Entry Information
Protein Name Bla
Accession No P62593
Protein description Beta-lactamase TEM
pI/Mw (Da)
Theoretical Experimental
5.46/28907 5.42/28618
Protein function and expression It hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics such as penicillins and cephalosporins.
Reference(s) Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)

Han, M. -J., K. J. Jeong, J. -S. Yoo, and S. Y. Lee. 2003. Engineering Escherichia coli for increased productivity of serine-rich proteins based on proteome profiling. Appl. Environ. Microbiol. 69:5772-5781. (NCBI)

2D gels information
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A A B B
pI/Mw: 5.42/28618

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
B
2-DE analysis of E. coli proteins from Nutropin production fermentation.
Map ID97
Reference(s)Han, M. -J., K. J. Jeong, J. -S. Yoo, and S. Y. Lee. 2003. Engineering Escherichia coli for increased productivity of serine-rich proteins based on proteome profiling. Appl. Environ. Microbiol. 69:5772-5781. (NCBI)
Protein function and expression(s)Map: F
Spot: 53
pI/Mw: 5.42/28618

F
2D gel of soluble protein fraction of BL21(DE3) (pEDob5 and pACYC104CysK), which overproduces leptin, 2h after induction.
Swiss-Prot Database Reference

Entry information
Entry Name BLAT_ECOLI
Primary accession number P62593
Secondary accession numbers P00810 Q47313 
Integrated into Swiss-Prot on 1986-07-21
Sequence was last modified on 1986-07-21 (Sequence version 1)
Annotations were last modified on 2006-07-25 (Entry version 25)
Name and origin of the protein
Protein name Beta-lactamase TEM precursor
Synonyms EC 3.5.2.6 Beta-lactamase TEM precursor
TEM-1
TEM-2
TEM-3
TEM-4
TEM-5
TEM-6
TEM-8/CAZ-2
TEM-16/CAZ-7
TEM-24/CAZ-6
IRT-4
Penicillinase
Gene name Name : blaName : blaT-3Name : blaT-4Name : blaT-5Name : blaT-6
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
plasmid = R1 (R7268)
transposon = Tn3
PubMed=358200[NCBI, ExPASy, EBI, Israel, Japan]
Sutcliffe J.G. ,
"Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322."
Proc. Natl. Acad. Sci. U.S.A.75:3737-3741(1978) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
plasmid = R1 (R7268)
transposon = Tn3
PubMed=383387[NCBI, ExPASy, EBI, Israel, Japan]
Sutcliffe J.G. ,
"Complete nucleotide sequence of the Escherichia coli plasmid pBR322."
Cold Spring Harb. Symp. Quant. Biol.43:77-90(1979) 
[3] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
plasmid = IncFII R100 (NR1)
DOI=10.1016/0065-227X(86)90018-3;PubMed=3019092[NCBI, ExPASy, EBI, Israel, Japan]
Ohtsubo H. , Ryder T.B. , Maeda Y. , Armstrong K. , Ohtsubo E. ,
"DNA replication of the resistance plasmid R100 and its control."
Adv. Biophys.21:115-133(1986) 
[4] PROTEIN SEQUENCE OF 24-286 (TEM-2).
plasmid = R6K
transposon = Tn1
PubMed=358199[NCBI, ExPASy, EBI, Israel, Japan]
Ambler R.P. , Scott G.K. ,
"Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K."
Proc. Natl. Acad. Sci. U.S.A.75:3732-3736(1978) 
[5] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
Sougakoff W. , Goussard S. , Courvalin P. ,
"The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum cephalosporins, is derived from the TEM-2 penicillinase by two amino acid substitutions."
FEMS Microbiol. Lett.56:343-348(1988) 
[6] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
plasmid = pCFF04
DOI=10.1007/BF00286188;PubMed=1331747[NCBI, ExPASy, EBI, Israel, Japan]
Mabilat C. , Lourencao-Vital J. , Goussard S. , Courvalin P. ,
"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."
Mol. Gen. Genet.235:113-121(1992) 
[7] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-4 AND TEM-5).
strain = CB86134
plasmid = pCFF04
plasmid = pUD16
DOI=10.1016/0378-1119(89)90236-9;PubMed=2550326[NCBI, ExPASy, EBI, Israel, Japan]
Sougakoff W. , Petit A. , Goussard S. , Sirot D. , Bure A. , Courvalin P. ,
"Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae."
Gene78:339-348(1989) 
[8] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-6).
strain = HB251
PubMed=1665171[NCBI, ExPASy, EBI, Israel, Japan]
Goussard S. , Sougakoff W. , Mabilat C. , Bauernfeind A. , Courvalin P. ,
"An IS1-like element is responsible for high-level synthesis of extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae."
J. Gen. Microbiol.137:2681-2687(1991) 
[9] NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-8; TEM-16 AND TEM-24).PubMed=1416873[NCBI, ExPASy, EBI, Israel, Japan]
Chanal C. , Poupart M.C. , Sirot D. , Labia R. , Sirot J. , Cluzel R. ,
"Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes."
Antimicrob. Agents Chemother.36:1817-1820(1992) 
[10] PROTEIN SEQUENCE OF 24-286 (IRT-4).
strain = PEY
DOI=10.1016/0378-1097(94)00186-3;PubMed=8056282[NCBI, ExPASy, EBI, Israel, Japan]
Brun T. , Peduzzi J. , Canica M.M. , Paul G. , Nevot P. , Barthelemy M. , Labia R. ,
"Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to beta-lactamase inhibitors."
FEMS Microbiol. Lett.120:111-117(1994) 
[11] X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TEM-1.DOI=10.1016/0014-5793(92)80232-6;PubMed=1544485[NCBI, ExPASy, EBI, Israel, Japan]
Jelsch C. , Lenfant F. , Masson J.-M. , Samama J.-P. ,
"Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution."
FEBS Lett.299:135-142(1992) 
[12] X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF TEM-1.DOI=10.1002/prot.340160406;PubMed=8356032[NCBI, ExPASy, EBI, Israel, Japan]
Jelsch C. , Mourey L. , Masson J.-M. , Samama J.-P. ,
"Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A resolution."
Proteins16:364-383(1993) 
[13] X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TEM-1 COMPLEXED WITH BLIP.PubMed=8605632[NCBI, ExPASy, EBI, Israel, Japan]
Strynadka N.C.J. , Jensen S.E. , Alzari P.M. , James M.N.G. ,
"A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex."
Nat. Struct. Biol.3:290-297(1996) 
[14] X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF TEM-1.DOI=10.1021/bi972501b;PubMed=9485412[NCBI, ExPASy, EBI, Israel, Japan]
Maveyraud L. , Pratt R.F. , Samama J.-P. ,
"Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases."
Biochemistry37:2622-2628(1998) 
[15] X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF TEM-1.DOI=10.1021/bi990758z;PubMed=10423234[NCBI, ExPASy, EBI, Israel, Japan]
Swaren P. , Golemi D. , Cabantous S. , Bulychev A. , Maveyraud L. , Mobashery S. , Samama J.-P. ,
"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."
Biochemistry38:9570-9576(1999) 
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 + H(2)O = a substituted beta-amino acid
  • BIOTECHNOLOGY : 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)
  • SIMILARITY : Belongs to the class-A beta-lactamase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL J01749;AAB59737.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    V00613;CAA23886.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X64523;CAA45828.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X57972;CAA41038.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X65252;CAA46344.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X65253;CAA46345.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X65254;CAA46346.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U89928;AAB64386.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U66885;AAC48875.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR A93821;PNECP.
    S30113;S30113.
    3D structure databases
    PDB 1AXB;X-ray;@=24-286[ExPASy/RCSB/EBI].
    1BT5;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1BTL;X-ray;@=24-286[ExPASy/RCSB/EBI].
    1CK3;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1ERM;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1ERO;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1ERQ;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1ESU;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1FQG;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1JTD;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1JTG;X-ray;A/C=24-286[ExPASy/RCSB/EBI].
    1JVJ;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1JWP;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1JWV;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1JWZ;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1LHY;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1LI0;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1LI9;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1M40;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1NXY;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1NY0;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1NYM;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1NYY;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1PZO;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1PZP;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1S0W;X-ray;A/B=-[ExPASy/RCSB/EBI].
    1TEM;X-ray;@=24-286[ExPASy/RCSB/EBI].
    1XPB;X-ray;@=24-286[ExPASy/RCSB/EBI].
    1XXM;X-ray;A/B=24-286[ExPASy/RCSB/EBI].
    1YT4;X-ray;A=24-286[ExPASy/RCSB/EBI].
    1ZG4;X-ray;A=1-286[ExPASy/RCSB/EBI].
    1ZG6;X-ray;A=1-286[ExPASy/RCSB/EBI].
    2B5R;X-ray;A/B=24-286[ExPASy/RCSB/EBI].
    Detailed list of linked structures
    ModBase P62593
    Protein-protein interaction databases
    DIP P62593
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR001466;Beta_lactamase.
    IPR000871;Beta_lactamase_A.
    IPR012338;PBP_tpept_fold.
    Graphical view of domain structure
    Pfam PF00144;Beta-lactamase;1.
    Pfam graphical view of domain structure
    PRINTS PR00118;BLACTAMASEA.
    BLOCKS P62593
    PROSITE PS00146;BETA_LACTAMASE_A;1.
    Other
    LinkHub P62593;-.
    ProtoNet P62593
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase; Plasmid; Signal; Transposable element;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    SIGNAL    1    23     23    
    CHAIN   24   286    263  Beta-lactamase TEM  PRO_0000016978
    REGION  232   234      3  Substrate binding  
    ACT_SITE   68    68    Acyl-ester intermediate  
    ACT_SITE  166   166    Proton acceptor  
    DISULFID   75   121     47    
    VARIANT   19    19    L -> F: (in TEM-4)  
    VARIANT   37    37    Q -> K: (in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24)  
    VARIANT   67    67    M -> L: (in IRT-4)  
    VARIANT  102   102    E -> K: (in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and TEM-24)  
    VARIANT  162   162    R -> H: (in TEM-6 and TEM-16)  
    VARIANT  162   162    R -> S: (in TEM-5, TEM-8 and TEM-24)  
    VARIANT  235   235    A -> T: (in TEM-5 and TEM-24)  
    VARIANT  236   236    G -> S: (in TEM-3, TEM-4 and TEM-8)  
    VARIANT  237   237    E -> K: (in TEM-5 and TEM-24)  
    VARIANT  261   261    T -> M: (in TEM-4)  
    VARIANT  272   272    N -> D: (in IRT-4)  
    HELIX   25    38     14    
    TURN   39    39      1    
    STRAND   40    48      9    
    TURN   49    51      3    
    STRAND   54    59      6    
    TURN   60    61      2    
    STRAND   62    62      1    
    STRAND   64    65      2    
    HELIX   67    83     17    
    TURN   84    85      2    
    STRAND   86    86      1    
    TURN   89    90      2    
    STRAND   92    93      2    
    HELIX   97    99      3    
    STRAND  102   102      1    
    TURN  105   106      2    
    HELIX  107   109      3    
    TURN  111   113      3    
    STRAND  115   116      2    
    HELIX  117   126     10    
    STRAND  127   127      1    
    HELIX  130   139     10    
    TURN  140   141      2    
    STRAND  142   142      1    
    HELIX  143   152     10    
    TURN  153   154      2    
    STRAND  156   157      2    
    TURN  164   165      2    
    HELIX  166   168      3    
    TURN  172   173      2    
    TURN  176   177      2    
    STRAND  178   179      2    
    HELIX  181   193     13    
    STRAND  194   194      1    
    TURN  195   196      2    
    STRAND  197   197      1    
    HELIX  199   210     12    
    STRAND  213   214      2    
    TURN  216   218      3    
    HELIX  219   222      4    
    TURN  225   226      2    
    STRAND  228   235      8    
    STRAND  237   237      1    
    TURN  238   239      2    
    STRAND  241   249      9    
    TURN  250   251      2    
    STRAND  255   263      9    
    HELIX  268   284     17    
    TURN  285   285      1    
    Sequence information
    Length: 286AA [This is the length of the unprocessed precursor] Molecular weight: 31515Da [This is the MW of the unprocessed precursor] CRC64: BB678943BB18934B[This is a checksum on the sequence]
            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
    P62593 in FASTA format