(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 119.
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}.
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   SMR; P37565; -.
DR   STRING; 224308.BSU00710; -.
DR   jPOST; P37565; -.
DR   PaxDb; P37565; -.
DR   PRIDE; P37565; -.
DR   EnsemblBacteria; CAB11847; CAB11847; BSU00710.
DR   GeneID; 936762; -.
DR   KEGG; bsu:BSU00710; -.
DR   PATRIC; fig|224308.179.peg.71; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261703; -.
DR   InParanoid; P37565; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   PhylomeDB; P37565; -.
DR   BioCyc; BSUB:BSU00710-MONOMER; -.
DR   EvolutionaryTrace; P37565; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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;
DR   PRODOM; P37565.
DR   SWISS-2DPAGE; P37565.
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:0000244|PDB:1VZY"
FT   TURN            10..13
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          14..20
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           22..32
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           36..53
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          61..67
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          74..80
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          83..90
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           106..110
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          112..121
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          126..133
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          135..139
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           140..151
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          155..163
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          169..179
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           185..195
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           201..207
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           211..219
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          224..230
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           239..247
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           251..261
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          262..267
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   TURN            269..271
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   STRAND          274..278
FT                   /evidence="ECO:0000244|PDB:1VZY"
FT   HELIX           279..288
FT                   /evidence="ECO:0000244|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
//

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