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Database: UniProt
Entry: A0A241WMX4_9GAMM
LinkDB: A0A241WMX4_9GAMM
Original site: A0A241WMX4_9GAMM 
ID   A0A241WMX4_9GAMM        Unreviewed;       291 AA.
AC   A0A241WMX4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Hsp33 family molecular chaperone {ECO:0000313|EMBL:OTG95552.1};
GN   ORFNames=B9T35_03150 {ECO:0000313|EMBL:OTG95552.1};
OS   Acinetobacter sp. ANC 3832.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG95552.1, ECO:0000313|Proteomes:UP000194704};
RN   [1] {ECO:0000313|EMBL:OTG95552.1, ECO:0000313|Proteomes:UP000194704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG95552.1,
RC   ECO:0000313|Proteomes:UP000194704};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-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:OTG95552.1}.
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DR   EMBL; NEGJ01000002; OTG95552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241WMX4; -.
DR   STRING; 1977874.B9T35_03150; -.
DR   OrthoDB; 9793753at2; -.
DR   Proteomes; UP000194704; 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   291 AA;  32798 MW;  79EAEF60A1A8C159 CRC64;
     MSDLRQRFYI EDSPVRGEVV HLEEALQTIL AQRDYAPAVQ ILLGEMLSAT ALLASTLKIK
     GRISLQIQAE GSLKWAMAEC NHLGQVRALA DYEEDSRFSH AENSSTVLSS LIKPVLFINI
     EPEHGERYQG IVPLDKPNLA GCLMQYYDLS AQIPTRIVLA STAKSSGGLL VQLLPRNNEE
     EQQLVDEDIW PRLTVLTETL KADELTQLDA QEILYRLYNE EEVRLPEVEQ LHFGCTCSRE
     RCTNALQQIG IDAVRETLEV QNPIEMDCQF CNSKYTFTAE EALSLFGEHL S
//
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