P04190 (BLA2_BACCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-lactamase 2
EC=3.5.2.6

Alternative name(s):
Beta-lactamase II
Cephalosporinase
Penicillinase

Gene names

Name:

blm

Organism

Bacillus cereus

Taxonomic identifier

1396 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	257 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	Can hydrolyze carbapenem compounds.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Cofactor	Binds 2 zinc ions per subunit. The enzyme can also function with only 1 zinc ion.
Subunit structure	Monomer.
Sequence similarities	Belongs to the class-B beta-lactamase family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	beta-lactamase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Ref.2

Chain

31 – 257

227

Beta-lactamase 2

PRO_0000016942

Sites

Metal binding

116

1

Zinc 1; high-affinity

Metal binding

118

1

Zinc 1; high-affinity

Metal binding

120

1

Zinc 2; low-affinity

Metal binding

179

1

Zinc 1; high-affinity

Metal binding

198

1

Zinc 2; low-affinity

Metal binding

240

1

Zinc 2; low-affinity

Secondary structure

1

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257

Helix Strand Turn

Details...

Beta strand

38 – 40

3

Beta strand

42 – 52

11

Beta strand

55 – 64

10

Beta strand

67 – 78

12

Beta strand

81 – 86

6

Helix

91 – 105

15

Beta strand

109 – 113

5

Beta strand

116 – 118

3

Helix

119 – 122

4

Helix

125 – 131

7

Beta strand

134 – 136

3

Helix

139 – 147

9

Beta strand

159 – 165

7

Beta strand

168 – 173

6

Beta strand

178 – 182

5

Beta strand

185 – 187

3

Turn

189 – 191

3

Beta strand

193 – 197

5

Helix

216 – 229

14

Beta strand

234 – 241

8

Helix

247 – 255

9

Sequences

	Sequence		Length	Mass (Da)
	P04190 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: 268EBFB7DDA45431	FASTA	257	28,092
	10 20 30 40 50 60 MKKNTLLKVG LCVGLLGTIQ FVSTISSVQA SQKVEKTVIK NETGTISISQ LNKNVWVHTE 70 80 90 100 110 120 LGSFNGEAVP SNGLVLNTSK GLVLVDSSWD DKLTKELIEM VEKKFQKRVT DVIITHAHAD 130 140 150 160 170 180 RIGGIKTLKE RGIKAHSTAL TAELAKKNGY EEPLGDLQTV TNLKFGNMKV ETFYPGKGHT 190 200 210 220 230 240 EDNIVVWLPQ YNILVGGCLV KSTSAKDLGN VADAYVNEWS TSIENVLKRY RNINAVVPGH 250 GEVGDKGLLL HTLDLLK

References

[1]	"Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli." Hussain M., Carlino A., Madonna M.J., Lampen J.O. J. Bacteriol. 164:223-229(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 569/H / NCTC 9945.
[2]	"The amino acid sequence of the zinc-requiring beta-lactamase II from the bacterium Bacillus cereus 569." Ambler R.P., Daniel M., Fleming J., Hermoso J.M., Pang C., Waley S.G. FEBS Lett. 189:207-211(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-183; 187-210 AND 214-257. Strain: 569/H / NCTC 9945.
[3]	"An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35-nm resolution." Sutton B.J., Artymiuk P.J., Cordero-Borboa A.E., Little C., Phillips D.C., Waley S.G. Biochem. J. 248:181-188(1987) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[4]	"The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold." Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J.-M., Dideberg O. EMBO J. 14:4914-4921(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]	"1.85-A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus." Carfi A., Duee E., Galleni M., Frere J.-M., Dideberg O. Acta Crystallogr. D 54:313-323(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[6]	"Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9-A resolution: binuclear active site with features of a mononuclear enzyme." Fabiane S.M., Sohi M.K., Wan T., Payne D.J., Bateson J.H., Mitchell T., Sutton B.J. Biochemistry 37:12404-12411(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). Strain: 569/H / NCTC 9945.
[7]	"Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase." Chantalat L., Duee E., Galleni M., Frere J.-M., Dideberg O. Protein Sci. 9:1402-1406(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT SER-198. Strain: 569/H / NCTC 9945.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11189 Genomic DNA. Translation: AAA22276.1.

PIR

PNBSU2. A91806.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BC2	X-ray	1.90	A/B	31-257	[»]
1BMC	X-ray	2.50	A	37-257	[»]
1BVT	X-ray	1.85	A	31-257	[»]
1DXK	X-ray	1.85	A	31-257	[»]
1MQO	X-ray	1.35	A	31-257	[»]
2BC2	X-ray	1.70	A/B	31-257	[»]
2BFK	X-ray	2.00	A/B	31-257	[»]
2BFL	X-ray	1.80	A/B	31-257	[»]
2BFZ	X-ray	2.30	A/B	31-257	[»]
2BG2	X-ray	2.40	A/B	31-257	[»]
2BG6	X-ray	2.30	A/B	31-257	[»]
2BG7	X-ray	2.10	A/B	31-257	[»]
2BG8	X-ray	2.50	A/B	31-257	[»]
2BGA	X-ray	2.70	A/B	31-257	[»]
2NXA	X-ray	2.29	A	37-257	[»]
2NYP	X-ray	1.84	A	37-257	[»]
2NZE	X-ray	1.80	A/B	36-257	[»]
2NZF	X-ray	2.28	A	37-257	[»]
2UYX	X-ray	1.95	A	30-257	[»]
3BC2	X-ray	1.70	A	31-257	[»]
3FCZ	X-ray	2.80	A/B	36-247	[»]
3I0V	X-ray	1.60	A	31-257	[»]
3I11	X-ray	1.45	A	31-257	[»]
3I13	X-ray	1.74	A	31-257	[»]
3I14	X-ray	1.55	A	31-257	[»]
3I15	X-ray	1.55	A	31-257	[»]
3KNR	X-ray	1.71	A/B/C/D	31-257	[»]
3KNS	X-ray	1.58	A/B/C/D	31-257	[»]

ProteinModelPortal

P04190.

SMR

P04190. Positions 37-247.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Enzyme and pathway databases

SABIO-RK

P04190.

Family and domain databases

InterPro

IPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]

Pfam

PF00753. Lactamase_B. 1 hit.
[Graphical view]

SMART

SM00849. Lactamase_B. 1 hit.
[Graphical view]

PROSITE

PS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04190.

Entry information

Entry name

BLA2_BACCE

Accession

Primary (citable) accession number: P04190

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program