(data stored in ACNUC7421 zone)

SWISSPROT: C3MFB8_SINFN

ID   C3MFB8_SINFN            Unreviewed;       331 AA.
AC   C3MFB8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=33 kDa chaperonin {ECO:0000256|SAAS:SAAS00739901};
GN   Name=hslO {ECO:0000313|EMBL:ACP23955.1};
GN   OrderedLocusNames=NGR_c01530 {ECO:0000313|EMBL:ACP23955.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23955.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23955.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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.
CC       {ECO:0000256|SAAS:SAAS00739892}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00739897}.
CC   -!- SIMILARITY: Belongs to the HSP33 family.
CC       {ECO:0000256|SAAS:SAAS00739880}.
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DR   EMBL; CP001389; ACP23955.1; -; Genomic_DNA.
DR   RefSeq; WP_012706740.1; NC_012587.1.
DR   RefSeq; YP_002824708.1; NC_012587.1.
DR   STRING; 394.NGR_c01530; -.
DR   EnsemblBacteria; ACP23955; ACP23955; NGR_c01530.
DR   GeneID; 7790732; -.
DR   KEGG; rhi:NGR_c01530; -.
DR   PATRIC; fig|394.7.peg.2949; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261999; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   OrthoDB; POG091H01DJ; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
DR   Gene3D; 3.55.30.10; -; 1.
DR   Gene3D; 3.90.1280.10; -; 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.
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; C3MFB8.
DR   SWISS-2DPAGE; C3MFB8.
KW   Chaperone {ECO:0000256|SAAS:SAAS00739870};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00739859};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00739861};
KW   Redox-active center {ECO:0000256|SAAS:SAAS00739906};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Zinc {ECO:0000256|SAAS:SAAS00739879}.
SQ   SEQUENCE   331 AA;  36759 MW;  B348345235C63EA1 CRC64;
     MTETAPGLGE FDFAGDDHVV PFQVEGLDVR GRAVQLGPML DAILERHSYP LPVARLVAET
     VVLAVLLGTS LKFEGKLIVQ TQGDGPVDLV VADFSTPDRV RAYARYDEEA LAAAEKGGRT
     QPHELLGNGI LAFTIDQGVH TQRYQGIVAL DGATLEEIAA VYFRQSEQIP TKVRLAVAEL
     LDRDENGKPR HRWRAGGMVA QFLPEAPERM RQPDLPGGDG DDGDSSLLFD EDDLWAEAKV
     MVETIDIDEL TDPTVGTERL LYRLFHERGV RVYQPQAVYD RCSCSRDKIR EVLEGLSDED
     IEHSIEDGQI KVTCEFCSTN YRFEASEVRS Q
//

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