Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05193 (AMPC_CITFR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 89. 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
Alternative name(s):
Cephalosporinase
Gene names
Name:ampC
Synonyms:blaC
OrganismCitrobacter freundii
Taxonomic identifier546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Enzyme regulation

Sulbactam is an effective progressive inhibitor but a poor competitive inhibitor.

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the class-C beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentPeriplasm
   DomainSignal
   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 mutant phenotype PubMed 21627834. Source: CACAO

   Cellular_componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 381361Beta-lactamase
PRO_0000016957

Regions

Region335 – 3373Substrate binding By similarity

Sites

Active site841Acyl-ester intermediate
Active site1701Proton acceptor

Natural variations

Natural variant971R → A in strain: GN346.
Natural variant1431G → D in strain: GN346.
Natural variant1451V → I in strain: GN346.
Natural variant1501E → A in strain: GN346.
Natural variant1851S → P in strain: GN346.
Natural variant2241L → R in strain: GN346.
Natural variant2431V → L in strain: GN346.
Natural variant3251A → V in strain: GN346.
Natural variant3681A → V in strain: GN346.

Experimental info

Sequence conflict981I → T Ref.3

Secondary structure

.................................................................. 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05193 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 3F955F6933F0D76B

FASTA38141,975
        10         20         30         40         50         60 
MMKKSICCAL LLTASFSTFA AAKTEQQIAD IVNRTITPLM QEQAIPGMAV AIIYEGKPYY 

        70         80         90        100        110        120 
FTWGKADIAN NHPVTQQTLF ELGSVSKTFN GVLGGDRIAR GEIKLSDPVT KYWPELTGKQ 

       130        140        150        160        170        180 
WRGISLLHLA TYTAGGLPLQ IPGDVTDKAE LLRFYQNWQP QWTPGAKRLY ANSSIGLFGA 

       190        200        210        220        230        240 
LAVKSSGMSY EEAMTRRVLQ PLKLAHTWIT VPQSEQKNYA WGYLEGKPVH VSPGQLDAEA 

       250        260        270        280        290        300 
YGVKSSVIDM ARWVQANMDA SHVQEKTLQQ GIELAQSRYW RIGDMYQGLG WEMLNWPLKA 

       310        320        330        340        350        360 
DSIINGSDSK VALAALPAVE VNPPAPAVKA SWVHKTGSTG GFGSYVAFVP EKNLGIVMLA 

       370        380 
NKSYPNPARV EAAWRILEKL Q 

« Hide

References

[1]"Sequence of the Citrobacter freundii OS60 chromosomal ampC beta-lactamase gene."
Lindberg F., Normark S.
Eur. J. Biochem. 156:441-445(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: OS60.
[2]"Role of lysine-67 in the active site of class C beta-lactamase from Citrobacter freundii GN346."
Tsukamoto K., Tachibana K., Yamazaki N., Ishii Y., Ujiie K., Nishida N., Sawai T.
Eur. J. Biochem. 188:15-22(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GN346.
[3]"Amino acid sequence, active-site residue, and effect of suicide inhibitors on cephalosporinase of Citrobacter freundii GN346."
Sawai T., Yamaguchi A., Tsukamoto K.
Rev. Infect. Dis. 10:721-725(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-381, INHIBITION BY SULBACTAM.
Strain: GN346.
[4]"Identification of the active site of Citrobacter freundii beta-lactamase using dansyl-penicillin."
Yamaguchi A., Adachi H., Sawai T.
FEBS Lett. 218:126-130(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 66-87.
[5]"Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis."
Oefner C., D'Arcy A.A., Daly J.J., Gubernator K., Charnas R.L., Heinze I., Hubschwerlen C., Winkler F.K.
Nature 343:284-288(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03866 Genomic DNA. Translation: CAA27494.1.
X51632 Genomic DNA. Translation: CAA35959.1.
PIRS08296.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RGYX-ray1.52A22-381[»]
ProteinModelPortalP05193.
SMRP05193. Positions 22-381.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP05193.
ChEMBLCHEMBL1255130.
DrugBankDB00355. Aztreonam.

Protein family/group databases

MEROPSS12.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP05193.

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. SSF56601. 1 hit.
PROSITEPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05193.

Entry information

Entry nameAMPC_CITFR
AccessionPrimary (citable) accession number: P05193
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: December 11, 2013
This is version 89 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