(data stored in ACNUC1104 zone)

SWISSPROT: D3UY43_XENBS

ID   D3UY43_XENBS            Unreviewed;       290 AA.
AC   D3UY43;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   RecName: Full=33 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00117};
DE   AltName: Full=Heat shock protein 33 homolog {ECO:0000256|HAMAP-Rule:MF_00117};
DE            Short=HSP33 {ECO:0000256|HAMAP-Rule:MF_00117};
GN   Name=hslO {ECO:0000256|HAMAP-Rule:MF_00117,
GN   ECO:0000313|EMBL:CBJ79221.1};
GN   OrderedLocusNames=XBJ1_0070 {ECO:0000313|EMBL:CBJ79221.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79221.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79221.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79221.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Redox regulated molecular chaperone. Protects both
CC       thermally unfolding and oxidatively damaged proteins from
CC       irreversible aggregation. Plays an important role in the bacterial
CC       defense system toward oxidative stress. {ECO:0000256|HAMAP-
CC       Rule:MF_00117, ECO:0000256|SAAS:SAAS01084509}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117,
CC       ECO:0000256|SAAS:SAAS01084524}.
CC   -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC       involving the reactive cysteines. Under reducing conditions zinc
CC       is bound to the reactive cysteines and the protein is inactive.
CC       {ECO:0000256|HAMAP-Rule:MF_00117}.
CC   -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00117, ECO:0000256|SAAS:SAAS01084516}.
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DR   EMBL; FN667741; CBJ79221.1; -; Genomic_DNA.
DR   RefSeq; WP_012986692.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0070; -.
DR   EnsemblBacteria; CBJ79221; CBJ79221; XBJ1_0070.
DR   GeneID; 8829696; -.
DR   KEGG; xbo:XBJ1_0070; -.
DR   PATRIC; fig|406818.4.peg.62; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261998; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   BioCyc; XBOV406818:XBJ1_RS00325-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00498; Hsp33; 1.
DR   Gene3D; 1.10.287.480; -; 1.
DR   Gene3D; 3.55.30.10; -; 1.
DR   Gene3D; 3.90.1280.10; -; 1.
DR   HAMAP; MF_00117; HslO; 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; PTHR30111; 1.
DR   Pfam; PF01430; HSP33; 1.
DR   PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR   SUPFAM; SSF118352; SSF118352; 1.
DR   SUPFAM; SSF64397; SSF64397; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY43.
DR   SWISS-2DPAGE; D3UY43.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084514};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084515};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084518};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Stress response {ECO:0000313|EMBL:CBJ79221.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00117, ECO:0000256|SAAS:SAAS01084517}.
FT   DISULFID    231    233       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00117}.
FT   DISULFID    264    267       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00117}.
SQ   SEQUENCE   290 AA;  32590 MW;  8AA43B8CFA7D0CA2 CRC64;
     MTKHDQLHRF LFESHSVRGE LVSVSETYQR MMENHHYPLP VQQLLGELLV ATSLLTATLK
     FNGDITVQIQ GDGPVRLAVI NGNNQQQMRG TARIDGDVDA ASSLRDMVGN GYMVITVTPT
     EGERYQGVVA LEGETLAECL DAYFKQSEQL PTRLFIRTGI LDGKMAAGGM LLQILPGAQE
     GSEDLLDHLV QLTATIKGEE LFTLDVKEIL HRLYHEEDVT LYEPQQVEFR CTCSHQRCAD
     TLVTLPDADL QEILLKDGKI DMECEFCGMH YIFNDKDISE IKIVKKELLH
//

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