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Database: UniProt
Entry: R7LRV8_9CLOT
LinkDB: R7LRV8_9CLOT
Original site: R7LRV8_9CLOT 
ID   R7LRV8_9CLOT            Unreviewed;       297 AA.
AC   R7LRV8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=33 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00117};
DE   AltName: Full=Heat shock protein 33 homolog {ECO:0000256|HAMAP-Rule:MF_00117};
DE            Short=HSP33 {ECO:0000256|HAMAP-Rule:MF_00117};
GN   Name=hslO {ECO:0000256|HAMAP-Rule:MF_00117};
GN   ORFNames=BN638_01129 {ECO:0000313|EMBL:CDE90102.1};
OS   Clostridium sp. CAG:389.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262801 {ECO:0000313|EMBL:CDE90102.1, ECO:0000313|Proteomes:UP000017978};
RN   [1] {ECO:0000313|EMBL:CDE90102.1, ECO:0000313|Proteomes:UP000017978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:389 {ECO:0000313|Proteomes:UP000017978};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:0000256|HAMAP-Rule:MF_00117}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00117}.
CC   -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00117}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE90102.1}.
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DR   EMBL; CBJV010000017; CDE90102.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7LRV8; -.
DR   STRING; 1262801.BN638_01129; -.
DR   Proteomes; UP000017978; Unassembled WGS sequence.
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; Hsp33 domain; 1.
DR   Gene3D; 3.90.1280.10; HSP33 redox switch-like; 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; 33 KDA CHAPERONIN; 1.
DR   PANTHER; PTHR30111:SF1; 33 KDA CHAPERONIN; 1.
DR   Pfam; PF01430; HSP33; 1.
DR   PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR   SUPFAM; SSF64397; Hsp33 domain; 1.
DR   SUPFAM; SSF118352; HSP33 redox switch-like; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00117};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00117};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_00117};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW   Rule:MF_00117}; Reference proteome {ECO:0000313|Proteomes:UP000017978};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT   DISULFID        238..240
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT   DISULFID        271..274
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   297 AA;  32282 MW;  DA860A21AE6E97C5 CRC64;
     MQDKIMKFLA YDGKISVVCT STTEVVEKAR QIHDLSPVAT AAFGRLLTIS AIMGNEMKSE
     KDKLTVQMKG NGPLGTMLVT SDNFPRVKGY VSNPVVDLPL NDMGKLDVGG AVGNAGFINV
     IKDIGLKEPY VGICPLISGE IAEDFAEYFA KSEQKNTAVA LGVLVDKNGV KSAGGYIITP
     MPDATDEEIS KIEQSIFKAG AISKMLDKNM TLSEIAKAVT GDENVQLIEE NITPVYECDC
     SKEHMEEGLA TLDKNVLKEM IEEDGKAELV CHFCNKKYEF SKEELEEILG KRINGGI
//
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