Belongs to the thioredoxin family. DsbA subfamily.
May be required for disulfide bond formation in some proteins.
Belongs to the bacterial ribosomal protein bL36 family.
Belongs to the bacterial ribosomal protein bL35 family.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the universal ribosomal protein uL14 family.
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8.
Belongs to the bacterial ribosomal protein bL33 family.
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.
Belongs to the bacterial ribosomal protein bS21 family.
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Belongs to the bacterial ribosomal protein bS18 family.
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6.