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Q59401 (Q59401_ENTCL) Unreviewed, UniProtKB/TrEMBL

Last modified April 5, 2011. Version 50. Feed History...

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

Protein names
EC=3.5.2.6 EMBL BAA07922.1
OrganismEnterobacter cloacae EMBL BAA07922.1
Taxonomic identifier550 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

Ontologies

Keywords
   DomainSignal EMBL BAA07922.1
   Molecular functionHydrolase EMBL BAA07922.1
   Technical term3D-structure PDB 1GA0 PDB 1ONH PDB 1Q2Q
Gene Ontology (GO)
   Biological processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

   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

Signal peptide1 – 2020 Potential EMBL BAA07922.1
Chain21 – 384364class C beta-lactamase EMBL BAA07922.1
PRO_5000139888

Sequences

Sequence LengthMass (Da)Tools
Q59401 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B3BC13B02531372F

FASTA38441,612
        10         20         30         40         50         60 
MMKKSLCCAL LLGISCSALA TPVSEKQLAE VVANTVTPLM KAQSVPGMAV AVIYQGKPHY 

        70         80         90        100        110        120 
YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR GEISLDDPVT RYWPQLTGKQ 

       130        140        150        160        170        180 
WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS LLRFYQNWQP QWKPGTTRLY ANASIGLFGA 

       190        200        210        220        230        240 
LAVKPSGMPY EQAMTTRVLK PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR AVRVSPGMLD 

       250        260        270        280        290        300 
AQAYGVKTNV QDMANWVMAN MAPENVADAS LKQGIALAQS RYWRIGSMYQ GLGWEMLNWP 

       310        320        330        340        350        360 
VEANTVVEGS DSKVALAPLP VAEVNPPAPP VKASWVHKTG STGGFGSYVA FIPEKQIGIV 

       370        380 
MLANTSYPNP ARVEAAYHIL EALQ 

« Hide

References

[1]"Molecular evolution of a class C beta-lactamase extending its substrate specificity."
Nukaga M., Haruta S., Tanimoto K., Kogure K., Taniguchi K., Tamaki M., Sawai T.
J. Biol. Chem. 270:5729-5735(1995) [PubMed: 7890700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: GC1 EMBL BAA07922.1.
[2]"Biochemical characterization of type A and type B beta-lactamase from Enterobacter cloacae."
Then R.L., Charnas R.L., Kocher H.P., Manneberg M., Rothlisberger U., Stocker J.
Rev. Infect. Dis. 10:714-720(1988) [PubMed: 3263683] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone."
Crichlow G.V., Nukaga M., Doppalapudi V.R., Buynak J.D., Knox J.R.
Biochemistry 40:6233-6239(2001) [PubMed: 11371184] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 21-384.
[4]"Inhibition of class A and class C beta-lactamases by penems: crystallographic structures of a novel 1,4-thiazepine intermediate."
Nukaga M., Abe T., Venkatesan A.M., Mansour T.S., Bonomo R.A., Knox J.R.
Biochemistry 42:13152-13159(2003) [PubMed: 14609325] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 21-384.
[5]"Structure-activity relationship of 6-methylidene penems bearing tricyclic heterocycles as broad-spectrum beta-lactamase inhibitors: crystallographic structures show unexpected binding of 1,4-thiazepine intermediates."
Venkatesan A.M., Gu Y., Dos Santos O., Abe T., Agarwal A., Yang Y., Petersen P.J., Weiss W.J., Mansour T.S., Nukaga M., Hujer A.M., Bonomo R.A., Knox J.R.
J. Med. Chem. 47:6556-6568(2004) [PubMed: 15588091] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 22-384.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D44479 Genomic DNA. Translation: BAA07922.1.
PIRB60908.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GA0X-ray1.60A21-384[»]
1ONHX-ray1.38A21-384[»]
1Q2QX-ray1.40A22-384[»]
ProteinModelPortalQ59401.
SMRQ59401. Positions 22-384.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
Gene3DG3DSA:3.40.710.10. G3DSA:3.40.710.10. 1 hit.
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMSSF56601. PBP_transp_fold. 1 hit.
PROSITEPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ59401_ENTCL
AccessionPrimary (citable) accession number: Q59401
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 5, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)