Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P80643 (ACP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl carrier protein

Short name=ACP
Gene names
Name:acpA
Synonyms:acpP
Ordered Locus Names:BSU15920
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length77 AA.
Sequence statusComplete.
Protein existenceEvidence 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 HAMAP-Rule 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-Rule MF_01217

Sequence similarities

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7777Acyl carrier protein HAMAP-Rule MF_01217
PRO_0000180104

Amino acid modifications

Modified residue371O-(pantetheine 4'-phosphoryl)serine HAMAP-Rule MF_01217

Secondary structure

............... 77
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80643 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 75E745DE3C6A0951

FASTA778,591
        10         20         30         40         50         60 
MADTLERVTK IIVDRLGVDE ADVKLEASFK EDLGADSLDV VELVMELEDE FDMEISDEDA 

        70 
EKIATVGDAV NYIQNQQ 

« Hide

References

« Hide '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, PHOSPHOPANTETHEINYLATION AT SER-37.
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. expand/collapse author list , 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.
PIRJC4822.
T46634.
RefSeqNP_389474.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F80X-ray2.30D/E/F2-77[»]
1HY8NMR-A2-77[»]
2X2BX-ray2.69A1-77[»]
ProteinModelPortalP80643.
SMRP80643. Positions 1-76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP80643. 2 interactions.
STRING224308.BSU15920.

Proteomic databases

PaxDbP80643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13465; CAB13465; BSU15920.
GeneID938486.
KEGGbsu:BSU15920.
PATRIC18974989. VBIBacSub10457_1686.

Organism-specific databases

GenoListBSU15920. [Micado]

Phylogenomic databases

eggNOGCOG0236.
HOGENOMHOG000178184.
KOK02078.
OMAAANDYIN.
OrthoDBEOG6MWNJM.
PhylomeDBP80643.

Enzyme and pathway databases

BioCycBSUB:BSU15920-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
HAMAPMF_01217. Acyl_carrier.
InterProIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006162. PPantetheine_attach_site.
[Graphical view]
PfamPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47336. SSF47336. 1 hit.
TIGRFAMsTIGR00517. acyl_carrier. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80643.

Entry information

Entry nameACP_BACSU
AccessionPrimary (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: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList