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P62593 (BLAT_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 78. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase TEM

EC=3.5.2.6
Alternative name(s):
IRT-4
Penicillinase
TEM-1
TEM-16/CAZ-7
TEM-2
TEM-24/CAZ-6
TEM-3
TEM-4
TEM-5
TEM-6
TEM-8/CAZ-2
Gene names
Name:bla
AND
Name:blaT-3
AND
Name:blaT-4
AND
Name:blaT-5
AND
Name:blaT-6
Encoded onPlasmid R1 (R7268) Ref.1 Ref.2
Plasmid IncFII R100 (NR1) Ref.3
Plasmid R6K Ref.4
Plasmid pUD16 Ref.7
Plasmid pCFF04 Ref.6 Ref.7
Plasmid pCFF14
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

Catalytic activity

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

Biotechnological use

This protein is used as a marker in many commonly used cloning vectors, such as pBR322 and the pUC series.

Miscellaneous

The beta-lactamase present on pBR322 was cloned from plasmid R1 (R7268).

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
Plasmid
Transposable element
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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P358042EBI-1031989,EBI-1031985From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.4 Ref.10
Chain24 – 286263Beta-lactamase TEM
PRO_0000016978

Regions

Region232 – 2343Substrate binding

Sites

Active site681Acyl-ester intermediate
Active site1661Proton acceptor

Amino acid modifications

Disulfide bond75 ↔ 121

Natural variations

Natural variant191L → F in TEM-4.
Natural variant371Q → K in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24.
Natural variant671M → L in IRT-4.
Natural variant1021E → K in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and TEM-24.
Natural variant1621R → H in TEM-6 and TEM-16.
Natural variant1621R → S in TEM-5, TEM-8 and TEM-24.
Natural variant2351A → T in TEM-5 and TEM-24.
Natural variant2361G → S in TEM-3, TEM-4 and TEM-8.
Natural variant2371E → K in TEM-5 and TEM-24.
Natural variant2611T → M in TEM-4.
Natural variant2721N → D in IRT-4.

Secondary structure

................................................ 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62593 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: BB678943BB18934B

FASTA28631,515
        10         20         30         40         50         60 
MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP 

        70         80         90        100        110        120 
EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL 

       130        140        150        160        170        180 
CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM 

       190        200        210        220        230        240 
PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS 

       250        260        270        280 
RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW 

« Hide

References

[1]"Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322."
Sutcliffe J.G.
Proc. Natl. Acad. Sci. U.S.A. 75:3737-3741(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
Transposon: Tn3.
[2]"Complete nucleotide sequence of the Escherichia coli plasmid pBR322."
Sutcliffe J.G.
Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
Transposon: Tn3.
[3]"DNA replication of the resistance plasmid R100 and its control."
Ohtsubo H., Ryder T.B., Maeda Y., Armstrong K., Ohtsubo E.
Adv. Biophys. 21:115-133(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
[4]"Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K."
Ambler R.P., Scott G.K.
Proc. Natl. Acad. Sci. U.S.A. 75:3732-3736(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-286 (TEM-2).
Transposon: Tn1.
[5]"The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum cephalosporins, is derived from the TEM-2 penicillinase by two amino acid substitutions."
Sougakoff W., Goussard S., Courvalin P.
FEMS Microbiol. Lett. 56:343-348(1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
[6]"A new example of physical linkage between Tn1 and Tn21: the antibiotic multiple-resistance region of plasmid pCFF04 encoding extended-spectrum beta-lactamase TEM-3."
Mabilat C., Lourencao-Vital J., Goussard S., Courvalin P.
Mol. Gen. Genet. 235:113-121(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
[7]"Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae."
Sougakoff W., Petit A., Goussard S., Sirot D., Bure A., Courvalin P.
Gene 78:339-348(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-4 AND TEM-5).
Strain: CB86134.
[8]"An IS1-like element is responsible for high-level synthesis of extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae."
Goussard S., Sougakoff W., Mabilat C., Bauernfeind A., Courvalin P.
J. Gen. Microbiol. 137:2681-2687(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-6).
Strain: HB251.
[9]"Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes."
Chanal C., Poupart M.C., Sirot D., Labia R., Sirot J., Cluzel R.
Antimicrob. Agents Chemother. 36:1817-1820(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-8; TEM-16 AND TEM-24).
[10]"Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to beta-lactamase inhibitors."
Brun T., Peduzzi J., Canica M.M., Paul G., Nevot P., Barthelemy M., Labia R.
FEMS Microbiol. Lett. 120:111-117(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-286 (IRT-4).
Strain: PEY.
[11]"Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution."
Jelsch C., Lenfant F., Masson J.-M., Samama J.-P.
FEBS Lett. 299:135-142(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TEM-1.
[12]"Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A resolution."
Jelsch C., Mourey L., Masson J.-M., Samama J.-P.
Proteins 16:364-383(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF TEM-1.
[13]"A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex."
Strynadka N.C.J., Jensen S.E., Alzari P.M., James M.N.G.
Nat. Struct. Biol. 3:290-297(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TEM-1 COMPLEXED WITH BLIP.
[14]"Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases."
Maveyraud L., Pratt R.F., Samama J.-P.
Biochemistry 37:2622-2628(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF TEM-1.
[15]"X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid."
Swaren P., Golemi D., Cabantous S., Bulychev A., Maveyraud L., Mobashery S., Samama J.-P.
Biochemistry 38:9570-9576(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF TEM-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01749 Genomic DNA. Translation: AAB59737.1.
V00613 Genomic DNA. Translation: CAA23886.1.
X64523 Genomic DNA. Translation: CAA45828.1.
X57972 Genomic DNA. Translation: CAA41038.1.
X65252 Genomic DNA. Translation: CAA46344.1.
X65253 Genomic DNA. Translation: CAA46345.1.
X65254 Genomic DNA. Translation: CAA46346.1.
U89928 Genomic DNA. Translation: AAB64386.1.
U66885 Genomic DNA. Translation: AAC48875.1.
PIRPNECP. A93821.
S30113.
RefSeqNP_943295.1. NC_005248.1.
NP_957565.1. NC_005327.1.
YP_001096393.1. NC_009132.1.
YP_001693174.1. NC_010378.1.
YP_003108102.1. NC_013120.1.
YP_003108210.1. NC_013121.1.
YP_003829069.1. NC_014383.1.
YP_003829170.1. NC_014384.1.
YP_003937675.1. NC_014615.1.
YP_004119720.1. NC_014843.1.
YP_004119734.1. NC_014843.1.
YP_006903139.1. NC_019047.1.
YP_006939984.1. NC_018994.1.
YP_006940092.1. NC_018995.1.
YP_006952181.1. NC_019056.1.
YP_006952421.1. NC_019062.1.
YP_006952427.1. NC_019063.1.
YP_006953479.1. NC_019073.1.
YP_006953762.1. NC_019088.1.
YP_006953988.1. NC_019091.1.
YP_006954235.1. NC_019095.1.
YP_007447512.1. NC_020278.2.
YP_008766498.1. NC_022742.1.
YP_008864019.1. NC_022992.1.
YP_008864686.1. NC_022996.1.
YP_008995211.1. NC_023277.1.
YP_190222.1. NC_006671.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXBX-ray2.00A24-286[»]
1BT5X-ray1.80A24-286[»]
1BTLX-ray1.80A24-286[»]
1CK3X-ray2.28A24-286[»]
1ERMX-ray1.70A24-286[»]
1EROX-ray2.10A24-286[»]
1ERQX-ray1.90A24-286[»]
1ESUX-ray2.00A24-284[»]
1FQGX-ray1.70A24-286[»]
1JTDX-ray2.30A24-286[»]
1JTGX-ray1.73A/C24-286[»]
1JVJX-ray1.73A24-286[»]
1JWPX-ray1.75A24-286[»]
1JWVX-ray1.85A24-286[»]
1JWZX-ray1.80A24-286[»]
1LHYX-ray2.00A24-284[»]
1LI0X-ray1.61A24-284[»]
1LI9X-ray1.52A24-284[»]
1M40X-ray0.85A24-286[»]
1NXYX-ray1.60A24-286[»]
1NY0X-ray1.75A24-286[»]
1NYMX-ray1.20A24-286[»]
1NYYX-ray1.90A24-286[»]
1PZOX-ray1.90A24-284[»]
1PZPX-ray1.45A24-284[»]
1S0WX-ray2.30A/B24-286[»]
1TEMX-ray1.95A24-286[»]
1XPBX-ray1.90A24-286[»]
1XXMX-ray1.90A/B24-286[»]
1YT4X-ray1.40A24-284[»]
1ZG4X-ray1.55A1-284[»]
1ZG6X-ray2.10A1-284[»]
2B5RX-ray1.65A/B24-286[»]
2V1ZX-ray1.60A25-286[»]
2V20X-ray1.67A25-286[»]
3C7UX-ray2.20A/C24-286[»]
3C7VX-ray2.07A/C24-286[»]
3CMZX-ray1.92A24-286[»]
3DTMX-ray2.00A24-286[»]
3JYIX-ray2.70A/B/C/D/E/F24-286[»]
3TOIX-ray1.90A/B39-283[»]
4DXBX-ray2.29A/B24-286[»]
4DXCX-ray2.30A24-286[»]
4GKUX-ray1.92A24-286[»]
4IBRX-ray2.20A24-286[»]
4IBXX-ray2.68A/B/C/D/E24-286[»]
4ID4X-ray1.05A24-147[»]
A185-286[»]
ProteinModelPortalP62593.
SMRP62593. Positions 24-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62593. 1 interaction.

Chemistry

BindingDBP62593.
ChEMBLCHEMBL2364670.

Proteomic databases

PRIDEP62593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10076131.
10076142.
13876868.
13877052.
13903673.
13905334.
13905363.
13906404.
13906709.
13906924.
13909533.
13909568.
14612524.
17500215.
17824300.
17824435.
18157686.
2716540.
3244915.
3722457.
4924718.
5961992.
8319064.
8319163.
9537966.
9538101.
9846067.

Phylogenomic databases

ProtClustDBPRK15442.

Enzyme and pathway databases

SABIO-RKP62593.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62593.

Entry information

Entry nameBLAT_ECOLX
AccessionPrimary (citable) accession number: P62593
Secondary accession number(s): P00810, Q47313
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 19, 2014
This is version 78 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