BLAST Search Results

BLAST Search Results
Page 1 of 2
BLASTP 2.0.8 [Jan-05-1999]


Reference: Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schaffer, 
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997), 
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs",  Nucleic Acids Res. 25:3389-3402.

Query = blat_ecoli.sw
         (286 letters)

Database: pir
           142,080 sequences; 47,169,319 total letters

Sequence	Description	Score (Bits)	E Value
PIR1:PNECP alignment	beta-lactamase (EC 3.5.2.6) precursor - Escherichia ... 547 e-155	547	e-155
PIR4:I40905 alignment	beta-lactamase (EC 3.5.2.6) - synthetic 547 e-155	547	e-155
PIR4:S41975 alignment	beta-lactamase (EC 3.5.2.6) precursor - synthetic 545 e-155	545	e-155
PIR2:S47061 alignment	beta-lactamase (EC 3.5.2.6) - phage phi-X174 545 e-155	545	e-155
PIR2:S60312 alignment	extended spectrum beta-lactamase CAZ-7 - Klebsiella... 541 e-154	541	e-154
PIR2:S30113 alignment	beta-lactamase (EC 3.5.2.6) TEM-3 - Klebsiella pneu... 541 e-154	541	e-154
PIR2:S60310 alignment	extended spectrum beta-lactamase CAZ-2 - Klebsiella... 539 e-153	539	e-153
PIR2:S60311 alignment	beta-lactamase (EC 3.5.2.6) TEM-1 - Klebsiella pneu... 538 e-153	538	e-153
PIR2:JQ1546 alignment	Bla protein - Salmonella typhimurium plasmid NTP16 536 e-152	536	e-152
PIR2:A60679 alignment	beta-lactamase (EC 3.5.2.6) SHV-2 precursor - Salmo... 362 e-100	362	e-100
PIR2:S16146 alignment	beta-lactamase (EC 3.5.2.6) - Klebsiella pneumoniae 362 e-100	362	e-100
PIR1:A44998 alignment	beta-lactamase (EC 3.5.2.6) SHV-2 - Klebsiella ozae...	361	2e-99
PIR2:A35395 alignment	beta-lactamase (EC 3.5.2.6) 2A precursor - Klebsiel...	361	2e-99
PIR2:A37200 alignment	beta-lactamase (EC 3.5.2.6) SHV-3, cefotaxime resis...	360	4e-99
PIR2:A60632 alignment	beta-lactamase (EC 3.5.2.6) precursor - Klebsiella ...	359	5e-99
PIR1:A44996 alignment	beta-lactamase (EC 3.5.2.6) shv-1 precursor - Klebs...	354	2e-97
PIR2:S00464 alignment	beta-lactamase (EC 3.5.2.6) class A - Escherichia c...	353	3e-97
PIR2:S02434 alignment	beta-lactamase (EC 3.5.2.6) SHV-2 - Escherichia coli	351	1e-96
PIR2:A60448 alignment	beta-lactamase (EC 3.5.2.6) CAZ-5 - Klebsiella pneu...	348	1e-95
PIR2:A24469 alignment	beta-lactamase (EC 3.5.2.6) precursor - Klebsiella ...	346	5e-95
PIR1:A44958 alignment	beta-lactamase (EC 3.5.2.6) (OHIO-1) - Enterobacter...	337	3e-92
PIR2:A41381 alignment	beta-lactamase (EC 3.5.2.6) precursor - Proteus mir...	243	3e-64
PIR2:A35001 alignment	beta-lactamase (EC 3.5.2.6) PSE-4 precursor - Staph...	199	8e-51
PIR2:A49789 alignment	beta-lactamase (EC 3.5.2.6) PSE-1 - Pseudomonas aer...	198	2e-50
PIR2:JQ1136 alignment	beta-lactamase (EC 3.5.2.6) CARB-3 - Pseudomonas ae...	195	1e-49
PIR2:JS0755 alignment	beta-lactamase (EC 3.5.2.6) precursor - Proteus mir...	193	6e-49
PIR2:JH0268 alignment	beta-lactamase (EC 3.5.2.6) - Proteus mirabilis	189	9e-48
PIR2:S04649 alignment	beta-lactamase (EC 3.5.2.6) precursor - Rhodobacter...	189	1e-47
PIR2:S42075 alignment	beta-lactamase (EC 3.5.2.6) precursor - Klebsiella ...	186	6e-47
PIR2:S16553 alignment	beta-lactamase (EC 3.5.2.6) - Yersinia enterocolitica	186	6e-47
PIR2:G69674 alignment	beta-lactamase (EC 3.5.2.6) penP - Bacillus subtilis	185	1e-46
PIR2:S36188 alignment	beta-lactamase (EC 3.5.2.6) I precursor - Streptomy...	185	1e-46
PIR2:A54543 alignment	beta-lactamase (EC 3.5.2.6), cefotaxime-hydrolyzing...	185	2e-46
PIR2:S47330 alignment	penicillinase - Bacillus amyloliquefaciens	183	7e-46
PIR2:JC2566 alignment	bla protein - Pseudomonas aeruginosa (fragment)	180	3e-45
PIR1:B45822 alignment	beta-lactamase (EC 3.5.2.6) precursor - Streptomyce...	180	4e-45
PIR2:JP0074 alignment	beta-lactamase (EC 3.5.2.6), cefotaxime-hydrolyzing...	178	2e-44
PIR2:S06967 alignment	beta-lactamase (EC 3.5.2.6) precursor, indubible (c...	177	3e-44
PIR2:A60680 alignment	beta-lactamase (EC 3.5.2.6) ROB-1 precursor - Haemo...	177	3e-44
PIR2:A57002 alignment	beta-lactamase (EC 3.5.2.6) ROB-1 - Actinobacillus ...	177	3e-44
PIR2:A61156 alignment	beta-lactamase (EC 3.5.2.6) ROB1 - Pasteurella haem...	177	3e-44
PIR2:S23929 alignment	beta-lactamase (EC 3.5.2.6) - Klebsiella oxytoca	175	1e-43
PIR2:S03167 alignment	beta-lactamase (EC 3.5.2.6) precursor - Bacillus ce...	173	4e-43
PIR2:S19006 alignment	beta-lactamase (EC 3.5.2.6) class A precursor - Cit...	173	4e-43
PIR1:PNBSL alignment	beta-lactamase (EC 3.5.2.6) precursor - Bacillus lic...	171	3e-42
PIR2:A37148 alignment	beta-lactamase (EC 3.5.2.6) precursor (clone pDML51...	171	3e-42
PIR1:PNBS5B alignment	beta-lactamase (EC 3.5.2.6) I precursor - Bacillus ...	170	4e-42
PIR2:JC4117 alignment	beta-lactamase (EC 3.5.2.6) precursor - Bacillus th...	170	5e-42
PIR2:S49543 alignment	beta-lactamase (EC 3.5.2.6) class A precursor - Myc...	170	5e-42
PIR2:JN0520 alignment	beta-lactamase (EC 3.5.2.6) - Streptomyces cellulosae	169	6e-42


Run Parameters
  Database: pir
    Posted date:  Oct 27, 1999  4:34 AM
  Number of letters in database: 47,169,319
  Number of sequences in database:  142,080
  
Lambda     K      H
   0.319    0.135    0.399 

Gapped
Lambda     K      H
   0.270   0.0470    0.230 


Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 24309732
Number of Sequences: 142080
Number of extensions: 964797
Number of successful extensions: 3440
Number of sequences better than 10.0: 79
Number of HSP's better than 10.0 without gapping: 70
Number of HSP's successfully gapped in prelim test: 9
Number of HSP's that attempted gapping in prelim test: 3321
Number of HSP's gapped (non-prelim): 81
length of query: 286
length of database: 47169319
effective HSP length: 52
effective length of query: 234
effective length of database: 39781159
effective search space: 9308791206
effective search space used: 9308791206
T: 11
A: 40
X1: 16 ( 7.4 bits)
X2: 38 (14.8 bits)
X3: 64 (24.9 bits)
S1: 41 (21.8 bits)
S2: 66 (30.1 bits)

Input Sequence: blat_ecoli.sw

!!AA_SEQUENCE 1.0
ID   BLAT_ECOLI     STANDARD;      PRT;   286 AA.
AC   P00810;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   15-DEC-1999 (Rel. 39, Last annotation update)
DE   BETA-LACTAMASE PRECURSOR (EC 3.5.2.6) (TEM-1 TO TEM-5, TEM-8, TEM-16,
DE   TEM-24 AND IRT-4) (PENICILLINASE).
GN   BLA AND BLAT-3 AND BLAT-4 AND BLAT-5.
OS   Escherichia coli.
OG   Plasmid pBR322, Plasmid IncFII R100, Plasmid R6K, Plasmid pUD16,
OG   Plasmid pCFF04, and Plasmid pCFF14.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A. (TEM-1).
RC   TRANSPOSON=TN3; PLASMID=PBR322;
RX   MEDLINE; 79012484.
RA   SUTCLIFFE J.G.;
RT   "Nucleotide sequence of the ampicillin resistance gene of Escherichia
RT   coli plasmid pBR322.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:3737-3741(1978).
RN   [2]
RP   SEQUENCE FROM N.A. (TEM-1).
RC   TRANSPOSON=TN3; PLASMID=PBR322;
RX   MEDLINE; 80002802.
RA   SUTCLIFFE J.G.;
RT   "Complete nucleotide sequence of the Escherichia coli plasmid
RT   pBR322.";
RL   Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979).
RN   [3]
RP   SEQUENCE FROM N.A. (TEM-1).
RC   PLASMID=INCFII R100;
RX   MEDLINE; 86319522.
RA   OHTSUBO H., RYDER T.B., MAEDA Y., ARMSTRONG K., OHTSUBO E.;
RT   "DNA replication of the resistance plasmid R100 and its control.";
RL   Adv. Biophys. 21:115-133(1986).
RN   [4]
RP   SEQUENCE OF 24-286 (TEM-2).
RC   TRANSPOSON=TN1; PLASMID=R6K;
RX   MEDLINE; 79012483.
RA   AMBLER R.P., SCOTT G.K.;
RT   "Partial amino acid sequence of penicillinase coded by Escherichia
RT   coli plasmid R6K.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:3732-3736(1978).
RN   [5]
RP   SEQUENCE FROM N.A. (TEM-3).
RA   SOUGAKOFF W., GOUSSARD S., COURVALIN P.;
RT   "The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum
RT   cephalosporins, is derived from the TEM-2 penicillinase by two amino
RT   acid substitutions.";
RL   FEMS Microbiol. Lett. 56:343-348(1988).
RN   [6]
RP   SEQUENCE FROM N.A. (TEM-3).
RC   PLASMID=PCFF04;
RX   MEDLINE; 93062798.
RA   MABILAT C., LOURENCAO-VITAL J., GOUSSARD S., COURVALIN P.;
RT   "A new example of physical linkage between Tn1 and Tn21: the
RT   antibiotic multiple-resistance region of plasmid pCFF04 encoding
RT   extended-spectrum beta-lactamase TEM-3.";
RL   Mol. Gen. Genet. 235:113-121(1992).
RN   [7]
RP   SEQUENCE FROM N.A. (TEM-4 AND TEM-5).
RC   STRAIN=CB86134; PLASMID=PUD16, AND PCFF04;
RX   MEDLINE; 89378760.
RA   SOUGAKOFF W., PETIT A., GOUSSARD S., SIROT D., BURE A., COURVALIN P.;
RT   "Characterization of the plasmid genes blaT-4 and blaT-5 which encode
RT   the broad-spectrum beta-lactamases TEM-4 and TEM-5 in
RT   enterobacteriaceae.";
RL   Gene 78:339-348(1989).
RN   [8]
RP   SEQUENCE FROM N.A. (TEM-8; TEM-16 AND TEM-24).
RX   MEDLINE; 93037315.
RA   CHANAL C., POUPART M.C., SIROT D., LABIA R., SIROT J., CLUZEL R.;
RT   "Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase
RT   genes.";
RL   Antimicrob. Agents Chemother. 36:1817-1820(1992).
RN   [9]
RP   SEQUENCE OF 24-286 (IRT-4).
RC   STRAIN=PEY;
RX   MEDLINE; 94333751.
RA   BRUN T., PEDUZZI J., CANICA M.M., PAUL G., NEVOT P., BARTHELEMY M.,
RA   LABIA R.;
RT   "Characterization and amino acid sequence of IRT-4, a novel TEM-type
RT   enzyme with a decreased susceptibility to beta-lactamase
RT   inhibitors.";
RL   FEMS Microbiol. Lett. 120:111-117(1994).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TEM-1.
RX   MEDLINE; 92183921.
RA   JELSCH C., LENFANT F., MASSON J.-M., SAMAMA J.-P.;
RT   "Beta-lactamase TEM1 of E. coli. Crystal structure determination at
RT   2.5-A resolution.";
RL   FEBS Lett. 299:135-142(1992).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF TEM-1.
RX   MEDLINE; 93361453.
RA   JELSCH C., MOUREY L., MASSON J.-M., SAMAMA J.-P.;
RT   "Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A
RT   resolution.";
RL   Proteins 16:364-383(1993).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TEM-1 COMPLEXED WITH BLIP.
RX   MEDLINE; 96186252.
RA   STRYNADKA N.C.J., JENSEN S.E., ALZARI P.M., JAMES M.N.G.;
RT   "A potent new mode of beta-lactamase inhibition revealed by the 1.7 A
RT   X-ray crystallographic structure of the TEM-1-BLIP complex.";
RL   Nat. Struct. Biol. 3:290-297(1996).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF TEM-1.
RX   MEDLINE; 98153145.
RA   MAVEYRAUD L., PRATT R.F., SAMAMA J.-P.;
RT   "Crystal structure of an acylation transition-state analog of the
RT   TEM-1 beta-lactamase. Mechanistic implications for class A beta-
RT   lactamases.";
RL   Biochemistry 37:2622-2628(1998).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF TEM-1.
RX   MEDLINE; 99352177.
RA   SWAREN P., GOLEMI D., CABANTOUS S., BULYCHEV A., MAVEYRAUD L.,
RA   MOBASHERY S., SAMAMA J.-P.;
RT   "X-ray structure of the Asn276Asp variant of the Escherichia coli
RT   TEM-1 beta-lactamase: direct observation of electrostatic modulation
RT   in resistance to inactivation by clavulanic acid.";
RL   Biochemistry 38:9570-9576(1999).
CC   -!- FUNCTION: TEM-TYPE ARE THE MOST PREVALENT BETA-LACTAMASES IN
CC       ENTEROBACTERIA.
CC   -!- FUNCTION: TEM-3 AND TEM-4 ARE CAPABLE OF HYDROLYZING CEFOTAXIME
CC       AND CEFTAZIDIME.
CC   -!- FUNCTION: TEM-5 IS CAPABLE OF HYDROLYZING CEFTAZIDIME.
CC   -!- FUNCTION: TEM-8 (OR CAZ-2); TEM-16 (OR CAZ-7) AND TEM-24 (CAZ-6)
CC       ARE MARKEDLY ACTIVE AGAINST CEFTAZIDIME.
CC   -!- FUNCTION: IRT-4 SHOWS RESISTANCE TO BETA-LACTAMASE INHIBITORS.
CC   -!- CATALYTIC ACTIVITY: A BETA-LACTAM + H(2)O = A SUBSTITUTED BETA-
CC       AMINO ACID.
CC   -!- SIMILARITY: BELONGS TO THE CLASS-A BETA-LACTAMASE FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J01749; AAB59737.1; -.
DR   EMBL; V00613; CAA23886.1; -.
DR   EMBL; X64523; CAA45828.1; -.
DR   EMBL; X65252; CAA46344.1; -.
DR   EMBL; X65253; CAA46345.1; -.
DR   EMBL; X65254; CAA46346.1; -.
DR   EMBL; U89928; AAB64386.1; -.
DR   EMBL; U66885; AAC48875.1; -.
DR   PIR; A01005; PNECP.
DR   PIR; S30113; S30113.
DR   PDB; 1BTL; 26-JAN-95.
DR   PDB; 1TEM; 15-MAY-97.
DR   PDB; 1XPB; 01-APR-97.
DR   PDB; 1AXB; 18-NOV-98.
DR   PDB; 1CK3; 18-AUG-99.
DR   SWISS-2DPAGE; P00810; COLI.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR   PFAM; PF00144; beta-lactamase; 1.
KW   Hydrolase; Antibiotic resistance; Plasmid; Transposable element;
KW   3D-structure; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    286       BETA-LACTAMASE.
FT   ACT_SITE     68     68
FT   BINDING     232    234       SUBSTRATE.
FT   DISULFID     75    121
FT   VARIANT      19     19       L -> F (IN TEM-4).
FT   VARIANT      37     37       Q -> K (IN TEM-2, TEM-3, TEM-8, TEM-16,
FT                                AND TEM-24).
FT   VARIANT      67     67       M -> L (IN IRT-4).
FT   VARIANT     102    102       E -> K (IN TEM-3, TEM-4 TEM-8, TEM-16,
FT                                AND TEM-24).
FT   VARIANT     162    162       R -> S (IN TEM-5, TEM-8, AND TEM-24).
FT   VARIANT     162    162       R -> H (IN TEM-16).
FT   VARIANT     235    235       A -> T (IN TEM-5 AND TEM-24).
FT   VARIANT     236    236       G -> S (IN TEM-3, TEM-4 AND TEM-8).
FT   VARIANT     237    237       E -> K (IN TEM-5 AND TEM-24).
FT   VARIANT     261    261       T -> M (IN TEM-4).
FT   VARIANT     272    272       N -> D (IN IRT-4).
SQ   SEQUENCE   286 AA;  31515 MW;  A26343B0 CRC32;

BLAT_ECOLI  Length: 286  April 7, 2000 11:57  Type: P  Check: 5209  ..

1  MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN

51  SGKILESFRP EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL

101  VEYSPVTEKH LTDGMTVREL CSAAITMSDN TAANLLLTTI GGPKELTAFL

151  HNMGDHVTRL DRWEPELNEA IPNDERDTTM PAAMATTLRK LLTGELLTLA

201  SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS RGIIAALGPD

251  GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW

Page 1