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P52663 (BLAN_ENTCL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:
Imipenem-hydrolyzing beta-lactamase

EC=3.5.2.6
Alternative name(s):
Carbapenemase
NMC-A
Gene names
Name:nmcA
OrganismEnterobacter cloacae
Taxonomic identifier550 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes carbapenems such as imipenem, which are extended-spectrum beta-lactam antibiotics.

Catalytic activity

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

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processbeta-lactam antibiotic 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 292265Imipenem-hydrolyzing beta-lactamase
PRO_0000017000

Regions

Region236 – 2383Substrate binding By similarity

Sites

Active site711Acyl-ester intermediate

Amino acid modifications

Disulfide bond70 ↔ 240

Secondary structure

...................................... 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52663 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4D33FD8669998F1B

FASTA29232,075
        10         20         30         40         50         60 
MSLNVKQSRI AILFSSCLIS ISFFSQANTK GIDEIKNLET DFNGRIGVYA LDTGSGKSFS 

        70         80         90        100        110        120 
YRANERFPLC SSFKGFLAAA VLKGSQDNRL NLNQIVNYNT RSLEFHSPIT TKYKDNGMSL 

       130        140        150        160        170        180 
GDMAAAALQY SDNGATNIIL ERYIGGPEGM TKFMRSIGDE DFRLDRWELD LNTAIPGDER 

       190        200        210        220        230        240 
DTSTPAAVAK SLKTLALGNI LSEHEKETYQ TWLKGNTTGA ARIRASVPSD WVVGDKTGSC 

       250        260        270        280        290 
GAYGTANDYA VVWPKNRAPL IISVYTTKNE KEAKHEDKVI AEASRIAIDN LK 

« Hide

References

[1]"Analysis of a carbapenem-hydrolyzing class A beta-lactamase from Enterobacter cloacae and of its LysR-type regulatory protein."
Naas T., Nordmann P.
Proc. Natl. Acad. Sci. U.S.A. 91:7693-7697(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-34.
Strain: NOR-1.
[2]"Inhibition of the broad spectrum nonmetallocarbapenamase of class A (NMC-A) beta-lactamase from Enterobacter cloacae by monocyclic beta-lactams."
Mourey L., Kotra L.P., Bellettini J., Bulychev A., O'Brien M., Miller M.J., Mobashery S., Samama J.-P.
J. Biol. Chem. 274:25260-25265(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
Strain: NOR-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21956 Genomic DNA. Translation: CAA79967.1.
PIRS35915.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUEX-ray1.64A28-292[»]
1BULX-ray1.89A28-292[»]
ProteinModelPortalP52663.
SMRP52663. Positions 28-292.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP52663.
ChEMBLCHEMBL4314.

Protein family/group databases

MEROPSS11.A01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP52663.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP52663.

Entry information

Entry nameBLAN_ENTCL
AccessionPrimary (citable) accession number: P52663
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 72 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