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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: 3 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

Pathology & Biotechi

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 – 106Combined sources
Beta strandi16 – 2611Combined sources
Beta strandi31 – 355Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 473Combined sources
Beta strandi50 – 523Combined sources
Beta strandi57 – 626Combined sources
Beta strandi64 – 674Combined sources
Beta strandi69 – 757Combined sources
Beta strandi80 – 856Combined sources
Turni87 – 893Combined sources
Beta strandi93 – 953Combined sources
Beta strandi101 – 1033Combined sources
Helixi105 – 1073Combined sources
Helixi108 – 1158Combined sources
Helixi119 – 1279Combined sources
Beta strandi129 – 1324Combined sources
Turni137 – 1393Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi178 – 1803Combined sources
Helixi182 – 1887Combined sources
Helixi189 – 1924Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi213 – 2153Combined sources
Helixi217 – 2193Combined sources
Helixi228 – 24114Combined sources
Helixi248 – 26013Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi278 – 2869Combined sources
Turni287 – 2904Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi299 – 3079Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi329 – 3313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MLGCSSLSIR TTDDKSLFAR TMDFTMEPDS KVIIVPRNYG IRLLEKENVV
60 70 80 90 100
INNSYAFVGM GSTDITSPVL YDGVNEKGLM GAMLYYATFA TYADEPKKGT
110 120 130 140 150
TGINPVYVIS QVLGNCVTVD DVIEKLTSYT LLNEANIILG FAPPLHYTFT
160 170 180 190 200
DASGESIVIE PDKTGITIHR KTIGVMTNSP GYEWHQTNLR AYIGVTPNPP
210 220 230 240 250
QDIMMGDLDL TPFGQGAGGL GLPGDFTPSA RFLRVAYWKK YTEKAKNETE
260 270 280 290 300
GVTNLFHILS SVNIPKGVVL TNEGKTDYTI YTSAMCAQSK NYYFKLYDNS
310 320 330
RISAVSLMAE NLNSQDLITF EWDRKQDIKQ LNQVNVMS
Length:338
Mass (Da):37,458
Last modified:October 1, 1989 - v1
Checksum:i69C8A9F69BB084B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15660 Genomic DNA. Translation: AAA22654.1.
PIRiA25559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15660 Genomic DNA. Translation: AAA22654.1 .
PIRi A25559.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

DrugBanki DB00417. Penicillin V.

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: November 26, 2014
This is version 76 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