ID A0A0R2I233_9LACO Unreviewed; 297 AA.
AC A0A0R2I233;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ORFNames=IV45_GL001379 {ECO:0000313|EMBL:KRN59232.1};
OS Limosilactobacillus secaliphilus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=396268 {ECO:0000313|EMBL:KRN59232.1, ECO:0000313|Proteomes:UP000050934};
RN [1] {ECO:0000313|EMBL:KRN59232.1, ECO:0000313|Proteomes:UP000050934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17896 {ECO:0000313|EMBL:KRN59232.1,
RC ECO:0000313|Proteomes:UP000050934};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRN59232.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQBW01000005; KRN59232.1; -; Genomic_DNA.
DR RefSeq; WP_057739952.1; NZ_JQBW01000005.1.
DR AlphaFoldDB; A0A0R2I233; -.
DR STRING; 396268.IV45_GL001379; -.
DR PATRIC; fig|396268.3.peg.1400; -.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000050934; Unassembled WGS sequence.
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:UP000050934};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT DISULFID 240..242
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT DISULFID 273..276
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ SEQUENCE 297 AA; 32228 MW; 4E54A07B6A99B1F1 CRC64;
MADDYLVKSV AEHGMFRAYA VRATNLVEEA HKIHDTWSTA SAAFGRALIG TLLLSTSGLQ
GQEGMTVKIQ GNGPIGYMVI DGTAQGTVKG YLHNPHVNLP LNAKGKIDVS GGVGKQGILS
VTKMAPGDKT PYTGQVNLVS GELGDDFTYY LAQSEQIPSS VGLSVYVDDH DNVTMAGGFL
VQVLPGASDQ QIADLEKSIK SLPLVSKLLR DGKTPEDILK MIFKGKDLKI LDKMPVAYRC
DCSKERFAHA LASVSKKDLE AMINQDHGAE AVCQFCHKKY HFDEDELKKL LKEDQSK
//
