ID   A0A2A4VXG9_9PROT        Unreviewed;       323 AA.
AC   A0A2A4VXG9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   03-MAY-2023, entry version 12.
DE   SubName: Full=Hsp33 family molecular chaperone {ECO:0000313|EMBL:PCI62898.1};
GN   ORFNames=COB37_06175 {ECO:0000313|EMBL:PCI62898.1};
OS   Kordiimonadales bacterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales.
OX   NCBI_TaxID=2030814 {ECO:0000313|EMBL:PCI62898.1, ECO:0000313|Proteomes:UP000217879};
RN   [1] {ECO:0000313|Proteomes:UP000217879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PCI62898.1}.
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DR   EMBL; NVTU01000015; PCI62898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4VXG9; -.
DR   Proteomes; UP000217879; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00498; Hsp33; 1.
DR   Gene3D; 1.10.287.480; helix hairpin bin; 1.
DR   Gene3D; 3.55.30.10; Hsp33 domain; 1.
DR   Gene3D; 3.90.1280.10; HSP33 redox switch-like; 1.
DR   InterPro; IPR000397; Heat_shock_Hsp33.
DR   InterPro; IPR016154; Heat_shock_Hsp33_C.
DR   InterPro; IPR016153; Heat_shock_Hsp33_N.
DR   InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom_sf.
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   4: Predicted;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   323 AA;  35875 MW;  78D8A811B04CB648 CRC64;
     MTDTPIVVTD PADSRDNEVR PFQIEGLSDE MSVRGRAVRL GTVVDQVLKA HDYPDAVAKI
     LGEMLVLTGM LGSIMKFDGI VTIQTKSGGP VPMIVADYER REDGVGRLRG YADVDAKKLS
     VYGKNPSFNG LIGSKSGYLA LTIDQGENMK RYQGIVDLKG DTLSEVARNY FADSEQTPTE
     IRLHCDKDAV TGNWRAGGIM VQHLARGEEG RERILDRETE EQWNRASILM SSVKASELLD
     PMLDIDTLLM RLYHEDGVRV FEAGHMIHKC RCSRERLLSV LQGFSDDDIE HATEEGSIDV
     NCQFCNTTYV FTPKEARAGK KPA
//