CH102_RHOBA
ID CH102_RHOBA Reviewed; 93 AA.
AC Q7TTZ0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Co-chaperonin GroES 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=Chaperonin-10 2 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Name=groES2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=groS2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN OrderedLocusNames=RB10627;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: Together with the chaperonin GroEL, plays an essential role
CC in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. GroES binds to the apical surface of the GroEL ring,
CC thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC Rule:MF_00580}.
CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC chaperonin GroEL. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC Rule:MF_00580}.
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DR EMBL; BX294152; CAD76884.1; -; Genomic_DNA.
DR RefSeq; NP_869523.1; NC_005027.1.
DR AlphaFoldDB; Q7TTZ0; -.
DR SMR; Q7TTZ0; -.
DR STRING; 243090.RB10627; -.
DR EnsemblBacteria; CAD76884; CAD76884; RB10627.
DR KEGG; rba:RB10627; -.
DR PATRIC; fig|243090.15.peg.5134; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_0_0; -.
DR InParanoid; Q7TTZ0; -.
DR OMA; KVFYRQW; -.
DR OrthoDB; 1965002at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 1.
DR HAMAP; MF_00580; CH10; 1.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..93
FT /note="Co-chaperonin GroES 2"
FT /id="PRO_0000174822"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 93 AA; 9984 MW; 48C1D346B6C25E34 CRC64;
MQPLGERIVV QREESETTTA GGIVLPDSAK EKPARGTVVA LGTGKLLDDG SRADFQLAAG
DRVLFSSYAG ETVEVDDTEY LLMREDDVLA VIE
