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P29958

- AAC_ACTUT

UniProt

P29958 - AAC_ACTUT

Protein

Aculeacin-A acylase

Gene

aac

Organism
Actinoplanes utahensis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of the palmitoyl moiety of the antifungal antibiotic, aculeacin-A, giving a hexapeptide moiety and a long chain fatty acid.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei230 – 2301NucleophileBy similarity

    GO - Molecular functioni

    1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: InterPro

    GO - Biological processi

    1. antibiotic biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aculeacin-A acylase (EC:3.5.1.-)
    Cleaved into the following 2 chains:
    Gene namesi
    Name:aac
    OrganismiActinoplanes utahensis
    Taxonomic identifieri1869 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeActinoplanes

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 34121 PublicationPRO_0000020598Add
    BLAST
    Chaini35 – 786752Aculeacin-A acylasePRO_0000253350Add
    BLAST
    Chaini35 – 214180Aculeacin-A acylase small subunitPRO_0000020599Add
    BLAST
    Propeptidei215 – 22915Spacer peptide1 PublicationPRO_0000020600Add
    BLAST
    Chaini230 – 786557Aculeacin-A acylase large subunitPRO_0000020601Add
    BLAST

    Keywords - PTMi

    Zymogen

    Interactioni

    Subunit structurei

    Heterodimer of a small subunit and a large subunit processed from the same precursor.

    Structurei

    3D structure databases

    ProteinModelPortaliP29958.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 13096Substrate-bindingSequence AnalysisAdd
    BLAST
    Regioni220 – 23920Possible recognition-sequence of an AAC processing enzymeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S45 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.10.439.10. 1 hit.
    3.60.20.10. 2 hits.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR002692. Penicillin_amidase-like.
    IPR023343. Penicillin_amidase_dom1.
    [Graphical view]
    PfamiPF01804. Penicil_amidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P29958-1 [UniParc]FASTAAdd to Basket

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    MTSSYMRLKA AAIAFGVIVA TAAVPSPASG REHDGGYAAL IRRASYGVPH    50
    ITADDFGSLG FGVGYVQAED NICVIAESVV TANGERSRWF GATGPDDADV 100
    RTTSSTQAID DRVAERLLEG PRDGVRAPCD DVRDQMRGFV AGYNHFLRRT 150
    GVHRLTDPAC RGKAWVRPLS EIDLWRTSWD SMVRAGSGAL LDGIVAATPP 200
    TAAGPASAPE APDAAAIAAA LDGTSAGIGS NAYGLGAQAT VNGSGMVLAN 250
    PHFPWQGAER FYRMHLKVPG RYDVEGAALI GDPIIEIGHN RTVAWSHTVS 300
    TARRFVWHRL SLVPGDPTSY YVDGRPERMR ARTVTVQTGS GPVSRTFHDT 350
    RYGPVAVVPG TFDWTPATAY AITDVNAGNN RAFDGWLRMG QAKDVRALKA 400
    VLDRHQFLPW VNVIAADARG EALYGDHSVV PRVTGALAAA CIPAPFQPLY 450
    ASSGQAVLDG SRSDCALGAD PDAAVPGILG PASLPVRFRD DYVTNSNDSH 500
    WLASPAAPLE GFPRILGNER TPRSLRTRLG LDQIQQRLAG TDGLPGKGFT 550
    TARLWQVMFG NRMHGAELVR DDLVALCRRQ PTATASNGAI VDLTAACTAL 600
    SRFDERADLD SRGAHLFTEF LAGGIRFADT FEVTDPVRTP APFWNTTDPR 650
    VRTALADACN GSPASPSTRS VGDIHTDSRG ERRIPIHGGR GEAGTFNVIT 700
    NPLVPGVGYP QVVHGTSFVM AVELGPHGPS GRQILTYAQS TNPNSPWYAD 750
    QTVLYSRKGW DTIKYTEAQI AADPNLRVYR VAQRGR 786
    Length:786
    Mass (Da):84,090
    Last modified:April 1, 1993 - v1
    Checksum:i721D8A9D71E4C38C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10610 Genomic DNA. Translation: BAA01465.1.
    PIRiJC1298.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10610 Genomic DNA. Translation: BAA01465.1 .
    PIRi JC1298.

    3D structure databases

    ProteinModelPortali P29958.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.439.10. 1 hit.
    3.60.20.10. 2 hits.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR002692. Penicillin_amidase-like.
    IPR023343. Penicillin_amidase_dom1.
    [Graphical view ]
    Pfami PF01804. Penicil_amidase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of the aculeacin A acylase-encoding gene from Actinoplanes utahensis and expression in Streptomyces lividans."
      Inokoshi J., Takeshima H., Ikeda H., Omura S.
      Gene 119:29-35(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-53; 212-214 AND 230-249.
      Strain: NRRL 12052.

    Entry informationi

    Entry nameiAAC_ACTUT
    AccessioniPrimary (citable) accession number: P29958
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 61 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

    Direct protein sequencing

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3