ID   B0VLR0_ACIBS            Unreviewed;       291 AA.
AC   B0VLR0;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Heat shock protein HSP33 {ECO:0000313|EMBL:CAP02426.1};
GN   Name=hslO {ECO:0000313|EMBL:CAP02426.1};
GN   OrderedLocusNames=ABSDF3146 {ECO:0000313|EMBL:CAP02426.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02426.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP02426.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP02426.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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DR   EMBL; CU468230; CAP02426.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VLR0; -.
DR   KEGG; abm:ABSDF3146; -.
DR   HOGENOM; CLU_054493_0_0_6; -.
DR   Proteomes; UP000001741; 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   Stress response {ECO:0000313|EMBL:CAP02426.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   291 AA;  32793 MW;  D1BE29C9311AA74E CRC64;
     MSDLRQRFYI EDFPVRGEVV HLEEALKTIL AQCDYMPAVQ ILLGEMLSAT ALLASTLKIK
     GRISLQIQAN GSFKWAMAEC NHLGEVRALA DYETDPRFGE ATDSSTVLTA LVNPVLFINI
     EPEHGERYQG IVPLDQANLA GCLMQYYDLS AQIPTRIVLA STAQRSGGLL IQLLPRHDEE
     EQKLVDEDLW PRLTMLTETL KSEELTELSA NEILYRLYNE EEVRLPEVEH LKFGCTCSKE
     RCAKALIQIG VDAVHETLEA QNPIQMDCQF CNTRYEFTAE EALGLFGEHL S
//