!!AA_SEQUENCE 1.0
ID   LACI_ECOLI     STANDARD;      PRT;   360 AA.
AC   P03023; P71309; Q47338; O09196;
DT   21-JUL-1986 (Rel. 01, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   LACTOSE OPERON REPRESSOR.
GN   LACI.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 78246991.
RA   FARABAUGH P.J.;
RT   "Sequence of the lacI gene.";
RL   Nature 274:765-769(1978).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V.,
RA   RILEY M., COLLADO-VIDES J., GLASNER F.D., RODE C.K., MAYHEW G.F.,
RA   GREGOR J., DAVIS N.W., KIRKPATRICK H.A., GOEDEN M.A., ROSE D.J.,
RA   MAU B., SHAO Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RA   DUNCAN M., ALLEN E., ARAUJO R., APARICIO A.M., CHUNG E., DAVIS K.,
RA   FEDERSPIEL N., HYMAN R., KALMAN S., KOMP C., KURDI O., LEW H.,
RA   LIN D., NAMATH A., OEFNER P., ROBERTS D., SCHRAMM S., DAVIS R.W.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE FROM N.A.
RA   CHEN J., MATTHEWS K.K.S.M.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SEQUENCE FROM N.A.
RA   MARSH S.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SEQUENCE OF 1-147; 159-230 AND 233-360.
RX   MEDLINE; 76091932.
RA   BEYREUTHER K., ADLER K., FANNING E., MURRAY C., KLEMM A., GEISLER N.;
RT   "Amino-acid sequence of lac repressor from Escherichia coli.
RT   Isolation, sequence analysis and sequence assembly of tryptic
RT   peptides and cyanogen-bromide fragments.";
RL   Eur. J. Biochem. 59:491-509(1975).
RN   [7]
RP   SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347.
RX   MEDLINE; 73143730.
RA   PLATT T., FILES J.G., WEBER K.;
RT   "Lac repressor. Specific proteolytic destruction of the NH 2
RT   -terminal region and loss of the deoxyribonucleic acid-binding
RT   activity.";
RL   J. Biol. Chem. 248:110-121(1973).
RN   [8]
RP   SEQUENCE OF 60-70; 73-78 AND 83-86.
RX   MEDLINE; 74126378.
RA   GANEM D., MILLER J.H., FILES J.G., PLATT T., WEBER K.;
RT   "Reinitiation of a lac repressor fragment at a condon other than
RT   AUG.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973).
RN   [9]
RP   SEQUENCE OF 1-60 FROM N.A.
RX   MEDLINE; 88230449.
RA   GORDON A.J.E., BURNS P.A., FIX D.F., YATAGAI F., ALLEN F.L.,
RA   HORSFALL M.J., HALLIDAY J.A., GRAY J., BERNELOT-MOENS C.,
RA   GLICKMAN B.W.;
RT   "Missense mutation in the lacI gene of Escherichia coli. Inferences
RT   on the structure of the repressor protein.";
RL   J. Mol. Biol. 200:239-251(1988).
RN   [10]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 89113344.
RA   BOELENS R., LAMERICHS R.M.J.N., RULLMANN J.A.C., VAN BOOM J.H.,
RA   KAPTEIN R.;
RT   "The interaction of lac repressor headpiece with its operator: an NMR
RT   view.";
RL   Protein Seq. Data Anal. 1:487-498(1988).
RN   [11]
RP   STRUCTURE BY NMR.
RX   MEDLINE; 89302886.
RA   LAMERICHS R.M.J.N., BOELENS R., VAN DER MAREL G.A., VAN BOOM J.H.,
RA   KAPTEIN R., BUCK F., FERA B., RUTERJANS H.;
RT   "H NMR study of a complex between the lac repressor headpiece and a
RT   22 base pair symmetric lac operator.";
RL   Biochemistry 28:2985-2991(1989).
RN   [12]
RP   STRUCTURE BY NMR OF 1-56.
RX   MEDLINE; 96275660.
RA   SLIJPER M., BONVIN A.M., BOELENS R., KAPTEIN R.;
RT   "Refined structure of lac repressor headpiece (1-56) determined by
RT   relaxation matrix calculations from 2D and 3D NOE data: change of
RT   tertiary structure upon binding to the lac operator.";
RL   J. Mol. Biol. 259:761-773(1996).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS).
RX   MEDLINE; 96239623.
RA   LEWIS M., CHANG G., HORTON N.C., KERCHER M.A., PACE H.C.,
RA   SCHUMACHER M.A., BRENNAN R.G., LU P.;
RT   "Crystal structure of the lactose operon repressor and its complexes
RT   with DNA and inducer.";
RL   Science 271:1247-1254(1996).
RN   [14]
RP   MUTAGENESIS.
RX   MEDLINE; 90183956.
RA   LEHMING N., SARTORIUS J., KISTERS-WOIKE B., VON WILCKEN-BERGMANN B.,
RA   MUELLER-HILL B.;
RT   "Mutant lac repressors with new specificities hint at rules for
RT   protein-DNA recognition.";
RL   EMBO J. 9:615-621(1990).
RN   [15]
RP   MUTAGENESIS.
RX   MEDLINE; 94322386.
RA   MARKIEWICZ P., KLEINA L.G., CRUZ C., EHRET S., MILLER J.H.;
RT   "Genetic studies of the lac repressor. XIV. Analysis of 4000 altered
RT   Escherichia coli lac repressors reveals essential and non-essential
RT   residues, as well as 'spacers' which do not require a specific
RT   sequence.";
RL   J. Mol. Biol. 240:421-433(1994).
RN   [16]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE; 91249837.
RA   KISTERS-WOIKE B., LEHMING N., SARTORIUS J., VON WILCKEN-BERGMANN B.,
RA   MUELLER-HILL B.;
RT   "A model of the lac repressor-operator complex based on physical and
RT   genetic data.";
RL   Eur. J. Biochem. 198:411-419(1991).
CC   -!- FUNCTION: REPRESSOR OF THE LACTOSE OPERON. BINDS LACTOSE AS AN
CC       INDUCER.
CC   -!- SUBUNIT: HOMOTETRAMER.
CC   -!- MISCELLANEOUS: REMOVAL OF RESIDUES 1-59 AND 328-347 RESULTS IN THE
CC       MOLECULE LOSING ITS DNA-BINDING ACTIVITY WHILE MAINTAINING ITS
CC       INDUCER-BINDING ACTIVITY AND ITS TETRAMERIC STRUCTURE.
CC   -!- SIMILARITY: BELONGS TO THE LACI FAMILY OF TRANSCRIPTIONAL
CC       REGULATORS.
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; V00294; CAA23569.1; -.
DR   EMBL; J01636; AAA24052.1; -.
DR   EMBL; AE000141; AAC73448.1; -.
DR   EMBL; U73857; AAB18069.1; ALT_INIT.
DR   EMBL; X58469; CAA41383.1; -.
DR   EMBL; U86347; AAB47270.1; ALT_INIT.
DR   EMBL; U72488; AAB36549.1; -.
DR   EMBL; U78872; AAB37348.1; -.
DR   EMBL; U78873; AAB37351.1; -.
DR   EMBL; U78874; AAB37354.1; -.
DR   PIR; A03558; RPECL.
DR   PIR; S02540; S02540.
DR   PDB; 1LCC; 31-JAN-94.
DR   PDB; 1LCD; 31-JAN-94.
DR   PDB; 1LTP; 31-OCT-93.
DR   PDB; 1TLF; 31-JUL-95.
DR   PDB; 1LBG; 11-JUL-96.
DR   PDB; 1LBH; 11-JUL-96.
DR   PDB; 1LBI; 11-JUL-96.
DR   PDB; 1LQC; 12-FEB-97.
DR   ECO2DBASE; H039.0; 6TH EDITION.
DR   ECOGENE; EG10525; LACI.
DR   PFAM; PF00356; lacI; 1.
DR   PFAM; PF00532; Peripla_BP_like; 1.
DR   PROSITE; PS00356; HTH_LACI_FAMILY; 1.
KW   Transcription regulation; DNA-binding; Repressor; 3D-structure.
FT   DNA_BIND      6     25       H-T-H MOTIF.
FT   MUTAGEN      17     17       Y->H: BROADENING OF SPECIFICITY.
FT   MUTAGEN      22     22       R->N: RECOGNIZE AN OPERATOR VARIANT.
FT   VARIANT     282    282       Y -> D (IN T41 MUTANT).
FT   CONFLICT    286    286       S -> L (IN AAA24052, REF. 2, 4 AND 5).
FT   HELIX         6     13
FT   TURN         14     14
FT   HELIX        17     24
FT   HELIX        32     44
FT   TURN         49     50
SQ   SEQUENCE   360 AA;  38564 MW;  4CA5A1D6 CRC32;

LACI_ECOLI  Length: 360  February 27, 2002 12:33  Type: P  Check: 1946  ..

       1  MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN 

      51  RVAQQLAGKQ SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE 

     101  RSGVEACKAA VHNLLAQRVS GLIINYPLDD QDAIAVEAAC TNVPALFLDV 

     151  SDQTPINSII FSHEDGTRLG VEHLVALGHQ QIALLAGPLS SVSARLRLAG 

     201  WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT AMLVANDQMA 

     251  LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPSTTIK QDFRLLGQTS 

     301  VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA 

     351  RQVSRLESGQ