ID A0A1Y3A5L1_9GAMM Unreviewed; 290 AA.
AC A0A1Y3A5L1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Molecular chaperone Hsp33 {ECO:0000313|EMBL:OTE98238.1};
GN ORFNames=BCS42_02760 {ECO:0000313|EMBL:OTE98238.1};
OS Crenothrix sp. D3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=1880899 {ECO:0000313|EMBL:OTE98238.1, ECO:0000313|Proteomes:UP000198219};
RN [1] {ECO:0000313|EMBL:OTE98238.1, ECO:0000313|Proteomes:UP000198219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OTE98238.1};
RA Oswald K., Graf J.S., Littman S., Tienken D., Brand A., Wehrli B.,
RA Albertsen M., Daims H., Wagner M., Kuypers M.M., Schubert C.J., Milucka J.;
RT "Crenothrix are major methane consumers in stratified lakes.";
RL ISME J. 0:0-0(2017).
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:OTE98238.1}.
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DR EMBL; MBQZ01000008; OTE98238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3A5L1; -.
DR STRING; 1880899.BCS42_02760; -.
DR Proteomes; UP000198219; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 290 AA; 32772 MW; 57D435F73A2293D2 CRC64;
MIEQDFLRRF LFEELGVRGE WVNLTTSWQA AKQHQHLSTV EQQLLGQALV AVVMLSATIK
FKGSMILQAQ GDGDITTLVA QSTDERKIRG LLRSRGEVTA GSLESLFGQG RLVLTIDSGN
ANKPYQGIVP LQGEQLATAL ESYFEQSEQL NTRLWLFAND THAAGLLLQE LPAQAGDEAD
WQRIEMLANT ITEAELLALD CETLLYRLFH EEKVRLFDAE AVEFECRCSR QKIEKTLRAM
GREEMEELLE ERGSVEVICE FCSEHYQFDK VDVETFLLAE SVSHDSTTVH
//
