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P80643

- ACP_BACSU

UniProt

P80643 - ACP_BACSU

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Protein

Acyl carrier protein

Gene

acpA

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

Functioni

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

Pathwayi

GO - Molecular functioni

  1. ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process Source: UniProtKB-HAMAP
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: Chromosome

Organism-specific databases

GenoListiBSU15920. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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)serine1 PublicationUniRule annotation

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.BSU15920.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiAANDYIN.
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:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59433 Genomic DNA. Translation: AAC44308.1 .
D64116 Genomic DNA. Translation: BAA10975.1 .
AL009126 Genomic DNA. Translation: CAB13465.1 .
PIRi JC4822.
T46634.
RefSeqi NP_389474.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P80643.
SMRi P80643. Positions 1-76.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P80643. 2 interactions.
STRINGi 224308.BSU15920.

Proteomic databases

PaxDbi P80643.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13465 ; CAB13465 ; BSU15920 .
GeneIDi 938486.
KEGGi bsu:BSU15920.
PATRICi 18974989. VBIBacSub10457_1686.

Organism-specific databases

GenoListi BSU15920. [Micado ]

Phylogenomic databases

eggNOGi COG0236.
HOGENOMi HOG000178184.
InParanoidi P80643.
KOi K02078.
OMAi AANDYIN.
OrthoDBi EOG6MWNJM.
PhylomeDBi P80643.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci BSUB:BSU15920-MONOMER.

Miscellaneous databases

EvolutionaryTracei P80643.

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
HAMAPi MF_01217. Acyl_carrier.
InterProi IPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006162. PPantetheine_attach_site.
[Graphical view ]
Pfami PF00550. PP-binding. 1 hit.
[Graphical view ]
ProDomi PD000887. PD000887. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF47336. SSF47336. 1 hit.
TIGRFAMsi TIGR00517. acyl_carrier. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 116 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