ID A0A0W0VHY7_9GAMM Unreviewed; 283 AA.
AC A0A0W0VHY7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Heat shock protein 33 {ECO:0000313|EMBL:KTD19743.1};
GN Name=yrfI {ECO:0000313|EMBL:KTD19743.1};
GN ORFNames=Llon_1915 {ECO:0000313|EMBL:KTD19743.1};
OS Legionella londiniensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD19743.1, ECO:0000313|Proteomes:UP000054997};
RN [1] {ECO:0000313|EMBL:KTD19743.1, ECO:0000313|Proteomes:UP000054997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD19743.1,
RC ECO:0000313|Proteomes:UP000054997};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD19743.1}.
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DR EMBL; LNYK01000033; KTD19743.1; -; Genomic_DNA.
DR RefSeq; WP_058529890.1; NZ_UGON01000002.1.
DR AlphaFoldDB; A0A0W0VHY7; -.
DR STRING; 45068.Llon_1915; -.
DR PATRIC; fig|45068.5.peg.2081; -.
DR OrthoDB; 9793753at2; -.
DR Proteomes; UP000054997; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; helix hairpin bin; 1.
DR Gene3D; 3.55.30.10; Hsp33 domain; 1.
DR Gene3D; 3.90.1280.10; HSP33 redox switch-like; 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; 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 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000054997};
KW Stress response {ECO:0000313|EMBL:KTD19743.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 283 AA; 32968 MW; 66A2DAA07FFDBB3E CRC64;
MKLMKHDSLQ RFLFEHANIR GEIAYLNAAY QTIMKQHPYP PAIRRLLGEA LVSCLLLAGS
IKFQGEISLQ FHGDENLPLL LAQCDHELQI RGFAKYKEEG NLNEYHESFM QGKMVLTINQ
YNQPKAYQSV VPIRSVSMGE NVMYYFAQSE QISSRVWLAV NEHQAAGMLL QLMPGQDTAQ
KEEFWEYAVQ LGQTISEDEL LSLDNETILH RLYHETDIRL FEPRTVRFHC RCSREKMKQA
LTILGEEDLK QLLKEREQVE ITCEFCNQQY VFDAIDVAML FHK
//
