ID B1TEF1_9BURK Unreviewed; 316 AA.
AC B1TEF1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Hsp33 protein {ECO:0000313|EMBL:EDT38059.1};
GN ORFNames=BamMEX5DRAFT_6167 {ECO:0000313|EMBL:EDT38059.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT38059.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT38059.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT38059.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) 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:EDT38059.1}.
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DR EMBL; ABLK01000337; EDT38059.1; -; Genomic_DNA.
DR RefSeq; WP_006761905.1; NZ_ABLK01000337.1.
DR AlphaFoldDB; B1TEF1; -.
DR PATRIC; fig|396597.7.peg.1325; -.
DR Proteomes; UP000004814; 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 316 AA; 35022 MW; 1BEE429BD4AA13B7 CRC64;
MSDQLQKFMF NSAPVRGEIV SLRNTWQEVL SRRDYPAPVR TVLGEMMAAC ALLSANLKFH
GTLIMQIFGD GPVQMLVVQC SSDLSMRATA KFAGDAAQTI GDDTRFASLV NASGHGRCVI
TLDPAEKLPG QQPYQGIVPL NGVDGPLESV SQVLEHYMHH SEQLDTRLWL AADRDRAVGM
LLQKLPGDGG IVPRNAETDI DTWERVCTLG GTLSAKELLE VEPEVVFRRL FWQENVQHFE
PAGTRFQCSC SREKVGAMLR MLGRDEVDSV IVERGHVEIH CEFCNQRYEF DPVDVAQLFA
VPELATGITP ATGQRH
//
