CH102_VIBCH
ID CH102_VIBCH Reviewed; 96 AA.
AC Q9KLC7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=VC_A0819;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE003853; AAF96717.1; -; Genomic_DNA.
DR PIR; C82412; C82412.
DR RefSeq; NP_233205.1; NC_002506.1.
DR RefSeq; WP_001026270.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KLC7; -.
DR SMR; Q9KLC7; -.
DR STRING; 243277.VC_A0819; -.
DR DNASU; 2612375; -.
DR EnsemblBacteria; AAF96717; AAF96717; VC_A0819.
DR GeneID; 57742197; -.
DR KEGG; vch:VC_A0819; -.
DR PATRIC; fig|243277.26.peg.3439; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_1_1_6; -.
DR OMA; LGIFEND; -.
DR BioCyc; VCHO:VCA0819-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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..96
FT /note="Co-chaperonin GroES 2"
FT /id="PRO_0000174892"
SQ SEQUENCE 96 AA; 10593 MW; A1004450991426AC CRC64;
MNIRPLHDKL IVERLEVENK SEGGIVLTSQ SVKKSNRGKV VAVGLGRPLK NGDRARMEVK
TGDQIIFNDG YGVKTEKVDG KEYLILSESD VLAIVE