UniProt functional annotation for P0A3B2



	UniProt functional annotation for P0A3B2

UniProt code: P0A3B2.

Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC).

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

Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352). {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:9622352}.

Catalytic activity: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP- Rule:MF_00849, ECO:0000269|PubMed:9622352};

Subunit: Purifies as a 125-130 kDa band, also copurifies with RNA polymerase. {ECO:0000269|PubMed:7783627}.

Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849}. Note=Binds to ribosomes. {ECO:0000255|HAMAP-Rule:MF_00849}.

Ptm: Phosphorylated on tyrosine, probably by autophosphorylation (PubMed:9622352, PubMed:9642082) (Probable). Phosphorylation is strongly activated by proteins present in strain E2348/69 / EPEC / MAR001 but not K12 / DH5 alpha. Phosphorylation increases GTPase activity (PubMed:9622352). {ECO:0000269|PubMed:9622352, ECO:0000269|PubMed:9642082, ECO:0000305|PubMed:7783627}.

Disruption phenotype: Deletion alters the pattern of protein synthesis during both exponential growth and carbon starvation (PubMed:9642082). No longer alters host cytoskeleton; upon infection of HeLa cells microvilli are not disrupted (although some thicken), bacteria adhere to host cells but actin does not accumulate beneath them. 100-fold increased sensitivity of bacteria to human BPI. Increased bacterial cell motililty, increased secretion of flagellin gene (fliC) (PubMed:9622352). Decreased accumulation in infected HeLa cells of a phosphotyrosine protein that might be bacterial Tir, enhanced Ca(2+) efflux from infected HeLa cells (PubMed:9765944). {ECO:0000269|PubMed:9622352, ECO:0000269|PubMed:9642082, ECO:0000269|PubMed:9765944}.

Miscellaneous: The initial events following infection of human cells by EPEC bacteria include the destruction of microvilli and the accumulation of actin underneath the adherent bacteria (part of the attaching and effacing lesion). {ECO:0000303|PubMed:9622352}.

Similarity: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily. {ECO:0000255|HAMAP-Rule:MF_00849}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli O127:H6 (strain E2348/69 / EPEC).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352). {ECO:0000255\|HAMAP-Rule:MF_00849, ECO:0000269\|PubMed:9622352}.


Catalytic activity:		Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255\|HAMAP- Rule:MF_00849, ECO:0000269\|PubMed:9622352};
Subunit:		Purifies as a 125-130 kDa band, also copurifies with RNA polymerase. {ECO:0000269\|PubMed:7783627}.
Subcellular location:		Cytoplasm {ECO:0000255\|HAMAP-Rule:MF_00849}. Note=Binds to ribosomes. {ECO:0000255\|HAMAP-Rule:MF_00849}.
Ptm:		Phosphorylated on tyrosine, probably by autophosphorylation (PubMed:9622352, PubMed:9642082) (Probable). Phosphorylation is strongly activated by proteins present in strain E2348/69 / EPEC / MAR001 but not K12 / DH5 alpha. Phosphorylation increases GTPase activity (PubMed:9622352). {ECO:0000269\|PubMed:9622352, ECO:0000269\|PubMed:9642082, ECO:0000305\|PubMed:7783627}.
Disruption phenotype:		Deletion alters the pattern of protein synthesis during both exponential growth and carbon starvation (PubMed:9642082). No longer alters host cytoskeleton; upon infection of HeLa cells microvilli are not disrupted (although some thicken), bacteria adhere to host cells but actin does not accumulate beneath them. 100-fold increased sensitivity of bacteria to human BPI. Increased bacterial cell motililty, increased secretion of flagellin gene (fliC) (PubMed:9622352). Decreased accumulation in infected HeLa cells of a phosphotyrosine protein that might be bacterial Tir, enhanced Ca(2+) efflux from infected HeLa cells (PubMed:9765944). {ECO:0000269\|PubMed:9622352, ECO:0000269\|PubMed:9642082, ECO:0000269\|PubMed:9765944}.
Miscellaneous:		The initial events following infection of human cells by EPEC bacteria include the destruction of microvilli and the accumulation of actin underneath the adherent bacteria (part of the attaching and effacing lesion). {ECO:0000303\|PubMed:9622352}.
Similarity:		Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily. {ECO:0000255\|HAMAP-Rule:MF_00849}.