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ID HSLO_ECOLI Reviewed; 292 AA.
AC P0A6Y5; P45803; Q2M766;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 05-FEB-2008, entry version 31.
DE 33 kDa chaperonin (Heat shock protein 33) (HSP33).
GN Name=hslO; Synonyms=yrfI; OrderedLocusNames=b3401, JW5692;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=99148267; PubMed=10025400; DOI=10.1016/S0092-8674(00)80547-4;
RA Jakob U., Muse W., Eser M., Bardwell J.C.A.;
RT "Chaperone activity with a redox switch.";
RL Cell 96:341-352(1999).
RN [4]
RP DISULFIDE BONDS.
RX MEDLINE=20317067; PubMed=10764757; DOI=10.1074/jbc.M001089200;
RA Barbirz S., Jakob U., Glocker M.O.;
RT "Mass spectrometry unravels disulfide bond formation as the mechanism
RT that activates a molecular chaperone.";
RL J. Biol. Chem. 275:18759-18766(2000).
CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both
CC thermally unfolding and oxidatively damaged proteins from
CC irreversible aggregation. Plays an important role in the bacterial
CC defense system toward oxidative stress.
CC -!- INTERACTION:
CC P0A6N1:tufA; NbExp=1; IntAct=EBI-562857, EBI-301077;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock.
CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC involving the reactive cysteines. Under reducing conditions zinc
CC is bound to the reactive cysteines and the protein is inactive.
CC -!- SIMILARITY: Belongs to the HSP33 family.
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DR EMBL; U18997; AAA58198.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76426.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP009048; BAE77890.1; -; Genomic_DNA.
DR PIR; D65135; D65135.
DR RefSeq; AP_004389.1; -.
DR RefSeq; NP_417860.2; -.
DR PDB; 1HW7; X-ray; 2.20 A; A=1-253.
DR PDB; 1I7F; X-ray; 2.70 A; A=1-292.
DR PDB; 1XJH; NMR; -; A=225-285.
DR PDBsum; 1HW7; -.
DR PDBsum; 1I7F; -.
DR PDBsum; 1XJH; -.
DR IntAct; P0A6Y5; -.
DR GeneID; 947178; -.
DR GenomeReviews; U00096_GR; b3401.
DR GenomeReviews; AP009048_GR; JW5692.
DR KEGG; ecj:JW5692; -.
DR KEGG; eco:b3401; -.
DR EchoBASE; EB2766; -.
DR EcoGene; EG12930; hslO.
DR BioCyc; EcoCyc:G7744-MON; -.
DR GO; GO:0005515; F:protein binding; IPI:IntAct.
DR HAMAP; MF_00117; -; 1.
DR InterPro; IPR000397; Hsp33.
DR Pfam; PF01430; HSP33; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Cytoplasm;
KW Redox-active center; Stress response; Zinc.
FT CHAIN 1 292 33 kDa chaperonin.
FT /FTId=PRO_0000192174.
FT DISULFID 230 232 Redox-active.
FT DISULFID 263 266 Redox-active.
FT STRAND 6 12
FT TURN 13 16
FT STRAND 17 23
FT HELIX 25 32
FT HELIX 39 56
FT STRAND 60 75
FT STRAND 77 83
FT STRAND 87 93
FT HELIX 104 108
FT STRAND 110 122
FT STRAND 125 131
FT STRAND 133 135
FT HELIX 136 147
FT STRAND 152 161
FT STRAND 164 174
FT HELIX 182 193
FT HELIX 197 202
FT HELIX 205 213
FT STRAND 218 220
SQ SEQUENCE 292 AA; 32534 MW; 18F05BD2F0257552 CRC64;
MPQHDQLHRY LFENFAVRGE LVTVSETLQQ ILENHDYPQP VKNVLAELLV ATSLLTATLK
FDGDITVQLQ GDGPMNLAVI NGNNNQQMRG VARVQGEIPE NADLKTLVGN GYVVITITPS
EGERYQGVVG LEGDTLAACL EDYFMRSEQL PTRLFIRTGD VDGKPAAGGM LLQVMPAQNA
QQDDFDHLAT LTETIKTEEL LTLPANEVLW RLYHEEEVTV YDPQDVEFKC TCSRERCADA
LKTLPDEEVD SILAEDGEID MHCDYCGNHY LFNAMDIAEI RNNASPADPQ VH
//