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Database: UniProt
Entry: A0A1M5ZVV2_9BURK
LinkDB: A0A1M5ZVV2_9BURK
Original site: A0A1M5ZVV2_9BURK 
ID   A0A1M5ZVV2_9BURK        Unreviewed;       307 AA.
AC   A0A1M5ZVV2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Molecular chaperone Hsp33 {ECO:0000313|EMBL:SHI28053.1};
GN   ORFNames=SAMN04488135_11914 {ECO:0000313|EMBL:SHI28053.1};
OS   Pollutimonas bauzanensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pollutimonas.
OX   NCBI_TaxID=658167 {ECO:0000313|EMBL:SHI28053.1, ECO:0000313|Proteomes:UP000184226};
RN   [1] {ECO:0000313|EMBL:SHI28053.1, ECO:0000313|Proteomes:UP000184226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10190 {ECO:0000313|EMBL:SHI28053.1,
RC   ECO:0000313|Proteomes:UP000184226};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQXE01000019; SHI28053.1; -; Genomic_DNA.
DR   RefSeq; WP_073108925.1; NZ_FQXE01000019.1.
DR   AlphaFoldDB; A0A1M5ZVV2; -.
DR   STRING; 658167.SAMN04488135_11914; -.
DR   OrthoDB; 9793753at2; -.
DR   Proteomes; UP000184226; 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:UP000184226};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   307 AA;  34510 MW;  1866A9C6D610F96F CRC64;
     MTDQLKKYLL PDHSTRLQAV KLTSAWQAGL VHQHYPECVQ RLLGELVSAA VLLATNIKFD
     GSLVLQLQGD GPIALVVVEC TADLAIRATV TLREGHDIPA DGTLQSLLNA HGKGRFVVVL
     DPNRDTTDLE PYQGIVPLEG DSVAQVLELY MRNSEQLDTR IWLASDAENS AGLLLQRLPD
     HGGTTDEDHE SRDETWTRVR HLAATVKYGE LLELDSDTLI HRLFWEEDLI AFEPQQVRWH
     CPCTRERVAN MLRMLGREEI EDILSEREKI DISCNFCGKP YQFDAIDCAG LFLDNLDTAH
     SDHKSVH
//
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