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P96618

- ACPS_BACSU

UniProt

P96618 - ACPS_BACSU

Protein

Holo-[acyl-carrier-protein] synthase

Gene

acpS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl carrier protein of secondary metabolism.1 Publication

    Catalytic activityi

    CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].1 PublicationUniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi8 – 81Magnesium
    Metal bindingi58 – 581Magnesium

    GO - Molecular functioni

    1. holo-[acyl-carrier-protein] synthase activity Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-HAMAP
    2. macromolecule biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU04620-MONOMER.
    SABIO-RKP96618.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Holo-[acyl-carrier-protein] synthaseUniRule annotation (EC:2.7.8.7UniRule annotation)
    Short name:
    Holo-ACP synthaseUniRule annotation
    Alternative name(s):
    4'-phosphopantetheinyl transferase AcpSUniRule annotation
    Gene namesi
    Name:acpSUniRule annotation
    Synonyms:ydcB
    Ordered Locus Names:BSU04620
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU04620. [Micado]

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21I → A: 6% of wild-type activity. 1 Publication
    Mutagenesisi5 – 51I → R: Loss of activity; no trimer formation. 1 Publication
    Mutagenesisi113 – 1131Q → E: 14% of wild-type activity. 1 Publication
    Mutagenesisi113 – 1131Q → R: Loss of activity; no trimer formation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 121121Holo-[acyl-carrier-protein] synthasePRO_0000175613Add
    BLAST

    Proteomic databases

    PaxDbiP96618.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    IntActiP96618. 1 interaction.
    STRINGi224308.BSU04620.

    Structurei

    Secondary structure

    1
    121
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1110
    Helixi12 – 2110
    Helixi25 – 295
    Helixi32 – 387
    Helixi43 – 6321
    Beta strandi68 – 714
    Helixi74 – 763
    Beta strandi78 – 814
    Beta strandi87 – 915
    Turni92 – 943
    Beta strandi95 – 10511
    Beta strandi107 – 11711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F7LX-ray1.50A1-121[»]
    1F7TX-ray1.80A/B/C/D/E/F2-121[»]
    1F80X-ray2.30A/B/C2-121[»]
    ProteinModelPortaliP96618.
    SMRiP96618. Positions 2-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96618.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the P-Pant transferase superfamily. AcpS family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0736.
    HOGENOMiHOG000014315.
    KOiK00997.
    OMAiRRWATED.
    OrthoDBiEOG6384R9.
    PhylomeDBiP96618.

    Family and domain databases

    Gene3Di3.90.470.20. 1 hit.
    HAMAPiMF_00101. AcpS.
    InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
    IPR002582. ACPS.
    IPR004568. PPantethiene-prot_Trfase_dom.
    [Graphical view]
    PfamiPF01648. ACPS. 1 hit.
    [Graphical view]
    ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF56214. SSF56214. 1 hit.
    TIGRFAMsiTIGR00516. acpS. 1 hit.
    TIGR00556. pantethn_trn. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P96618-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIYGIGLDIT ELKRIASMAG RQKRFAERIL TRSELDQYYE LSEKRKNEFL    50
    AGRFAAKEAF SKAFGTGIGR QLSFQDIEIR KDQNGKPYII CTKLSQAAVH 100
    VSITHTKEYA AAQVVIERLS S 121
    Length:121
    Mass (Da):13,718
    Last modified:May 1, 1997 - v1
    Checksum:i6C10401DA7116701
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001488 Genomic DNA. Translation: BAA19299.1.
    AL009126 Genomic DNA. Translation: CAB12269.1.
    PIRiH69772.
    RefSeqiNP_388343.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12269; CAB12269; BSU04620.
    GeneIDi938194.
    KEGGibsu:BSU04620.
    PATRICi18972508. VBIBacSub10457_0482.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001488 Genomic DNA. Translation: BAA19299.1 .
    AL009126 Genomic DNA. Translation: CAB12269.1 .
    PIRi H69772.
    RefSeqi NP_388343.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F7L X-ray 1.50 A 1-121 [» ]
    1F7T X-ray 1.80 A/B/C/D/E/F 2-121 [» ]
    1F80 X-ray 2.30 A/B/C 2-121 [» ]
    ProteinModelPortali P96618.
    SMRi P96618. Positions 2-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P96618. 1 interaction.
    STRINGi 224308.BSU04620.

    Chemistry

    BindingDBi P96618.
    ChEMBLi CHEMBL4734.

    Proteomic databases

    PaxDbi P96618.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12269 ; CAB12269 ; BSU04620 .
    GeneIDi 938194.
    KEGGi bsu:BSU04620.
    PATRICi 18972508. VBIBacSub10457_0482.

    Organism-specific databases

    GenoListi BSU04620. [Micado ]

    Phylogenomic databases

    eggNOGi COG0736.
    HOGENOMi HOG000014315.
    KOi K00997.
    OMAi RRWATED.
    OrthoDBi EOG6384R9.
    PhylomeDBi P96618.

    Enzyme and pathway databases

    BioCyci BSUB:BSU04620-MONOMER.
    SABIO-RK P96618.

    Miscellaneous databases

    EvolutionaryTracei P96618.
    PROi P96618.

    Family and domain databases

    Gene3Di 3.90.470.20. 1 hit.
    HAMAPi MF_00101. AcpS.
    InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
    IPR002582. ACPS.
    IPR004568. PPantethiene-prot_Trfase_dom.
    [Graphical view ]
    Pfami PF01648. ACPS. 1 hit.
    [Graphical view ]
    ProDomi PD004282. PPantethiene-prot_Trfase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF56214. SSF56214. 1 hit.
    TIGRFAMsi TIGR00516. acpS. 1 hit.
    TIGR00556. pantethn_trn. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome."
      Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "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.
    3. "4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis."
      Mootz H.D., Finking R., Marahiel M.A.
      J. Biol. Chem. 276:37289-37298(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    4. "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: MUTAGENESIS OF ILE-2; ILE-5 AND GLN-113, X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH COENZYME A AND WITH HOLO-(ACYL-CARRIER-PROTEIN), SUBUNIT.

    Entry informationi

    Entry nameiACPS_BACSU
    AccessioniPrimary (citable) accession number: P96618
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 113 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, Reference proteome

    Documents

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

    External Data

    Dasty 3