http://togogenome.org/gene/2051959:KFE12_RS07295 ^@ http://purl.uniprot.org/uniprot/A0A7W8IE64 ^@ Caution|||Function|||Similarity|||Subcellular Location Annotation|||Subunit ^@ Belongs to the peptidase S14 family.|||Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.|||Cytoplasm|||Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS20650 ^@ http://purl.uniprot.org/uniprot/A0A7W8IJK1 ^@ Caution|||Similarity ^@ Belongs to the bacterial ribosomal protein bS21 family.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS23195 ^@ http://purl.uniprot.org/uniprot/A0A7Y9NR14 ^@ Caution|||Similarity|||Subunit ^@ Belongs to the bacterial ribosomal protein bL17 family.|||Part of the 50S ribosomal subunit. Contacts protein L32.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS23115 ^@ http://purl.uniprot.org/uniprot/A0A7W8MSY1 ^@ Caution|||Cofactor|||Function|||Similarity|||Subunit ^@ Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.|||Binds 1 zinc ion per subunit.|||Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.|||Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS10350 ^@ http://purl.uniprot.org/uniprot/A0A7W8N144 ^@ Caution|||Subcellular Location Annotation ^@ Cytoplasm|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS23045 ^@ http://purl.uniprot.org/uniprot/A0A7W8JAJ7 ^@ Caution|||Function|||Similarity|||Subunit ^@ Belongs to the universal ribosomal protein uS10 family.|||Involved in the binding of tRNA to the ribosomes.|||Part of the 30S ribosomal subunit.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS04145 ^@ http://purl.uniprot.org/uniprot/A0A7W8J229 ^@ Caution ^@ The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS22435 ^@ http://purl.uniprot.org/uniprot/A0A7W8J0S6 ^@ Caution|||Similarity ^@ Belongs to the universal ribosomal protein uS9 family.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS13775 ^@ http://purl.uniprot.org/uniprot/A0A7W8ILF2 ^@ Caution|||Subcellular Location Annotation ^@ Cytoplasm|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. http://togogenome.org/gene/2051959:KFE12_RS06250 ^@ http://purl.uniprot.org/uniprot/A0A7Y9T5K8 ^@ Caution|||Function|||Similarity|||Subcellular Location Annotation|||Subunit ^@ Belongs to the GroES chaperonin family.|||Cytoplasm|||Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.|||The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.|||Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.