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P62593

- BLAT_ECOLX

UniProt

P62593 - BLAT_ECOLX

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Protein

Beta-lactamase TEM

Gene

bla

more
Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei68 – 681Acyl-ester intermediate
Active sitei166 – 1661Proton acceptor

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-lactam antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

SABIO-RKP62593.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:bla
AND
Name:blaT-3
AND
Name:blaT-4
AND
Name:blaT-5
AND
Name:blaT-6
Encoded oniPlasmid R1 (R7268)2 Publications
Plasmid IncFII R100 (NR1)1 Publication
Plasmid R6K1 Publication
Plasmid pUD161 Publication
Plasmid pCFF042 Publications
Plasmid pCFF140 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Biotechnological usei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 286263Beta-lactamase TEMPRO_0000016978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 121

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP62593.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
P358042EBI-1031989,EBI-1031985From a different organism.

Protein-protein interaction databases

IntActiP62593. 1 interaction.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3814Combined sources
Beta strandi40 – 489Combined sources
Turni49 – 513Combined sources
Beta strandi54 – 596Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8314Combined sources
Helixi97 – 993Combined sources
Helixi107 – 1093Combined sources
Turni111 – 1133Combined sources
Helixi117 – 12610Combined sources
Helixi130 – 13910Combined sources
Helixi143 – 15210Combined sources
Helixi166 – 1683Combined sources
Turni171 – 1733Combined sources
Helixi181 – 19313Combined sources
Beta strandi194 – 1974Combined sources
Helixi199 – 21012Combined sources
Beta strandi213 – 2153Combined sources
Turni216 – 2183Combined sources
Helixi219 – 2224Combined sources
Beta strandi228 – 2358Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2499Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi255 – 2639Combined sources
Beta strandi264 – 2663Combined sources
Helixi268 – 28417Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXBX-ray2.00A24-286[»]
1BT5X-ray1.80A24-286[»]
1BTLX-ray1.80A24-286[»]
1CK3X-ray2.28A24-284[»]
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[»]
ProteinModelPortaliP62593.
SMRiP62593. Positions 24-286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62593.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni232 – 2343Substrate binding

Sequence similaritiesi

Belongs to the class-A beta-lactamase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62593 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN
60 70 80 90 100
SGKILESFRP EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL
110 120 130 140 150
VEYSPVTEKH LTDGMTVREL CSAAITMSDN TAANLLLTTI GGPKELTAFL
160 170 180 190 200
HNMGDHVTRL DRWEPELNEA IPNDERDTTM PAAMATTLRK LLTGELLTLA
210 220 230 240 250
SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS RGIIAALGPD
260 270 280
GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW
Length:286
Mass (Da):31,515
Last modified:July 21, 1986 - v1
Checksum:iBB678943BB18934B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191L → F in TEM-4.
Natural varianti37 – 371Q → K in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24.
Natural varianti67 – 671M → L in IRT-4.
Natural varianti102 – 1021E → K in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and TEM-24.
Natural varianti162 – 1621R → H in TEM-6 and TEM-16.
Natural varianti162 – 1621R → S in TEM-5, TEM-8 and TEM-24.
Natural varianti235 – 2351A → T in TEM-5 and TEM-24.
Natural varianti236 – 2361G → S in TEM-3, TEM-4 and TEM-8.
Natural varianti237 – 2371E → K in TEM-5 and TEM-24.
Natural varianti261 – 2611T → M in TEM-4.
Natural varianti272 – 2721N → D in IRT-4.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA93821. PNECP.
S30113.
RefSeqiNP_943295.1. NC_005248.1.
NP_957565.1. NC_005327.1.
YP_001096393.1. NC_009132.1.
YP_001693174.1. NC_010378.1.
YP_001816609.1. NC_010558.1.
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_023277.2.
YP_190222.1. NC_006671.1.

Genome annotation databases

GeneIDi10076131.
10076142.
13876868.
13877052.
13903673.
13905334.
13905363.
13906404.
13906709.
13906924.
13909533.
13909568.
14612524.
17500215.
17824300.
17824435.
18157686.
2716540.
3244915.
3722457.
4924718.
5961992.
6276043.
8319064.
8319163.
9537966.
9538101.
9846067.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A93821. PNECP.
S30113.
RefSeqi NP_943295.1. NC_005248.1.
NP_957565.1. NC_005327.1.
YP_001096393.1. NC_009132.1.
YP_001693174.1. NC_010378.1.
YP_001816609.1. NC_010558.1.
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_023277.2.
YP_190222.1. NC_006671.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AXB X-ray 2.00 A 24-286 [» ]
1BT5 X-ray 1.80 A 24-286 [» ]
1BTL X-ray 1.80 A 24-286 [» ]
1CK3 X-ray 2.28 A 24-284 [» ]
1ERM X-ray 1.70 A 24-286 [» ]
1ERO X-ray 2.10 A 24-286 [» ]
1ERQ X-ray 1.90 A 24-286 [» ]
1ESU X-ray 2.00 A 24-284 [» ]
1FQG X-ray 1.70 A 24-286 [» ]
1JTD X-ray 2.30 A 24-286 [» ]
1JTG X-ray 1.73 A/C 24-286 [» ]
1JVJ X-ray 1.73 A 24-286 [» ]
1JWP X-ray 1.75 A 24-286 [» ]
1JWV X-ray 1.85 A 24-286 [» ]
1JWZ X-ray 1.80 A 24-286 [» ]
1LHY X-ray 2.00 A 24-284 [» ]
1LI0 X-ray 1.61 A 24-284 [» ]
1LI9 X-ray 1.52 A 24-284 [» ]
1M40 X-ray 0.85 A 24-286 [» ]
1NXY X-ray 1.60 A 24-286 [» ]
1NY0 X-ray 1.75 A 24-286 [» ]
1NYM X-ray 1.20 A 24-286 [» ]
1NYY X-ray 1.90 A 24-286 [» ]
1PZO X-ray 1.90 A 24-284 [» ]
1PZP X-ray 1.45 A 24-284 [» ]
1S0W X-ray 2.30 A/B 24-286 [» ]
1TEM X-ray 1.95 A 24-286 [» ]
1XPB X-ray 1.90 A 24-286 [» ]
1XXM X-ray 1.90 A/B 24-286 [» ]
1YT4 X-ray 1.40 A 24-284 [» ]
1ZG4 X-ray 1.55 A 1-284 [» ]
1ZG6 X-ray 2.10 A 1-284 [» ]
2B5R X-ray 1.65 A/B 24-286 [» ]
2V1Z X-ray 1.60 A 25-286 [» ]
2V20 X-ray 1.67 A 25-286 [» ]
3C7U X-ray 2.20 A/C 24-286 [» ]
3C7V X-ray 2.07 A/C 24-286 [» ]
3CMZ X-ray 1.92 A 24-286 [» ]
3DTM X-ray 2.00 A 24-286 [» ]
3JYI X-ray 2.70 A/B/C/D/E/F 24-286 [» ]
3TOI X-ray 1.90 A/B 39-283 [» ]
4DXB X-ray 2.29 A/B 24-286 [» ]
4DXC X-ray 2.30 A 24-286 [» ]
4GKU X-ray 1.92 A 24-286 [» ]
4IBR X-ray 2.20 A 24-286 [» ]
4IBX X-ray 2.68 A/B/C/D/E 24-286 [» ]
4ID4 X-ray 1.05 A 24-147 [» ]
A 185-286 [» ]
ProteinModelPortali P62593.
SMRi P62593. Positions 24-286.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P62593. 1 interaction.

Chemistry

BindingDBi P62593.
ChEMBLi CHEMBL2364670.

Proteomic databases

PRIDEi P62593.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 10076131.
10076142.
13876868.
13877052.
13903673.
13905334.
13905363.
13906404.
13906709.
13906924.
13909533.
13909568.
14612524.
17500215.
17824300.
17824435.
18157686.
2716540.
3244915.
3722457.
4924718.
5961992.
6276043.
8319064.
8319163.
9537966.
9538101.
9846067.

Enzyme and pathway databases

SABIO-RK P62593.

Miscellaneous databases

EvolutionaryTracei P62593.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view ]
Pfami PF00144. Beta-lactamase. 1 hit.
[Graphical view ]
PRINTSi PR00118. BLACTAMASEA.
SUPFAMi SSF56601. SSF56601. 1 hit.
PROSITEi PS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    Plasmid: R1 (R7268)
  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.
    Plasmid: R1 (R7268)
  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).
    Plasmid: IncFII R100 (NR1)
  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.
    Plasmid: R6K
  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).
    Plasmid: pCFF04
  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.
    Plasmid: pCFF04 pUD16
  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.

Entry informationi

Entry nameiBLAT_ECOLX
AccessioniPrimary (citable) accession number: P62593
Secondary accession number(s): P00810, Q47313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3