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P12256

- PAC_LYSSH

UniProt

P12256 - PAC_LYSSH

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Protein
Penicillin acylase
Gene
N/A
Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 form
PRO_0000045278
Chaini4 – 338335Penicillin acylase
PRO_0000045279Add
BLAST

Keywords - PTMi

Zymogen

Miscellaneous databases

PMAP-CutDBP12256.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP12256.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C59 family.

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: September 3, 2014
This is version 73 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

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