ID G8PTJ6_PSEUV Unreviewed; 328 AA.
AC G8PTJ6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Hsp33-like chaperonin {ECO:0000313|EMBL:AEV36210.1};
GN OrderedLocusNames=PSE_1698 {ECO:0000313|EMBL:AEV36210.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV36210.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV36210.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV36210.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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DR EMBL; CP003147; AEV36210.1; -; Genomic_DNA.
DR RefSeq; WP_008549972.1; NC_016642.1.
DR AlphaFoldDB; G8PTJ6; -.
DR STRING; 911045.PSE_1698; -.
DR KEGG; psf:PSE_1698; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_0_1_5; -.
DR Proteomes; UP000005634; Chromosome.
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 328 AA; 35693 MW; 71A82D01C9244F0C CRC64;
MTNTPAQPTA AGVDAVVPFA VEALDVRGRV INMGPVLNSM LARHKYPAPV NKLLSEAIVL
TSMLGSTLKF EGRLTLQAQT DGAVSMLVVD FNAPDGLRAM AQFDEAKVAE VASKDGFKPD
QLLGKGHLAF TIDQGAHTSR YQGIVVLNGT TLEEAAHEYF QKSEQIPTFV RLGVAEVLTK
AEEGGAEHSW AAGGIMVQFL PQSLDRLRQA DIHPGDAPEG HEAHQVDEDD AWVEARSLVE
TVKDDELIDP SLTVEGLLYR LFHERGASVF SPQSMADKCT CSEEKITAMM QNFSDADKAE
MKAEGTVHIK CDFCSKDYEL DANKVFKD
//
