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 (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

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-Rule MF_01217
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01217
Subcellular location	Cytoplasm By similarity.
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-Rule MF_01217
Sequence similarities	Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	Phosphopantetheine
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process 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 – 77

77

Acyl carrier protein HAMAP-Rule MF_01217

PRO_0000180104

Amino acid modifications

Modified residue

37

1

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

77

Helix Strand Turn

Details...

Helix

3 – 15

13

Helix

20 – 22

3

Beta strand

25 – 27

3

Helix

29 – 32

4

Helix

39 – 50

12

Helix

57 – 62

6

Helix

66 – 72

7

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 2 interactions.

STRING

224308.BSU15920.

Proteomic databases

PaxDb

P80643.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13465; CAB13465; BSU15920.

GeneID

938486.

KEGG

bsu:BSU15920.

PATRIC

18974989. VBIBacSub10457_1686.

Organism-specific databases

GenoList

BSU15920. [Micado]

Phylogenomic databases

eggNOG

COG0236.

HOGENOM

HOG000178184.

KO

K02078.

OMA

KIVCEQL.

ProtClustDB

PRK00982.

Enzyme and pathway databases

BioCyc

BSUB:BSU15920-MONOMER.

UniPathway

UPA00094.

Family and domain databases

Gene3D

1.10.1200.10. 1 hit.

HAMAP

MF_01217. Acyl_carrier.

InterPro

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

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...

Other

EvolutionaryTrace

P80643.

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:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program