002064.

HOGENOM

HBG755218.

OMA

KIVCEQL.

PhylomeDB

P80643.

ProtClustDB

PRK00982.

Enzyme and pathway databases

BioCyc

BSUB:BSU15920-MONOMER.

Family and domain databases

HAMAP

MF_01217. Acyl_carrier.
[Tree]

InterPro

IPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006163. Phsphopanteth-bd.
IPR006162. PPantetheine_attach_site.
[Graphical view]

Gene3D

G3DSA:1.10.1200.10. ACP_like. 1 hit.

KO

K02078.

Pfam

PF00550. PP-binding. 1 hit.
[Graphical view]

ProDom

PD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF47336. ACP_like. 1 hit.

TIGRFAMs

TIGR00517. Acyl_carrier. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACP_BACSU

Accession

Primary (citable) accession number: P80643
Secondary accession number(s): P51832

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program