HSLO_THEMA
ID HSLO_THEMA Reviewed; 290 AA.
AC Q9X1B4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117};
DE AltName: Full=Heat shock protein 33 homolog {ECO:0000255|HAMAP-Rule:MF_00117};
DE Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117};
GN Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; OrderedLocusNames=TM_1394;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both thermally
CC unfolding and oxidatively damaged proteins from irreversible
CC aggregation. Plays an important role in the bacterial defense system
CC toward oxidative stress. {ECO:0000255|HAMAP-Rule:MF_00117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}.
CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC involving the reactive cysteines. Under reducing conditions zinc is
CC bound to the reactive cysteines and the protein is inactive.
CC {ECO:0000255|HAMAP-Rule:MF_00117}.
CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP-
CC Rule:MF_00117}.
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DR EMBL; AE000512; AAD36465.1; -; Genomic_DNA.
DR PIR; C72259; C72259.
DR RefSeq; NP_229195.1; NC_000853.1.
DR RefSeq; WP_004081604.1; NZ_CP011107.1.
DR PDB; 1VQ0; X-ray; 2.20 A; A/B=1-290.
DR PDBsum; 1VQ0; -.
DR AlphaFoldDB; Q9X1B4; -.
DR SMR; Q9X1B4; -.
DR STRING; 243274.THEMA_07345; -.
DR EnsemblBacteria; AAD36465; AAD36465; TM_1394.
DR KEGG; tma:TM1394; -.
DR eggNOG; COG1281; Bacteria.
DR InParanoid; Q9X1B4; -.
DR OMA; DMQCECC; -.
DR OrthoDB; 1406579at2; -.
DR EvolutionaryTrace; Q9X1B4; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd00498; Hsp33; 1.
DR Gene3D; 3.55.30.10; -; 1.
DR Gene3D; 3.90.1280.10; -; 1.
DR HAMAP; MF_00117; HslO; 1.
DR InterPro; IPR000397; Heat_shock_Hsp33.
DR InterPro; IPR016154; Heat_shock_Hsp33_C.
DR InterPro; IPR016153; Heat_shock_Hsp33_N.
DR PANTHER; PTHR30111; PTHR30111; 1.
DR Pfam; PF01430; HSP33; 1.
DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR SUPFAM; SSF118352; SSF118352; 1.
DR SUPFAM; SSF64397; SSF64397; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome; Zinc.
FT CHAIN 1..290
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192220"
FT DISULFID 231..233
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 263..266
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:1VQ0"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 34..50
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 164..176
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1VQ0"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1VQ0"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1VQ0"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1VQ0"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:1VQ0"
SQ SEQUENCE 290 AA; 32541 MW; 22CD6658EA62692F CRC64;
MIYYGTMFDH KVRFSIVRMR EVVEEARNRH ALSYLATVVL GRALIGAALV TPWLAEKERW
TLDIEGNGPI RRVVAQSTSE FTVRGYVANP KVELPLNEKG KFDVAGAIGQ GVLRVVRDLG
LKTPFVSQVP LVSGEIAEDL AYYFAVSEQI PSAFSIGVLV DSDGVKIAGG FAVQIIDRTL
EQEKVEMIEK NIKNLPSISK LFQEAEPLDV LERIFGEKVG FVETAEIKYK CDCNREKAKN
ALLVLDKKEL EDMRKEGKGE VVCKWCNTRY VFSEEELEEL LKFKVDDSGS
