P12256 (PAC_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Penicillin acylase EC=3.5.1.11 Alternative name(s): Penicillin V amidase Short name=PVA
Organism	Lysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifier	1421 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Lysinibacillus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Antibiotic resistance
Molecular function	Hydrolase
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	penicillin amidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 3

3

Removed in mature form

PRO_0000045278

Chain

4 – 338

335

Penicillin acylase

PRO_0000045279

Sites

Active site

4

1

Secondary structure

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338

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Beta strand

16 – 26

11

Beta strand

31 – 35

5

Beta strand

41 – 43

3

Beta strand

45 – 47

3

Beta strand

50 – 52

3

Beta strand

57 – 62

6

Beta strand

64 – 67

4

Beta strand

69 – 75

7

Beta strand

80 – 85

6

Turn

87 – 89

3

Beta strand

93 – 95

3

Beta strand

101 – 103

3

Helix

105 – 107

3

Helix

108 – 115

8

Helix

119 – 127

9

Beta strand

129 – 132

4

Turn

137 – 139

3

Beta strand

145 – 150

6

Beta strand

156 – 162

7

Beta strand

165 – 169

5

Beta strand

174 – 176

3

Beta strand

178 – 180

3

Helix

182 – 188

7

Helix

189 – 192

4

Beta strand

203 – 205

3

Beta strand

208 – 210

3

Beta strand

213 – 215

3

Helix

217 – 219

3

Helix

228 – 241

14

Helix

248 – 260

13

Beta strand

268 – 270

3

Beta strand

278 – 286

9

Turn

287 – 290

4

Beta strand

291 – 296

6

Beta strand

299 – 307

9

Beta strand

318 – 321

4

Beta strand

329 – 331

3

Sequences

	Sequence		Length	Mass (Da)
	P12256 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 69C8A9F69BB084B3	FASTA	338	37,458
	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

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.

PIR

A25559.

3D structure databases

PDBe
RCSB PDB
PDBj

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	5-338	[»]
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	[»]

ProteinModelPortal

P12256.

SMR

P12256. Positions 4-337.

ModBase

Search...

Protein family/group databases

MEROPS

C59.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.60.60.10. 1 hit.

InterPro

IPR003199. Chologlycine_hydro.
[Graphical view]

Pfam

PF02275. CBAH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12256.

PMAP-CutDB

P12256.

Entry information

Entry name

PAC_LYSSH

Accession

Primary (citable) accession number: P12256

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 29, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program