UniProt functional annotation for P0AFG0



	UniProt functional annotation for P0AFG0

UniProt code: P0AFG0.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis (PubMed:32871103). Participates in transcription elongation, termination and antitermination. In the absence of Rho, increases the rate of transcription elongation by the RNAP, probably by partially suppressing pausing. In the presence of Rho, modulates most Rho-dependent termination events by interacting with the RNAP to render the complex more susceptible to the termination activity of Rho. May be required to overcome a kinetic limitation of Rho to function at certain terminators. Also involved in ribosomal RNA and phage lambda N-mediated transcriptional antitermination. {ECO:0000255|HAMAP-Rule:MF_00948, ECO:0000269|PubMed:10383769, ECO:0000269|PubMed:10820031, ECO:0000269|PubMed:14973028, ECO:0000269|PubMed:1532577, ECO:0000269|PubMed:1547498, ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:7505669, ECO:0000269|PubMed:7761393, ECO:0000269|PubMed:7868616, ECO:0000269|PubMed:8422985}.

Subunit: Monomer. Interacts with the transcription termination factor Rho and with RNAP. One NusG monomer forms a stable complex with a Rho hexamer. Binds directly, but weakly, to the core enzyme of RNAP. Also interacts with RpsJ (NusE). The rRNA transcription and antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits (PubMed:32871103). {ECO:0000255|HAMAP-Rule:MF_00948, ECO:0000269|PubMed:10820031, ECO:0000269|PubMed:1532577, ECO:0000269|PubMed:20413501, ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:8422985}.

Domain: The N-terminal domain interacts with RNAP and the C-terminal domain binds either to Rho or to RpsJ (NusE). These domains are separated by a flexible linker. {ECO:0000269|PubMed:20413501}.

Similarity: Belongs to the NusG family. {ECO:0000255|HAMAP- Rule:MF_00948}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis (PubMed:32871103). Participates in transcription elongation, termination and antitermination. In the absence of Rho, increases the rate of transcription elongation by the RNAP, probably by partially suppressing pausing. In the presence of Rho, modulates most Rho-dependent termination events by interacting with the RNAP to render the complex more susceptible to the termination activity of Rho. May be required to overcome a kinetic limitation of Rho to function at certain terminators. Also involved in ribosomal RNA and phage lambda N-mediated transcriptional antitermination. {ECO:0000255\|HAMAP-Rule:MF_00948, ECO:0000269\|PubMed:10383769, ECO:0000269\|PubMed:10820031, ECO:0000269\|PubMed:14973028, ECO:0000269\|PubMed:1532577, ECO:0000269\|PubMed:1547498, ECO:0000269\|PubMed:32871103, ECO:0000269\|PubMed:7505669, ECO:0000269\|PubMed:7761393, ECO:0000269\|PubMed:7868616, ECO:0000269\|PubMed:8422985}.


Subunit:		Monomer. Interacts with the transcription termination factor Rho and with RNAP. One NusG monomer forms a stable complex with a Rho hexamer. Binds directly, but weakly, to the core enzyme of RNAP. Also interacts with RpsJ (NusE). The rRNA transcription and antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits (PubMed:32871103). {ECO:0000255\|HAMAP-Rule:MF_00948, ECO:0000269\|PubMed:10820031, ECO:0000269\|PubMed:1532577, ECO:0000269\|PubMed:20413501, ECO:0000269\|PubMed:32871103, ECO:0000269\|PubMed:8422985}.
Domain:		The N-terminal domain interacts with RNAP and the C-terminal domain binds either to Rho or to RpsJ (NusE). These domains are separated by a flexible linker. {ECO:0000269\|PubMed:20413501}.
Similarity:		Belongs to the NusG family. {ECO:0000255\|HAMAP- Rule:MF_00948}.