http://togogenome.org/gene/37331:H6H00_RS13480 ^@ http://purl.uniprot.org/uniprot/A0A7G7MPT7 ^@ Cofactor|||Function|||PTM|||Similarity|||Subcellular Location Annotation ^@ Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA.|||Belongs to the WhiB family.|||Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.|||Cytoplasm|||The Fe-S cluster can be nitrosylated by nitric oxide (NO).|||Upon Fe-S cluster removal intramolecular disulfide bonds are formed. http://togogenome.org/gene/37331:H6H00_RS12145 ^@ http://purl.uniprot.org/uniprot/A0A7G7MP55 ^@ 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. http://togogenome.org/gene/37331:H6H00_RS12300 ^@ http://purl.uniprot.org/uniprot/A0A7G7MP82 ^@ Function|||Similarity|||Subcellular Location Annotation|||Subunit ^@ Belongs to the IF-1 family.|||Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.|||Cytoplasm|||One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. http://togogenome.org/gene/37331:H6H00_RS12500 ^@ http://purl.uniprot.org/uniprot/A0A7G7MPB6 ^@ Caution ^@ Lacks conserved residue(s) required for the propagation of feature annotation. http://togogenome.org/gene/37331:H6H00_RS12305 ^@ http://purl.uniprot.org/uniprot/A0A7G7MP83 ^@ Similarity ^@ Belongs to the bacterial ribosomal protein bL36 family.