ID   HSLO_ALKOO              Reviewed;         299 AA.
AC   A8MIA8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Clos_2003;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000853; ABW19540.1; -; Genomic_DNA.
DR   RefSeq; WP_012159849.1; NC_009922.1.
DR   AlphaFoldDB; A8MIA8; -.
DR   SMR; A8MIA8; -.
DR   STRING; 350688.Clos_2003; -.
DR   EnsemblBacteria; ABW19540; ABW19540; Clos_2003.
DR   KEGG; aoe:Clos_2003; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_9; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; 1406579at2; -.
DR   Proteomes; UP000000269; 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   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW   Reference proteome; Zinc.
FT   CHAIN           1..299
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_1000057783"
FT   DISULFID        238..240
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        271..274
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   299 AA;  32613 MW;  A6926BE6290A62E1 CRC64;
     MKNTVIRGTA ASNQIRVFVA NTTEMVAKAQ ELQMATPVAI AALGRTLTAT SMMGLMSKSE
     KEKITVNING GGPLGPIVVV GNSKGIVKGY VSHPHVEGSN LYPGKLDVGS AVGTDGTITV
     VKDLGLKEPY IGTYPLSTGE IAEDFAAYFA FSEQQPSGIA LGVLVDVDYT IKAAGGYIIQ
     VLPNIEEETL TKLESKLSTL EPITSIIDRI QDPEEILNHI LGEFEPVILE TYDVDFVCDC
     SEERLEQVLI SIGEKELTEI IEEDKQAELV CHFCNKKYHF DEEHLNKLRS EILNKNNNI