CH10_BACSU
ID CH10_BACSU Reviewed; 94 AA.
AC P28599; O08341;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 141.
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}, mopB;
GN OrderedLocusNames=BSU06020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1350777; DOI=10.1128/jb.174.12.3993-3999.1992;
RA Schmidt A., Schiesswohl M., Voelker U., Hecker M., Schumann W.;
RT "Cloning, sequencing, mapping, and transcriptional analysis of the groESL
RT operon from Bacillus subtilis.";
RL J. Bacteriol. 174:3993-3999(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1350776; DOI=10.1128/jb.174.12.3981-3992.1992;
RA Li M., Wong S.L.;
RT "Cloning and characterization of the groESL operon from Bacillus
RT subtilis.";
RL J. Bacteriol. 174:3981-3992(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1369494; DOI=10.1271/bbb.56.1995;
RA Tozawa Y., Yoshikawa H., Kawamura F., Itaya M., Takahashi H.;
RT "Isolation and characterization of the groES and groEL genes of Bacillus
RT subtilis Marburg.";
RL Biosci. Biotechnol. Biochem. 56:1995-2002(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-94.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=9455482; DOI=10.1093/dnares/4.5.335;
RA Kasahara Y., Nakai S., Ogasawara N., Yata K., Sadaie Y.;
RT "Sequence analysis of the groESL-cotA region of the Bacillus subtilis
RT genome, containing the restriction/modification system genes.";
RL DNA Res. 4:335-339(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [7]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
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 -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC Rule:MF_00580, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19726.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M84965; AAA22530.1; -; Genomic_DNA.
DR EMBL; M81132; AAA22502.1; -; Genomic_DNA.
DR EMBL; D10972; BAA22518.1; -; Genomic_DNA.
DR EMBL; D88802; BAA19726.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB007637; BAA22746.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12421.2; -; Genomic_DNA.
DR PIR; A41884; A41884.
DR RefSeq; NP_388483.2; NC_000964.3.
DR RefSeq; WP_003155970.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P28599; -.
DR SMR; P28599; -.
DR STRING; 224308.BSU06020; -.
DR jPOST; P28599; -.
DR PaxDb; P28599; -.
DR PRIDE; P28599; -.
DR EnsemblBacteria; CAB12421; CAB12421; BSU_06020.
DR GeneID; 64302471; -.
DR GeneID; 66327387; -.
DR GeneID; 938006; -.
DR KEGG; bsu:BSU06020; -.
DR PATRIC; fig|224308.179.peg.647; -.
DR eggNOG; COG0234; Bacteria.
DR InParanoid; P28599; -.
DR OMA; EVKYSGE; -.
DR PhylomeDB; P28599; -.
DR BioCyc; BSUB:BSU06020-MON; -.
DR PRO; PR:P28599; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Stress response.
FT CHAIN 1..94
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174698"
SQ SEQUENCE 94 AA; 10176 MW; B25C835957B16251 CRC64;
MLKPLGDRVV IELVESEEKT ASGIVLPDSA KEKPQEGKIV AAGSGRVLES GERVALEVKE
GDRIIFSKYA GTEVKYEGTE YLILRESDIL AVIG
