Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P12256

- PAC_LYSSH

UniProt

P12256 - PAC_LYSSH

Protein

Penicillin acylase

Gene
N/A
Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The enzyme catalyzes the conversion of penicillin to 6-aminopenicillanate The precursor, furthermore, acts as a self-processing peptidase that cleaves off the propeptide. All peptidase activity is lost on conversion to the mature peptidase.

    Catalytic activityi

    Penicillin + H2O = a carboxylate + 6-aminopenicillanate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei4 – 41

    GO - Molecular functioni

    1. penicillin amidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Protein family/group databases

    MEROPSiC59.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Penicillin acylase (EC:3.5.1.11)
    Alternative name(s):
    Penicillin V amidase
    Short name:
    PVA
    OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
    Taxonomic identifieri1421 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 33Removed in mature form1 PublicationPRO_0000045278
    Chaini4 – 338335Penicillin acylasePRO_0000045279Add
    BLAST

    Keywords - PTMi

    Zymogen

    Miscellaneous databases

    PMAP-CutDBP12256.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Beta strandi16 – 2611
    Beta strandi31 – 355
    Beta strandi41 – 433
    Beta strandi45 – 473
    Beta strandi50 – 523
    Beta strandi57 – 626
    Beta strandi64 – 674
    Beta strandi69 – 757
    Beta strandi80 – 856
    Turni87 – 893
    Beta strandi93 – 953
    Beta strandi101 – 1033
    Helixi105 – 1073
    Helixi108 – 1158
    Helixi119 – 1279
    Beta strandi129 – 1324
    Turni137 – 1393
    Beta strandi145 – 1506
    Beta strandi156 – 1627
    Beta strandi165 – 1695
    Beta strandi174 – 1763
    Beta strandi178 – 1803
    Helixi182 – 1887
    Helixi189 – 1924
    Beta strandi203 – 2053
    Beta strandi208 – 2103
    Beta strandi213 – 2153
    Helixi217 – 2193
    Helixi228 – 24114
    Helixi248 – 26013
    Beta strandi268 – 2703
    Beta strandi278 – 2869
    Turni287 – 2904
    Beta strandi291 – 2966
    Beta strandi299 – 3079
    Beta strandi318 – 3214
    Beta strandi329 – 3313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IWMX-ray2.50A/B/C/D1-338[»]
    2PVAX-ray2.50A/B/C/D4-338[»]
    2QUYX-ray1.70A/B/C/D/E/F/G/H4-338[»]
    2Z71X-ray2.60A/C4-338[»]
    3MJIX-ray2.50A/B/C/D1-338[»]
    3PVAX-ray2.80A/B/C/D/E/F/G/H4-338[»]
    ProteinModelPortaliP12256.
    SMRiP12256. Positions 4-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12256.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C59 family.Curated

    Family and domain databases

    Gene3Di3.60.60.10. 1 hit.
    InterProiIPR029132. CBAH/NAAA_C.
    IPR003199. Chologlycine_hydro/PeptC59.
    IPR029055. Ntn_hydrolases_N.
    [Graphical view]
    PfamiPF02275. CBAH. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P12256-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGCSSLSIR TTDDKSLFAR TMDFTMEPDS KVIIVPRNYG IRLLEKENVV    50
    INNSYAFVGM GSTDITSPVL YDGVNEKGLM GAMLYYATFA TYADEPKKGT 100
    TGINPVYVIS QVLGNCVTVD DVIEKLTSYT LLNEANIILG FAPPLHYTFT 150
    DASGESIVIE PDKTGITIHR KTIGVMTNSP GYEWHQTNLR AYIGVTPNPP 200
    QDIMMGDLDL TPFGQGAGGL GLPGDFTPSA RFLRVAYWKK YTEKAKNETE 250
    GVTNLFHILS SVNIPKGVVL TNEGKTDYTI YTSAMCAQSK NYYFKLYDNS 300
    RISAVSLMAE NLNSQDLITF EWDRKQDIKQ LNQVNVMS 338
    Length:338
    Mass (Da):37,458
    Last modified:October 1, 1989 - v1
    Checksum:i69C8A9F69BB084B3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15660 Genomic DNA. Translation: AAA22654.1.
    PIRiA25559.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15660 Genomic DNA. Translation: AAA22654.1 .
    PIRi A25559.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IWM X-ray 2.50 A/B/C/D 1-338 [» ]
    2PVA X-ray 2.50 A/B/C/D 4-338 [» ]
    2QUY X-ray 1.70 A/B/C/D/E/F/G/H 4-338 [» ]
    2Z71 X-ray 2.60 A/C 4-338 [» ]
    3MJI X-ray 2.50 A/B/C/D 1-338 [» ]
    3PVA X-ray 2.80 A/B/C/D/E/F/G/H 4-338 [» ]
    ProteinModelPortali P12256.
    SMRi P12256. Positions 4-337.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C59.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P12256.
    PMAP-CutDB P12256.

    Family and domain databases

    Gene3Di 3.60.60.10. 1 hit.
    InterProi IPR029132. CBAH/NAAA_C.
    IPR003199. Chologlycine_hydro/PeptC59.
    IPR029055. Ntn_hydrolases_N.
    [Graphical view ]
    Pfami PF02275. CBAH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing and heterologous expression of the gene encoding penicillin V amidase from Bacillus sphaericus."
      Olsson A., Uhlen M.
      Gene 45:175-181(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-338, PROTEIN SEQUENCE OF N-TERMINUS.

    Entry informationi

    Entry nameiPAC_LYSSH
    AccessioniPrimary (citable) accession number: P12256
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 74 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3