P62593 (BLAT_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	bla
AND
Name:	blaT-3
AND
Name:	blaT-4
AND
Name:	blaT-5
AND
Name:	blaT-6

Encoded on

Plasmid 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

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Antibiotic resistance
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing Plasmid Transposable element
Gene Ontology (GO)
Biological_process	beta-lactam antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	beta-lactamase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P35804	2	EBI-1031989,EBI-1031985	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.4 Ref.10

Chain

24 – 286

263

Beta-lactamase TEM

PRO_0000016978

Regions

Region

232 – 234

3

Substrate binding

Sites

Active site

68

1

Acyl-ester intermediate

Active site

166

1

Proton acceptor

Amino acid modifications

Disulfide bond

75 ↔ 121

Natural variations

Natural variant

19

1

L → F in TEM-4.

Natural variant

37

1

Q → K in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24.

Natural variant

67

1

M → L in IRT-4.

Natural variant

102

1

E → K in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and TEM-24.

Natural variant

162

1

R → H in TEM-6 and TEM-16.

Natural variant

162

1

R → S in TEM-5, TEM-8 and TEM-24.

Natural variant

235

1

A → T in TEM-5 and TEM-24.

Natural variant

236

1

G → S in TEM-3, TEM-4 and TEM-8.

Natural variant

237

1

E → K in TEM-5 and TEM-24.

Natural variant

261

1

T → M in TEM-4.

Natural variant

272

1

N → D in IRT-4.

Secondary structure

1

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286

Helix Strand Turn

Details...

Helix

25 – 38

14

Beta strand

40 – 48

9

Turn

49 – 51

3

Beta strand

54 – 59

6

Helix

67 – 69

3

Helix

70 – 83

14

Helix

97 – 99

3

Helix

107 – 109

3

Turn

111 – 113

3

Helix

117 – 126

10

Helix

130 – 139

10

Helix

143 – 152

10

Helix

166 – 168

3

Turn

171 – 173

3

Helix

181 – 193

13

Beta strand

194 – 197

4

Helix

199 – 210

12

Beta strand

213 – 215

3

Turn

216 – 218

3

Helix

219 – 222

4

Beta strand

228 – 235

8

Turn

237 – 239

3

Beta strand

241 – 249

9

Beta strand

250 – 252

3

Beta strand

255 – 263

9

Beta strand

264 – 266

3

Helix

268 – 284

17

Sequences

	Sequence		Length	Mass (Da)
	P62593 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: BB678943BB18934B	FASTA	286	31,515
	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

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.

PIR

PNECP. A93821.
S30113.

RefSeq

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_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_020278.1.
YP_190222.1. NC_006671.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	24-286	[»]
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	[»]

ProteinModelPortal

P62593.

SMR

P62593. Positions 24-286.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62593. 1 interaction.

Proteomic databases

PRIDE

P62593.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

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

Phylogenomic databases

ProtClustDB

PRK15442.

Enzyme and pathway databases

SABIO-RK

P62593.

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]

Pfam

PF00144. Beta-lactamase. 1 hit.
[Graphical view]

PRINTS

PR00118. BLACTAMASEA.

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

PROSITE

PS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62593.

ChEMBL

CHEMBL2065.

EvolutionaryTrace

P62593.

Entry information

Entry name

BLAT_ECOLX

Accession

Primary (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:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program