Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acyl carrier protein

Gene

acpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Carrier of the growing fatty acid chain in fatty acid biosynthesis.

Pathway: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU15920-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl carrier proteinUniRule annotation
Short name:
ACPUniRule annotation
Gene namesi
Name:acpA
Synonyms:acpP
Ordered Locus Names:BSU15920
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU15920. [Micado]

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7777Acyl carrier proteinPRO_0000180104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371O-(pantetheine 4'-phosphoryl)serineUniRule annotation1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP80643.

Interactioni

Protein-protein interaction databases

IntActiP80643. 2 interactions.
STRINGi224308.Bsubs1_010100008781.

Structurei

Secondary structure

1
77
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513Combined sources
Helixi20 – 223Combined sources
Beta strandi25 – 273Combined sources
Helixi29 – 324Combined sources
Helixi39 – 5012Combined sources
Helixi57 – 626Combined sources
Helixi66 – 727Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F80X-ray2.30D/E/F2-77[»]
1HY8NMR-A2-77[»]
2X2BX-ray2.69A1-77[»]
ProteinModelPortaliP80643.
SMRiP80643. Positions 1-76.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80643.

Family & Domainsi

Sequence similaritiesi

Contains 1 acyl carrier domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0236.
HOGENOMiHOG000178184.
InParanoidiP80643.
KOiK02078.
OMAiKFDVRIP.
OrthoDBiEOG6MWNJM.
PhylomeDBiP80643.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
HAMAPiMF_01217. Acyl_carrier.
InterProiIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomiPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47336. SSF47336. 1 hit.
TIGRFAMsiTIGR00517. acyl_carrier. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTLERVTK IIVDRLGVDE ADVKLEASFK EDLGADSLDV VELVMELEDE
60 70
FDMEISDEDA EKIATVGDAV NYIQNQQ
Length:77
Mass (Da):8,591
Last modified:October 1, 1996 - v1
Checksum:i75E745DE3C6A0951
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59433 Genomic DNA. Translation: AAC44308.1.
D64116 Genomic DNA. Translation: BAA10975.1.
AL009126 Genomic DNA. Translation: CAB13465.1.
PIRiJC4822.
T46634.
RefSeqiNP_389474.1. NC_000964.3.
WP_003154310.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13465; CAB13465; BSU15920.
GeneIDi938486.
9778756.
KEGGibsu:BSU15920.
PATRICi18974989. VBIBacSub10457_1686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59433 Genomic DNA. Translation: AAC44308.1.
D64116 Genomic DNA. Translation: BAA10975.1.
AL009126 Genomic DNA. Translation: CAB13465.1.
PIRiJC4822.
T46634.
RefSeqiNP_389474.1. NC_000964.3.
WP_003154310.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F80X-ray2.30D/E/F2-77[»]
1HY8NMR-A2-77[»]
2X2BX-ray2.69A1-77[»]
ProteinModelPortaliP80643.
SMRiP80643. Positions 1-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP80643. 2 interactions.
STRINGi224308.Bsubs1_010100008781.

Proteomic databases

PaxDbiP80643.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13465; CAB13465; BSU15920.
GeneIDi938486.
9778756.
KEGGibsu:BSU15920.
PATRICi18974989. VBIBacSub10457_1686.

Organism-specific databases

GenoListiBSU15920. [Micado]

Phylogenomic databases

eggNOGiCOG0236.
HOGENOMiHOG000178184.
InParanoidiP80643.
KOiK02078.
OMAiKFDVRIP.
OrthoDBiEOG6MWNJM.
PhylomeDBiP80643.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciBSUB:BSU15920-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP80643.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
HAMAPiMF_01217. Acyl_carrier.
InterProiIPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomiPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47336. SSF47336. 1 hit.
TIGRFAMsiTIGR00517. acyl_carrier. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACP_BACSU
AccessioniPrimary (citable) accession number: P80643
Secondary accession number(s): P51832
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.