P00808 (BLAC_BACLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-lactamase
EC=3.5.2.6

Alternative name(s):
Penicillinase

Cleaved into the following 2 chains:

1. Large exopenicillinase
2. Small exopenicillinase

Gene names

Name:	penP
Synonyms:	blaP

Organism

Bacillus licheniformis

Taxonomic identifier

1402 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group

Protein attributes

Sequence length	307 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)

Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Subcellular location	Cell membrane; Lipid-anchor Probable.
Induction	By the bacillus licheniformis protein BlaR1.
Post-translational modification	Large exopenicillinase is the primary secretion product; it can be converted to small exopenicillinase.
Sequence similarities	Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Hydrolase
PTM	Lipoprotein Palmitate
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	beta-lactam antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-lactamase 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

Signal peptide

1 – 26

26

Chain

27 – 307

281

Large exopenicillinase

PRO_0000016973

Chain

43 – 307

265

Small exopenicillinase

PRO_0000016974

Regions

Region

248 – 250

3

Substrate binding

Sites

Active site

86

1

Acyl-ester intermediate

Active site

182

1

Proton acceptor

Amino acid modifications

Lipidation

27

1

N-palmitoyl cysteine

Lipidation

27

1

S-diacylglycerol cysteine

Secondary structure

1

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307

Helix Strand Turn

Details...

Helix

49 – 57

9

Beta strand

60 – 67

8

Turn

68 – 70

3

Beta strand

73 – 77

5

Beta strand

81 – 83

3

Helix

85 – 87

3

Helix

88 – 99

12

Helix

103 – 106

4

Turn

113 – 115

3

Helix

123 – 125

3

Turn

127 – 129

3

Helix

133 – 143

11

Helix

146 – 155

10

Helix

158 – 168

11

Beta strand

178 – 180

3

Helix

182 – 184

3

Beta strand

194 – 196

3

Helix

197 – 208

12

Beta strand

210 – 213

4

Helix

215 – 226

12

Turn

232 – 234

3

Helix

235 – 238

4

Beta strand

244 – 252

9

Turn

253 – 255

3

Beta strand

256 – 264

9

Beta strand

266 – 268

3

Beta strand

271 – 278

8

Helix

289 – 301

13

Sequences

	Sequence		Length	Mass (Da)
	P00808 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 7E25B1E72129A6DA	FASTA	307	33,996
	10 20 30 40 50 60 MKLWFSTLKL KKAAAVLLFS CVALAGCANN QTNASQPAEK NEKTEMKDDF AKLEEQFDAK 70 80 90 100 110 120 LGIFALDTGT NRTVAYRPDE RFAFASTIKA LTVGVLLQQK SIEDLNQRIT YTRDDLVNYN 130 140 150 160 170 180 PITEKHVDTG MTLKELADAS LRYSDNAAQN LILKQIGGPE SLKKELRKIG DEVTNPERFE 190 200 210 220 230 240 PELNEVNPGE TQDTSTARAL VTSLRAFALE DKLPSEKREL LIDWMKRNTT GDALIRAGVP 250 260 270 280 290 300 DGWEVADKTG AASYGTRNDI AIIWPPKGDP VVLAVLSSRD KKDAKYDDKL IAEATKVVMK ALNMNGK

References

[1]	"Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium." Neugebauer K., Sprengel R., Schaller H. Nucleic Acids Res. 9:2577-2588(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25972 / 749/C / DSM 8782 / NCIMB 11109 / IMET 10723.
[2]	"The promoter-proximal region of the Bacillus licheniformis penicillinase gene: nucleotide sequence and predicted leader peptide sequence." Kroyer J., Chang S. Gene 15:343-347(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72. Strain: ATCC 25972 / 749/C / DSM 8782 / NCIMB 11109 / IMET 10723.
[3]	"The amino acid sequence of penicillinase from Bacillus licheniformis." Meadway R.J. Biochem. J. 115:12P-13P(1969) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 43-307.
[4]	"Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators." Wittman V., Wong H.C. J. Bacteriol. 170:3206-3212(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15. Strain: ATCC 25972 / 749/C / DSM 8782 / NCIMB 11109 / IMET 10723.
[5]	"Large exopenicillinase, initial extracellular form detected in cultures of Bacillus licheniformis." Izui K., Nielsen J.B.K., Caulfield M.P., Lampen J.O. Biochemistry 19:1882-1886(1980) [PubMed] [Europe PMC] [Abstract] Cited for: CONFIRMATION OF THE AMINO ENDS OF THE LARGE AND SMALL EXOPENICILLINASE.
[6]	"Beta-lactamase of Bacillus licheniformis 749/C at 2-A resolution." Moews P.C., Knox J.R., Dideberg O., Charlier P., Frere J.-M. Proteins 7:156-171(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]	"Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2-A resolution and analysis of hydration." Knox J.R., Moews P.C. J. Mol. Biol. 220:435-455(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]	"Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin." Fonze E., Vanhove M., Dive G., Sauvage E., Frere J.-M., Charlier P. Biochemistry 41:1877-1885(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00093 Genomic DNA. Translation: CAA23431.1.
M21337 Genomic DNA. Translation: AAA22649.2.

PIR

PNBSL. A93727.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I2S	X-ray	1.70	A/B	26-307	[»]
1I2W	X-ray	1.70	A/B	26-307	[»]
1MBL	X-ray	2.00	A/B	48-303	[»]
1W7F	X-ray	1.80	A/B	1-307	[»]
2BLM	X-ray	2.00	A/B	43-307	[»]
2WK0	X-ray	1.65	A/B	43-307	[»]
2Y91	X-ray	2.00	A/B	43-307	[»]
3B3X	X-ray	2.50	A/B	43-307	[»]
3LY3	X-ray	1.80	A	47-305	[»]
3LY4	X-ray	1.80	A	47-303	[»]
3M2J	X-ray	1.80	A/B	47-303	[»]
3M2K	X-ray	3.50	A/B	47-303	[»]
3SH7	X-ray	2.50	A/B	43-307	[»]
3SH8	X-ray	2.00	A/B	43-307	[»]
3SH9	X-ray	1.90	A/B	43-307	[»]
3SOI	X-ray	1.73	A/B	46-303	[»]
4BLM	X-ray	2.00	A/B	43-307	[»]

ProteinModelPortal

P00808.

SMR

P00808. Positions 48-303.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]

Pfam

PF00144. Beta-lactamase. 1 hit.
[Graphical view]

PRINTS

PR00118. BLACTAMASEA.

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

PROSITE

PS00146. BETA_LACTAMASE_A. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00808.

ChEMBL

CHEMBL5633.

DrugBank

DB01331. Cefoxitin.

EvolutionaryTrace

P00808.

Entry information

Entry name

BLAC_BACLI

Accession

Primary (citable) accession number: P00808

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program