ID H0C125_9BURK Unreviewed; 330 AA.
AC H0C125;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Hsp33 protein {ECO:0000313|EMBL:EHL21680.1};
GN ORFNames=KYG_16852 {ECO:0000313|EMBL:EHL21680.1};
OS Acidovorax sp. NO-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL21680.1, ECO:0000313|Proteomes:UP000003485};
RN [1] {ECO:0000313|EMBL:EHL21680.1, ECO:0000313|Proteomes:UP000003485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NO-1 {ECO:0000313|EMBL:EHL21680.1,
RC ECO:0000313|Proteomes:UP000003485};
RX PubMed=22374962; DOI=10.1128/JB.06814-11;
RA Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL J. Bacteriol. 194:1635-1636(2012).
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DR EMBL; AGTS01000100; EHL21680.1; -; Genomic_DNA.
DR RefSeq; WP_008906026.1; NZ_AGTS01000100.1.
DR AlphaFoldDB; H0C125; -.
DR STRING; 512030.KYG_16852; -.
DR PATRIC; fig|512030.4.peg.3322; -.
DR OrthoDB; 9793753at2; -.
DR Proteomes; UP000003485; 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 Reference proteome {ECO:0000313|Proteomes:UP000003485};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 330 AA; 35919 MW; 20931B261E25437E CRC64;
MSELHKFLFD GLPVRGMIVR LTDAWTEILR VRAGNSATGA YPAPVSELLG EMAAAGVLMQ
SNIKFNGALV LQVFGDGPVK LAVAEVQSDL SLRATATING DVPDGARLSQ MVNVGGGGRC
AITLDPKDRH PGQQPYQGVV PLHGDHHEKL DRLSDVLQHY MLQSEQLDTI LVLGANEQVA
AGLLIQRMPI KGEGNLAAGL SHRENEDQIG HNEDYNRIAH LAASLTREEL LTLDVDTILH
RLFWEEKLLR FEPQQGASGP RFACTCSRER VSNMLRNLGA EEAESILAER EDIEVGCEFC
GQQYRFDAVD AAQIFVSPAV SQPPGPTGIQ
//
