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P26918 (BLAB_AERHY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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

EC=3.5.2.6
Gene names
Name:cphA
OrganismAeromonas hydrophila
Taxonomic identifier644 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length254 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 By similarity.

Subunit structure

Monomer.

Subcellular location

Periplasm Probable.

Induction

By beta-lactam antibiotics.

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentPeriplasm
   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

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 2727 Potential
Chain28 – 254227Beta-lactamase
PRO_0000016941

Sites

Metal binding951Zinc 1 By similarity
Metal binding971Zinc 1 By similarity
Metal binding991Zinc 2 By similarity
Metal binding1741Zinc 1 By similarity
Metal binding1931Zinc 2 By similarity
Metal binding2311Zinc 2 By similarity

Secondary structure

............................................... 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26918 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 9D54760E17CF4B50

FASTA25428,016
        10         20         30         40         50         60 
MMKGWMKCGL AGAVVLMASF WGGSVRAAGM SLTQVSGPVY VVEDNYYVQE NSMVYFGAKG 

        70         80         90        100        110        120 
VTVVGATWTP DTARELHKLI KRVSRKPVLE VINTNYHTDR AGGNAYWKSI GAKVVSTRQT 

       130        140        150        160        170        180 
RDLMKSDWAE IVAFTRKGLP EYPDLPLVLP NVVHDGDFTL QEGKVRAFYA GPAHTPDGIF 

       190        200        210        220        230        240 
VYFPDEQVLY GNCILKEKLG NLSFADVKAY PQTLERLKAM KLPIKTVIGG HDSPLHGPEL 

       250 
IDHYEALIKA APQS 

« Hide

References

[1]"The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases."
Massidda O., Rossolini G.M., Satta G.
J. Bacteriol. 173:4611-4617(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AE036.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57102 Genomic DNA. Translation: CAA40386.1.
PIRS17287.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X8GX-ray1.70A28-254[»]
1X8HX-ray1.60A28-254[»]
1X8IX-ray1.90A28-254[»]
2GKLX-ray1.86A28-254[»]
2QDSX-ray1.66A28-254[»]
3F9OX-ray2.03A28-254[»]
3FAIX-ray1.70A28-254[»]
3IOFX-ray1.44A28-254[»]
3IOGX-ray1.41A28-254[»]
3SW3X-ray2.35A28-254[»]
3T9MX-ray2.03A28-254[»]
ProteinModelPortalP26918.
SMRP26918. Positions 28-251.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP26918.
ChEMBLCHEMBL1169593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP26918.

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

EvolutionaryTraceP26918.

Entry information

Entry nameBLAB_AERHY
AccessionPrimary (citable) accession number: P26918
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 84 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