CH10_STRPN
ID CH10_STRPN Reviewed; 94 AA.
AC Q97NV3;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580}; OrderedLocusNames=SP_1907;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 -!- INTERACTION:
CC Q97NV3; P0A2W6: acpS; NbExp=2; IntAct=EBI-2206949, EBI-2207344;
CC Q97NV3; Q97SU1: adk; NbExp=2; IntAct=EBI-2206949, EBI-2206969;
CC Q97NV3; P63544: apt; NbExp=2; IntAct=EBI-2206949, EBI-2207316;
CC Q97NV3; Q54869: argS; NbExp=2; IntAct=EBI-2206949, EBI-2207421;
CC Q97NV3; Q9S400: aroA; NbExp=2; IntAct=EBI-2206949, EBI-2207276;
CC Q97NV3; P63588: aroD; NbExp=2; IntAct=EBI-2206949, EBI-2207290;
CC Q97NV3; Q97PR0: asnS; NbExp=2; IntAct=EBI-2206949, EBI-2207302;
CC Q97NV3; Q97R25: dapA; NbExp=2; IntAct=EBI-2206949, EBI-2207165;
CC Q97NV3; P95830: dnaJ; NbExp=2; IntAct=EBI-2206949, EBI-2207079;
CC Q97NV3; Q97QS2: eno; NbExp=2; IntAct=EBI-2206949, EBI-2207206;
CC Q97NV3; Q97SE6: gatA; NbExp=2; IntAct=EBI-2206949, EBI-2207039;
CC Q97NV3; Q97SE7: gatB; NbExp=2; IntAct=EBI-2206949, EBI-2207023;
CC Q97NV3; Q97SE5: gatC; NbExp=2; IntAct=EBI-2206949, EBI-2207053;
CC Q97NV3; P0A335: groEL; NbExp=2; IntAct=EBI-2206949, EBI-2207395;
CC Q97NV3; Q97NV3: groES; NbExp=2; IntAct=EBI-2206949, EBI-2206949;
CC Q97NV3; Q97S73: grpE; NbExp=2; IntAct=EBI-2206949, EBI-2207065;
CC Q97NV3; P65144: infC; NbExp=2; IntAct=EBI-2206949, EBI-2207149;
CC Q97NV3; A0A0H2UNP1: lacF-1; NbExp=2; IntAct=EBI-2206949, EBI-2207447;
CC Q97NV3; Q97RS9: lysS; NbExp=2; IntAct=EBI-2206949, EBI-2207121;
CC Q97NV3; P0A4T1: malR; NbExp=2; IntAct=EBI-2206949, EBI-2207435;
CC Q97NV3; Q97Q68: mecA; NbExp=2; IntAct=EBI-2206949, EBI-2207260;
CC Q97NV3; P41354: mutX; NbExp=2; IntAct=EBI-2206949, EBI-2207232;
CC Q97NV3; P65887: purA; NbExp=2; IntAct=EBI-2206949, EBI-2206955;
CC Q97NV3; P0CB75: pyrF; NbExp=2; IntAct=EBI-2206949, EBI-2207109;
CC Q97NV3; P65946: pyrR; NbExp=2; IntAct=EBI-2206949, EBI-2207248;
CC Q97NV3; Q97QV8: rex; NbExp=2; IntAct=EBI-2206949, EBI-2207177;
CC Q97NV3; Q97NX5: scpA; NbExp=2; IntAct=EBI-2206949, EBI-2207368;
CC Q97NV3; Q97NX6: scpB; NbExp=2; IntAct=EBI-2206949, EBI-2206697;
CC Q97NV3; P0A4J6: sodA; NbExp=2; IntAct=EBI-2206949, EBI-2207137;
CC Q97NV3; A0A0H2UPY3: SP_1103; NbExp=2; IntAct=EBI-2206949, EBI-2207193;
CC Q97NV3; P0A4S9: SP_1877; NbExp=2; IntAct=EBI-2206949, EBI-2207382;
CC Q97NV3; P05382: sulA; NbExp=2; IntAct=EBI-2206949, EBI-2206997;
CC Q97NV3; P22291: sulD; NbExp=2; IntAct=EBI-2206949, EBI-2207011;
CC Q97NV3; Q97PI4: thrS; NbExp=2; IntAct=EBI-2206949, EBI-2207332;
CC Q97NV3; P67049: thyA; NbExp=2; IntAct=EBI-2206949, EBI-2207093;
CC Q97NV3; Q97SR4: uppS; NbExp=2; IntAct=EBI-2206949, EBI-2206983;
CC Q97NV3; Q97QP2: xerS; NbExp=2; IntAct=EBI-2206949, EBI-2207218;
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; AE005672; AAK75977.1; -; Genomic_DNA.
DR PIR; H95222; H95222.
DR RefSeq; WP_000917330.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97NV3; -.
DR SMR; Q97NV3; -.
DR IntAct; Q97NV3; 36.
DR STRING; 170187.SP_1907; -.
DR EnsemblBacteria; AAK75977; AAK75977; SP_1907.
DR GeneID; 45219136; -.
DR GeneID; 66806977; -.
DR KEGG; spn:SP_1907; -.
DR eggNOG; COG0234; Bacteria.
DR OMA; EVKYSGE; -.
DR PhylomeDB; Q97NV3; -.
DR BioCyc; SPNE170187:G1FZB-1960-MON; -.
DR Proteomes; UP000000585; 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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm.
FT CHAIN 1..94
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174866"
SQ SEQUENCE 94 AA; 9912 MW; D0FBAD63EA9BB48F CRC64;
MLKPLGDRVV LKIEEKEQTV GGFVLAGSAQ EKTKTAQVVA TGQGVRTLNG DLVAPSVKTG
DRVLVEAHAG LDVKDGDEKY IIVGEANILA IIEE
