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O08498 (BLAB1_ELIME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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:
Carbapenem-hydrolyzing beta-lactamase BlaB-1

Short name=CHbetaL-1
EC=3.5.2.6
Alternative name(s):
Class B carbapenemase BlaB-1
Gene names
Name:blaB1
Synonyms:blaB
OrganismElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifier238 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

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

Hydrolyzes penicillins, cephalosporins (including cefoxitin), carbapenems and 6-beta-iodopenicillanate.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Cofactor

Binds 2 zinc ions per subunit By similarity.

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 – 2222 Ref.1
Chain23 – 249227Carbapenem-hydrolyzing beta-lactamase BlaB-1
PRO_0000016949

Sites

Metal binding981Zinc 1 By similarity
Metal binding1001Zinc 1 By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1611Zinc 1 By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2221Zinc 2 By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O08498 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 0F042B5126E338F6

FASTA24928,144
        10         20         30         40         50         60 
MLKKIKISLI LALGLTSLQA FGQENPDVKI EKLKDNLYVY TTYNTFNGTK YAANAVYLVT 

        70         80         90        100        110        120 
DKGVVVIDCP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH DDRAGGLEYF GKIGAKTYST 

       130        140        150        160        170        180 
KMTDSILAKE NKPRAQYTFD NNKSFKVGKS EFQVYYPGKG HTADNVVVWF PKEKVLVGGC 

       190        200        210        220        230        240 
IIKSADSKDL GYIGEAYVND WTQSVHNIQQ KFSGAQYVVA GHDDWKDQRS IQHTLDLINE 


YQQKQKASN 

« Hide

References

[1]"Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile."
Rossolini G.M., Franceschini N., Riccio M.L., Mercuri P.S., Perilli M., Galleni M., Frere J.-M., Amicosante G.
Biochem. J. 332:145-152(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-27, CHARACTERIZATION.
Strain: ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585.
[2]"Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum."
Bellais S., Aubert D., Naas T., Nordmann P.
Antimicrob. Agents Chemother. 44:1878-1886(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PINT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96858 Genomic DNA. Translation: CAA65601.1.
AF189298 Genomic DNA. Translation: AAF89154.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2XX-ray1.50A/B/C/D27-245[»]
ProteinModelPortalO08498.
SMRO08498. Positions 27-245.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1667692.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13428.

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

EvolutionaryTraceO08498.

Entry information

Entry nameBLAB1_ELIME
AccessionPrimary (citable) accession number: O08498
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 76 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