ID D6GR36_FILAD Unreviewed; 295 AA.
AC D6GR36;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:EFE28127.1};
GN OrderedLocusNames=HMPREF0389_00040 {ECO:0000313|EMBL:EFE28127.1};
OS Filifactor alocis (strain ATCC 35896 / CCUG 47790 / D40 B5) (Fusobacterium
OS alocis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Filifactor.
OX NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE28127.1, ECO:0000313|Proteomes:UP000007468};
RN [1] {ECO:0000313|Proteomes:UP000007468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., Izard J.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both thermally
CC unfolding and oxidatively damaged proteins from irreversible
CC aggregation. Plays an important role in the bacterial defense system
CC toward oxidative stress. {ECO:0000256|HAMAP-Rule:MF_00117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117}.
CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC involving the reactive cysteines. Under reducing conditions zinc is
CC 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}.
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DR EMBL; CP002390; EFE28127.1; -; Genomic_DNA.
DR RefSeq; WP_014262251.1; NC_016630.1.
DR AlphaFoldDB; D6GR36; -.
DR STRING; 546269.HMPREF0389_00040; -.
DR KEGG; faa:HMPREF0389_00040; -.
DR PATRIC; fig|546269.5.peg.625; -.
DR eggNOG; COG1281; Bacteria.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000007468; 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; 3.55.30.10; Hsp33 domain; 1.
DR Gene3D; 3.90.1280.10; HSP33 redox switch-like; 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 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 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00117};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00117};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00117};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00117}; Reference proteome {ECO:0000313|Proteomes:UP000007468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT DISULFID 238..240
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT DISULFID 271..274
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ SEQUENCE 295 AA; 32609 MW; 16E6196C304C858E CRC64;
MGRLLRAISD NKTINMIAID SKDMVEEARK VHQCTPVATA ALGRVITAGT MMGVMMKEKN
AKLTLQFKGD GPLGLLVCVS NSQGDAKGYI AHPEVNLPIR INDRKLDVSA GVGTKGTVSV
IRDLGLKEPY IGQYPLTNGE IAEDLTAYYA NSEQVPSSVA LGVLVDVDGT VKSAGGFIVQ
LMPDASEEDI EILERNLRGV LSISHMLDEA ERLEQIMEVI LGELGMNVVE ERQTRYFCDC
SRERMERALI SLGRYELEQL LMEDGQAELT CHFCNNRYLF QEKDLKELIL ASRPK
//
