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P12256 (PAC_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Penicillin acylase

EC=3.5.1.11
Alternative name(s):
Penicillin V amidase
Short name=PVA
OrganismLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifier1421 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Penicillin + H2O = a carboxylate + 6-aminopenicillanate.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the peptidase C59 family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Molecular functionHydrolase
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processresponse to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpenicillin amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 33Removed in mature form
PRO_0000045278
Chain4 – 338335Penicillin acylase
PRO_0000045279

Sites

Active site41

Secondary structure

......................................................................... 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12256 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 69C8A9F69BB084B3

FASTA33837,458
        10         20         30         40         50         60 
MLGCSSLSIR TTDDKSLFAR TMDFTMEPDS KVIIVPRNYG IRLLEKENVV INNSYAFVGM 

        70         80         90        100        110        120 
GSTDITSPVL YDGVNEKGLM GAMLYYATFA TYADEPKKGT TGINPVYVIS QVLGNCVTVD 

       130        140        150        160        170        180 
DVIEKLTSYT LLNEANIILG FAPPLHYTFT DASGESIVIE PDKTGITIHR KTIGVMTNSP 

       190        200        210        220        230        240 
GYEWHQTNLR AYIGVTPNPP QDIMMGDLDL TPFGQGAGGL GLPGDFTPSA RFLRVAYWKK 

       250        260        270        280        290        300 
YTEKAKNETE GVTNLFHILS SVNIPKGVVL TNEGKTDYTI YTSAMCAQSK NYYFKLYDNS 

       310        320        330 
RISAVSLMAE NLNSQDLITF EWDRKQDIKQ LNQVNVMS 

« Hide

References

[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]"Penicillin V acylase crystal structure reveals new Ntn-hydrolase family members."
Suresh C.G., Pundle A.V., SivaRaman H., Rao K.N., Brannigan J.A., McVey C.E., Verma C.S., Dauter Z., Dodson E.J., Dodson G.G.
Nat. Struct. Biol. 6:414-416(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-338, PROTEIN SEQUENCE OF N-TERMINUS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15660 Genomic DNA. Translation: AAA22654.1.
PIRA25559.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP12256.
SMRP12256. Positions 4-337.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC59.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.60.60.10. 1 hit.
InterProIPR029132. CBAH/NAAA_C.
IPR003199. Chologlycine_hydro.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PfamPF02275. CBAH. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP12256.
PMAP-CutDBP12256.

Entry information

Entry namePAC_LYSSH
AccessionPrimary (citable) accession number: P12256
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references