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P25910 (BLAB_BACFG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. 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 type II

EC=3.5.2.6
Alternative name(s):
Cephalosporinase
Imipenem-cefoxitin hydrolyzing enzyme
Penicillinase
Gene names
Name:ccrA
Synonyms:cfiA
OrganismBacteroides fragilis
Taxonomic identifier817 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length249 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.

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
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 – 1717
Chain18 – 249232Beta-lactamase type II
PRO_0000016945

Sites

Metal binding991Zinc 1 Ref.3
Metal binding1011Zinc 1 Ref.3
Metal binding1031Zinc 2
Metal binding1621Zinc 1 Ref.3
Metal binding1811Zinc 2
Metal binding2231Zinc 2

Secondary structure

......................................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25910 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 972B5A594DF5D40D

FASTA24927,257
        10         20         30         40         50         60 
MKTVFILISM LFPVAVMAQK SVKISDDISI TQLSDKVYTY VSLAEIEGWG MVPSNGMIVI 

        70         80         90        100        110        120 
NNHQAALLDT PINDAQTEML VNWVTDSLHA KVTTFIPNHW HGDCIGGLGY LQRKGVQSYA 

       130        140        150        160        170        180 
NQMTIDLAKE KGLPVPEHGF TDSLTVSLDG MPLQCYYLGG GHATDNIVVW LPTENILFGG 

       190        200        210        220        230        240 
CMLKDNQATS IGNISDADVT AWPKTLDKVK AKFPSARYVV PGHGDYGGTE LIEHTKQIVN 


QYIESTSKP 

« Hide

References

[1]"Cloning and sequencing of the class B beta-lactamase gene (ccrA) from Bacteroides fragilis TAL3636."
Rasmussen B.A., Gluzman Y., Tally F.P.
Antimicrob. Agents Chemother. 34:1590-1592(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TAL3636.
[2]"Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-beta-lactamase gene, ccrA."
Rasmussen B.A., Gluzman Y., Tally F.P.
Mol. Microbiol. 5:1211-1219(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TAL3636.
[3]"Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus beta-lactamase II."
Thompson J.S., Malamy M.H.
J. Bacteriol. 172:2584-2593(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TAL2480.
[4]"Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis."
Concha N.O., Rasmusssen B.A., Bush K., Herzberg O.
Structure 4:823-836(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[5]"Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis."
Concha N.O., Rasmussen B.A., Bush K., Herzberg O.
Protein Sci. 6:2671-2676(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[6]"X-ray structure of the ZnII beta-Lactamase from Bacteroides fragilis in an orthorhombic crystal form."
Carfi A., Duee E., Soto R.-P., Galleni M., Frere J.-M., Dideberg O.
Acta Crystallogr. D 54:47-57(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: TAL2480.
[7]"Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution."
Fitzgerald P.M., Wu J.K., Toney J.H.
Biochemistry 37:6791-6800(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[8]"Structural consequences of the active site substitution Cys181 --> Ser in metallo-beta-lactamase from Bacteroides fragilis."
Li Z., Rasmussen B.A., Herzberg O.
Protein Sci. 8:249-252(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63556 Genomic DNA. Translation: AAA22904.1.
M34831 Genomic DNA. Translation: AAA22907.1.
PIRA35263. A44999.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7TX-ray1.85A/B18-249[»]
1A8TX-ray2.55A/B18-249[»]
1HLKX-ray2.50A/B21-247[»]
1KR3X-ray2.50A/B18-249[»]
1ZNBX-ray1.85A/B18-249[»]
2BMIX-ray2.00A/B18-249[»]
2ZNBX-ray2.15A/B18-249[»]
3ZNBX-ray2.70A/B18-249[»]
4ZNBX-ray2.65A/B18-249[»]
ProteinModelPortalP25910.
SMRP25910. Positions 20-249.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP25910.
ChEMBLCHEMBL4840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP25910.

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

EvolutionaryTraceP25910.

Entry information

Entry nameBLAB_BACFG
AccessionPrimary (citable) accession number: P25910
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 90 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