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P04190 (BLA2_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase 2

EC=3.5.2.6
Alternative name(s):
Beta-lactamase II
Cephalosporinase
Penicillinase
Gene names
Name:blm
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus 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 metallo-beta-lactamase superfamily. 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: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

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 [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] [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.
PIRPNBSU2. A91806.

3D structure databases

PDBe
RCSB-PDB
PDBj
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/B31-191[»]
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[»]
2M5CNMR-A31-257[»]
2M5DNMR-A31-257[»]
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[»]
3I0VX-ray1.60A31-257[»]
3I11X-ray1.45A31-257[»]
3I13X-ray1.74A31-257[»]
3I14X-ray1.55A31-257[»]
3I15X-ray1.55A31-257[»]
3KNRX-ray1.71A/B/C/D31-257[»]
3KNSX-ray1.58A/B/C/D31-257[»]
ProteinModelPortalP04190.
SMRP04190. Positions 37-247.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP04190.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
PROSITEPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04190.

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: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references