ID B9E8U0_MACCJ Unreviewed; 291 AA.
AC B9E8U0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=MCCL_1901 {ECO:0000313|EMBL:BAH18608.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH18608.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH18608.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH18608.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH18608.1; -; Genomic_DNA.
DR RefSeq; WP_015912400.1; NC_011999.1.
DR AlphaFoldDB; B9E8U0; -.
DR STRING; 458233.MCCL_1901; -.
DR KEGG; mcl:MCCL_1901; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_9; -.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000001383; 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:UP000001383};
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 291 AA; 31758 MW; 00D7054192EBD71B CRC64;
MTQDYLVRAL AFNDEVRAFS VRTTNTVETA RQKHDTWRVG TAALGRTITA GAMMGAMLKN
EEKLTITING GGPLGQIVVD ANGKGEVRGY VENPHVEVES IRPGKMNVGA AVGANGFLRV
VKDIGMRDYF TGSTELHNGE IAEDFTYYFA TSEQVPSAVG LGVLCTPEEV TEAAGGFIIQ
LMPGASEETI SLLEERLANL TPISTLIDRG LSPEQVLEEV LGEDNIRILD QMPVEFKCNC
GREKFLAAIK GLGEAEIVSM IEEDHGAEVE CHFCRQQYHY SEEDLRALIA D
//
