ID H8L093_FRAAD Unreviewed; 299 AA.
AC H8L093;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Disulfide bond chaperone {ECO:0000313|EMBL:AFC87131.1};
GN OrderedLocusNames=Fraau_2795 {ECO:0000313|EMBL:AFC87131.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC87131.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003350; AFC87131.1; -; Genomic_DNA.
DR RefSeq; WP_014404134.1; NC_017033.1.
DR AlphaFoldDB; H8L093; -.
DR STRING; 767434.Fraau_2795; -.
DR KEGG; fau:Fraau_2795; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_0_0_6; -.
DR OrthoDB; 9793753at2; -.
DR Proteomes; UP000005234; Chromosome.
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:UP000005234};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 299 AA; 32993 MW; 18FCF53E21FB41CA CRC64;
MDTSLADDVL HRFVLERAGV RGVLVRLGPV WQEIAARAEY PAPLRQLLGQ SMAASALLTG
NIKLEGELSL ELKTNGPLRL LFAECTEQGR MRGLARWQGD LPEPLALNQL DGALMAITIG
NIDRGQRYQG LVGLEQAGLG PALEAYFAQS EQLPAKLLLA ADGEHAVGLM LQRMPGHGGH
EVEVDEDGWD RVRHLMATLG DEEALSVAPE VLLHRLFHEE QVQVFEARPL RFGCSCSRER
VQRMLRSLGR EEVEAALAVR DGEIEVICEF CAERYTFDRV DAEHLLTADL PAEVHPGVQ
//
