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Database: UniProt
Entry: A0A1M4WNS4_9CLOT
LinkDB: A0A1M4WNS4_9CLOT
Original site: A0A1M4WNS4_9CLOT 
ID   A0A1M4WNS4_9CLOT        Unreviewed;       294 AA.
AC   A0A1M4WNS4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN05443638_11325 {ECO:0000313|EMBL:SHE82827.1};
OS   Clostridium fallax.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1533 {ECO:0000313|EMBL:SHE82827.1, ECO:0000313|Proteomes:UP000184035};
RN   [1] {ECO:0000313|EMBL:SHE82827.1, ECO:0000313|Proteomes:UP000184035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2631 {ECO:0000313|EMBL:SHE82827.1,
RC   ECO:0000313|Proteomes:UP000184035};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQVM01000013; SHE82827.1; -; Genomic_DNA.
DR   RefSeq; WP_072895913.1; NZ_UAVV01000002.1.
DR   AlphaFoldDB; A0A1M4WNS4; -.
DR   STRING; 1533.SAMN05443638_11325; -.
DR   OrthoDB; 9776534at2; -.
DR   Proteomes; UP000184035; 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:UP000184035};
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   294 AA;  31995 MW;  890D7EC6CACB99DE CRC64;
     MSDKILRATA KGGMVRIIAA DTRELVNEGV KLHNCTPTAA AALGRMLTAG TLMSAMAKGE
     KETLTLQING GGEAKGITVT AYSNNTVKGY IGNPEVDLPL NQKGKLDVSG AIGKEGSLVV
     IKDLGLKDPY VGQVPIYTGE IAEDLAYYFT VSEQTPSAVA LGVLVDKDLS IKSAGGFIIQ
     MMPGADELLA DLLMYRLQEV PSVTTMLSEG KTIKDILEVI FEDMDLKIND ELNPKYECDC
     SKEKVEKALI SIGYKDLKEI YDDNKDEELK CHFCNKSYKF THEDIGNLLK TLEK
//
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