HSPS_METJA
ID HSPS_METJA Reviewed; 147 AA.
AC Q57733;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Small heat shock protein HSP16.5;
GN OrderedLocusNames=MJ0285;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=9689045; DOI=10.1073/pnas.95.16.9129;
RA Kim R., Kim K.K., Yokota H., Kim S.-H.;
RT "Small heat shock protein of Methanococcus jannaschii, a
RT hyperthermophile.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9129-9133(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=9707123; DOI=10.1038/29106;
RA Kim K.K., Kim R., Kim S.-H.;
RT "Crystal structure of a small heat-shock protein.";
RL Nature 394:595-599(1998).
CC -!- FUNCTION: Chaperone that confers thermal protection to other proteins.
CC -!- SUBUNIT: Homooligomer of 24 subunits. Forms a spherical shape.
CC -!- INTERACTION:
CC Q57733; Q57733: MJ0285; NbExp=2; IntAct=EBI-15555697, EBI-15555697;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; L77117; AAB98273.1; -; Genomic_DNA.
DR PIR; F64335; F64335.
DR RefSeq; WP_010869783.1; NC_000909.1.
DR PDB; 1SHS; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-147.
DR PDB; 4ELD; X-ray; 2.70 A; A/B=1-147.
DR PDB; 4I88; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-147.
DR PDBsum; 1SHS; -.
DR PDBsum; 4ELD; -.
DR PDBsum; 4I88; -.
DR AlphaFoldDB; Q57733; -.
DR SMR; Q57733; -.
DR DIP; DIP-48450N; -.
DR STRING; 243232.MJ_0285; -.
DR EnsemblBacteria; AAB98273; AAB98273; MJ_0285.
DR GeneID; 1451140; -.
DR KEGG; mja:MJ_0285; -.
DR eggNOG; arCOG01832; Archaea.
DR HOGENOM; CLU_046737_12_4_2; -.
DR InParanoid; Q57733; -.
DR OMA; SGKGFMP; -.
DR OrthoDB; 100198at2157; -.
DR PhylomeDB; Q57733; -.
DR EvolutionaryTrace; Q57733; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0043621; F:protein self-association; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IDA:CAFA.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
DR DisProt; DP00067; -.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..147
FT /note="Small heat shock protein HSP16.5"
FT /id="PRO_0000126060"
FT DOMAIN 36..147
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:4ELD"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4ELD"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:4ELD"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4ELD"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4ELD"
SQ SEQUENCE 147 AA; 16452 MW; 0A53C6981CFD4266 CRC64;
MFGRDPFDSL FERMFKEFFA TPMTGTTMIQ SSTGIQISGK GFMPISIIEG DQHIKVIAWL
PGVNKEDIIL NAVGDTLEIR AKRSPLMITE SERIIYSEIP EEEEIYRTIK LPATVKEENA
SAKFENGVLS VILPKAESSI KKGINIE
