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P85302 (AMPC_PSEFL) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-lactamase
EC=3.5.2.6
Alternative name(s):
Cephalosporinase
Gene names
Name:ampC
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid. Ref.2

Subcellular location

Periplasm Ref.2.

Sequence similarities

Belongs to the class-C beta-lactamase family.

Biophysicochemical properties

Kinetic parameters:

KM=120 µM for nitrocefin Ref.1 Ref.2

KM=116 µM for nitrocefin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0) Ref.1

KM=50 µM for cephalexin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0)

KM=2.3 µM for benzylpenicillin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0) Ref.1

KM=5.1 µM for ampicillin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0)

KM=3.7 µM for carbenicillin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0)

KM=0.118 µM for oxacillin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0)

KM=0.016 µM for cloxacillin (at 30 degrees Celsius in 50 mM sodium phosphate, pH 7.0)

Mass spectrometry

Molecular mass is 38723.1±4.9 Da from positions 1 - 358. Determined by ESI. Ref.1

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentPeriplasm
   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

   Cellular_componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Beta-lactamase
PRO_0000308487

Regions

Region311 – 3133Substrate binding By similarity UniProtKB P05364

Sites

Active site601Acyl-ester intermediate By similarity UniProtKB P05364
Active site1461Proton acceptor By similarity UniProtKB P05364

Secondary structure

1 ................................................................. 358
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P85302 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: C2C35CB71DF9E501

FASTA35838,728
        10         20         30         40         50         60 
ATDIRQVVDS TVEPLMQQQD IAGLSVAVIQ NGKAQYFNYG VANKDSKQPI TENTLFEIGS 

        70         80         90        100        110        120 
VSKTFTATLA GYALANGKLK LSDPASQYLP ALRGDKFDHI SLLNLGTYTA GGLPLQFPEE 

       130        140        150        160        170        180 
SDNTGKMISY YQHWKPAFAP GTQRLYSNPS IGLFGHLAAQ SLGQPFEKLM EQTVLPKLGL 

       190        200        210        220        230        240 
KHTFISVPET QMSLYAQGYD KAGKPVRVSP GALDAEAYGI KTSTSDLIHY VEVNMHPAKL 

       250        260        270        280        290        300 
EKPLQQAIAA THTGYYTVDG MTQGLGWEMY PYPIKVDALV EGNSTQMAME PHKVNWLTPP 

       310        320        330        340        350 
QAAPLDTLVN KTGSTGGFGA YVAYVPSKGL GVVILANKNY PNAERVKAAH AILSAMDQ

« Hide

References

[1]"Crystal structure of a cold-adapted class C beta-lactamase."
Michaux C., Massant J., Kerff F., Frere J.-M., Docquier J.-D., Vandenberghe I., Samyn B., Pierrard A., Feller G., Charlier P., Van Beeumen J., Wouters J.
FEBS J. 275:1687-1697(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
Strain: TAE 4.
[2]"Inducible class C beta-lactamases produced by psychrophilic bacteria."
Pierrard A., Ledent P., Docquier J.-D., Feller G., Gerday C., Frere J.-M.
FEMS Microbiol. Lett. 161:311-315(1998)
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZ6X-ray2.26A1-358[»]
ProteinModelPortalP85302.
SMRP85302. Positions 3-356.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMSSF56601. PBP_transp_fold. 1 hit.
PROSITEPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP85302.

Entry information

Entry nameAMPC_PSEFL
AccessionPrimary (citable) accession number: P85302
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: March 6, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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