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P80643 (ACP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acyl carrier protein

Short name=ACP
Gene names
Name:acpA
Synonyms:acpP
Ordered Locus Names:BSU15920
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7777Acyl carrier protein HAMAP MF_01217
PRO_0000180104

Amino acid modifications

Modified residue371O-(pantetheine 4'-phosphoryl)serine HAMAP 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: 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. 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: 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.
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...

Protein-protein interaction databases

IntActP80643. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002503; EBBACP00000002503; EBBACG00000002498.
GeneID938486.
GenomeReviewsGene locus BSU15920 in contig AL009126_GR.
KEGGbsu:BSU15920.
NMPDRfig|224308.1.peg.1594.
PATRIC18974989. VBIBacSub10457_1686.

Organism-specific databases

GenoListBSU15920. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002064.
HOGENOMHBG755218.
OMAKIVCEQL.
PhylomeDBP80643.
ProtClustDBPRK00982.

Enzyme and pathway databases

BioCycBSUB:BSU15920-MONOMER.

Family and domain databases

HAMAPMF_01217. Acyl_carrier.
[Tree]
InterProIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006163. Phsphopanteth-bd.
IPR006162. PPantetheine_attach_site.
[Graphical view]
Gene3DG3DSA:1.10.1200.10. ACP_like. 1 hit.
KOK02078.
PfamPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47336. ACP_like. 1 hit.
TIGRFAMsTIGR00517. Acyl_carrier. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families