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Reviewed, UniProtKB/Swiss-Prot P04190 (BLA2_BACCE)

Last modified November 3, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-lactamase 2
    EC=3.5.2.6
Alternative name(s):
    Beta-lactamase II
    Penicillinase
    Cephalosporinase
Gene names
Name: blm
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processAntibiotic resistance
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-lactamase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.2
Chain31 – 257227Beta-lactamase 2
PRO_0000016942

Sites

Metal binding1161Zinc 1; high-affinity
Metal binding1181Zinc 1; high-affinity
Metal binding1201Zinc 2; low-affinity
Metal binding1791Zinc 1; high-affinity
Metal binding1981Zinc 2; low-affinity
Metal binding2401Zinc 2; low-affinity

Secondary structure

......................................... 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04190-1 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 268EBFB7DDA45431

FASTA25728,092
        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 

« Hide

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: 3930467] [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: 3930290] [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: 3124808] [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: 7588620] [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: 9761898] [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: 9730812] [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: 10933508] [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

M11189 Genomic DNA. Translation: AAA22276.1.
PIRPNBSU2. A91806.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BC2X-ray1.90A/B31-257[»]
1BMCX-ray2.50A37-257[»]
1BVTX-ray1.85A31-257[»]
1DXKX-ray1.85A31-257[»]
1MQOX-ray1.35A31-257[»]
2BC2X-ray1.70A/B31-257[»]
2BFKX-ray2.00A/B31-257[»]
2BFLX-ray1.80A/B31-257[»]
2BFZX-ray2.30A/B31-257[»]
2BG2X-ray2.40A/B31-257[»]
2BG6X-ray2.30A/B31-257[»]
2BG7X-ray2.10A/B31-257[»]
2BG8X-ray2.50A/B31-257[»]
2BGAX-ray2.70A/B31-257[»]
2NXAX-ray2.29A37-257[»]
2NYPX-ray1.84A37-257[»]
2NZEX-ray1.80A/B36-257[»]
2NZFX-ray2.28A37-257[»]
2UYXX-ray1.95A30-257[»]
3BC2X-ray1.70A31-257[»]
3FCZX-ray2.80A/B36-247[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.5.2.6. 604.

Family and domain databases

InterProIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Blactmase-like.
[Graphical view]
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
PROSITEPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLA2_BACCE
AccessionPrimary (citable) accession number: P04190
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: November 3, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents