HSLO_BACSU
ID HSLO_BACSU Reviewed; 291 AA.
AC P37565;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
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}; Synonyms=yacC;
GN OrderedLocusNames=BSU00710;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; D26185; BAA05306.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11847.1; -; Genomic_DNA.
DR PIR; S66101; S66101.
DR RefSeq; NP_387952.1; NC_000964.3.
DR RefSeq; WP_003226695.1; NZ_JNCM01000028.1.
DR PDB; 1VZY; X-ray; 1.97 A; A/B=1-291.
DR PDBsum; 1VZY; -.
DR AlphaFoldDB; P37565; -.
DR SMR; P37565; -.
DR STRING; 224308.BSU00710; -.
DR jPOST; P37565; -.
DR PaxDb; P37565; -.
DR PRIDE; P37565; -.
DR DNASU; 936762; -.
DR EnsemblBacteria; CAB11847; CAB11847; BSU_00710.
DR GeneID; 936762; -.
DR KEGG; bsu:BSU00710; -.
DR PATRIC; fig|224308.179.peg.71; -.
DR eggNOG; COG1281; Bacteria.
DR InParanoid; P37565; -.
DR OMA; DMQCECC; -.
DR PhylomeDB; P37565; -.
DR BioCyc; BSUB:BSU00710-MON; -.
DR EvolutionaryTrace; P37565; -.
DR Proteomes; UP000001570; 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..291
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192167"
FT DISULFID 235..237
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 268..271
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1VZY"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 36..53
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1VZY"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1VZY"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1VZY"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1VZY"
SQ SEQUENCE 291 AA; 31811 MW; 194F742BC0946DD5 CRC64;
MDYLVKALAY DGKVRAYAAR TTDMVNEGQR RHGTWPTASA ALGRTMTASL MLGAMLKGDD
KLTVKIEGGG PIGAIVADAN AKGEVRAYVS NPQVHFDLNE QGKLDVRRAV GTNGTLSVVK
DLGLREFFTG QVEIVSGELG DDFTYYLVSS EQVPSSVGVG VLVNPDNTIL AAGGFIIQLM
PGTDDETITK IEQRLSQVEP ISKLIQKGLT PEEILEEVLG EKPEILETMP VRFHCPCSKE
RFETAILGLG KKEIQDMIEE DGQAEAVCHF CNEKYLFTKE ELEGLRDQTT R
