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P80643

- ACP_BACSU

UniProt

P80643 - ACP_BACSU

Protein

Acyl carrier protein

Gene

acpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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-SubCell

    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.
    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

    MADTLERVTK IIVDRLGVDE ADVKLEASFK EDLGADSLDV VELVMELEDE   50
    FDMEISDEDA EKIATVGDAV NYIQNQQ 77
    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.
    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

    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 1, 2014
    This is version 115 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