rbfA

Functionⁱ

One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S subunit. Essential for efficient processing of pre-16S rRNA (PubMed:9422595, PubMed:12963368, PubMed:12628255). Probably part of the 30S subunit prior to or during the final step in the processing of 16S free 30S ribosomal subunits. Probably interacts with the 5'-terminal helix region of 16S rRNA (PubMed:7535280). Has affinity for free ribosomal 30S subunits but not for 70S ribosomes (PubMed:7535280, PubMed:12963368). Overexpression suppresses a cold-sensitive C23U 16S rRNA mutation (PubMed:7535280). Overexpression decreases the lag time following cold-shock by about half, leading to faster adaptation and increased protein synthesis (PubMed:8898389). Overexpression also partially suppresses a rimM deletion mutant and partially rescues its 16S rRNA processing deficiency (PubMed:9422595). Its function overlaps that of Era in ribosome biogenesis (PubMed:16825789). A number of RbfA mutants suppress RsgA/YjeQ deletions, in all cases less RbfA is bound to the 30S ribosome (PubMed:21102555). Released from 30S ribosomes by RsgA; stimulates the ribosome-associated GTPase activity of RsgA (PubMed:21102555).7 Publications

GO - Molecular functionⁱ

ribosomal small subunit binding
Source: EcoCyc
Inferred from direct assayⁱ
- 7535280

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to DNA damage stimulus
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 18824089
maturation of SSU-rRNA
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 9422595
response to cold
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 8898389
ribosome biogenesis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Ribosome biogenesis, Stress response

Biological process

Ribosome biogenesis, Stress response

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11178-MONOMER

BioCycⁱ

EcoCyc:EG11178-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 30S ribosome-binding factor1 Publication Alternative name(s): Protein P15B1 Publication Ribosome-binding factor A1 PublicationUniRule annotation Short name: RbfA1 Publication
Gene namesⁱ	Name:rbfA1 PublicationUniRule annotation Synonyms:P15B1 Publication, yhbB Ordered Locus Names:b3167, JW3136
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11178 rbfA

EcoGeneⁱ

EG11178 rbfA

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00003
2 Publications
Manual assertion based on experiment inⁱ
- Ref.5
  "Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor, RbfA."
  Dammel C.S., Noller H.F.
  Genes Dev. 9:626-637(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: IDENTIFICATION, FUNCTION IN SUPPRESSION OF AN RRNA COLD-SENSITIVE MUTATION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
- Ref.9
  "The role of RbfA in 16S rRNA processing and cell growth at low temperature in Escherichia coli."
  Xia B., Ke H., Shinde U., Inouye M.
  J. Mol. Biol. 332:575-584(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 109-MET--ASP-133.

Note:

About 1/3 associates with free 30S ribosomal subunits at 37 degrees Celsius, 6 hours after a 15 degrees Celsius cold-shock about 4-fold more protein is associated with 30S ribosomes (PubMed:7535280, PubMed:12963368).2 Publications

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Severe growth defect at 26 and 30 degrees Celsius, with poor growth at 37 and 42 degrees; has decreased amounts of 70S ribosomes and polysomes and increased amounts of 30S and 50S subunits (PubMed:7535280). Results in a constitutive induction of the cold-shock response; increased cold-shock and ribosomal protein synthesis continues in the presence of general translation inhibition (PubMed:8898389). Less efficient processing of 5' end of 16S rRNA, increased levels of precursor 17S rRNA; effect is more pronounced in cold-shocked cells (PubMed:9422595, PubMed:12963368). Both phenotypes are partially suppressed by overexpression of Era and completely suppressed by overexpression of Era-delta 'Ala-40-Gly-49' mutation (PubMed:12753192). Double rbfA-rsgA deletion mutants have the same phenotype as single mutants (PubMed:21102555).6 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	R → H: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication	1
Mutagenesisⁱ	30	P → L: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication	1
Mutagenesisⁱ	77	G → D: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication	1
Mutagenesisⁱ	84	G → E: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication	1
Mutagenesisⁱ	100	D → G: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication	1
Mutagenesisⁱ	109 – 133	Missing : Complements small colony and slow growth phenotype of the deletion mutant at 15 degrees Celsius, growth is not quite wild-type. Restores pre-16S rRNA processing but does not suppress cold-sensitive C23U 16S rRNA mutation. 2 PublicationsAdd BLAST	25
Mutagenesisⁱ	112 – 133	LVTSV…DSKED → GDQRGQT: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 PublicationAdd BLAST	22
Mutagenesisⁱ	120	D → N: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication	1
Mutagenesisⁱ	122 – 133	Missing : Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 PublicationAdd BLAST	12

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000102658	2 – 133	30S ribosome-binding factorAdd BLAST		132

Proteomic databases

PaxDbⁱ	P0A7G2
PRIDEⁱ	P0A7G2

2D gel databases

SWISS-2DPAGEⁱ	P0A7G2

SWISS-2DPAGEⁱ

P0A7G2

Expressionⁱ

Inductionⁱ

Fairly strongly expressed in maxicells, part of the metY operon that extends to pnp (at protein level) (PubMed:2849753). Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389).2 Publications

Interactionⁱ

Subunit structureⁱ

Monomer (PubMed:12628255). Binds 30S but not 50S or 70S ribosomes (PubMed:7535280, PubMed:12963368, PubMed:25904134). Binds equally well to mature and immature 30S ribosomes, but is more stably associated with immature 30S ribosomes (PubMed:21102555).2 Publications

Protein-protein interaction databases

BioGridⁱ	4262435, 190 interactors
IntActⁱ	P0A7G2, 2 interactors
STRINGⁱ	316385.ECDH10B_3341

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 7	Combined sources	3
Helixⁱ	8 – 22	Combined sources	15
Beta strandⁱ	25 – 29	Combined sources	5
Helixⁱ	30 – 32	Combined sources	3
Beta strandⁱ	41 – 44	Combined sources	4
Turnⁱ	45 – 48	Combined sources	4
Beta strandⁱ	49 – 55	Combined sources	7
Helixⁱ	58 – 60	Combined sources	3
Helixⁱ	62 – 74	Combined sources	13
Helixⁱ	76 – 86	Combined sources	11
Beta strandⁱ	94 – 99	Combined sources	6
Beta strandⁱ	104 – 106	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A7G2
SMRⁱ	P0A7G2
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A7G2

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	109 – 133	Required for stable 30S ribosomal association in vitro1 PublicationAdd BLAST		25

Domainⁱ

The C-terminus (residues 109-133) is required for stable association with the 30S ribosomal subunit in vitro.1 Publication

Sequence similaritiesⁱ

Belongs to the RbfA family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105KG7 Bacteria COG0858 LUCA
HOGENOMⁱ	HOG000218325
InParanoidⁱ	P0A7G2
KEGG Orthology (KO) More...KOⁱ	K02834
PhylomeDBⁱ	P0A7G2

Family and domain databases

Gene3Dⁱ	3.30.300.20, 1 hit
HAMAPⁱ	MF_00003 RbfA, 1 hit
InterProⁱ	View protein in InterPro IPR015946 KH_dom-like_a/b IPR000238 RbfA IPR023799 RbfA_dom_sf IPR020053 Ribosome-bd_factorA_CS
PANTHERⁱ	PTHR33515 PTHR33515, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02033 RBFA, 1 hit
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD007327 Rib_bd_factA, 1 hit
SUPFAMⁱ	SSF89919 SSF89919, 1 hit
TIGRFAMsⁱ	TIGR00082 rbfA, 1 hit
PROSITEⁱ	View protein in PROSITE PS01319 RBFA, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0A7G2-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAKEFGRPQR VAQEMQKEIA LILQREIKDP RLGMMTTVSG VEMSRDLAYA 
        60         70         80         90        100
KVYVTFLNDK DEDAVKAGIK ALQEASGFIR SLLGKAMRLR IVPELTFFYD 
       110        120        130 
NSLVEGMRMS NLVTSVVKHD EERRVNPDDS KED

Length:133

Mass (Da):15,154

Last modified:January 23, 2007 - v2

Checksum:ⁱC8EE4FBFD8C01F08

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X13270 Genomic DNA Translation: CAA31634.1 X13775 Genomic DNA Translation: CAA32020.1 U18997 Genomic DNA Translation: AAA57970.1 U00096 Genomic DNA Translation: AAC76201.1 AP009048 Genomic DNA Translation: BAE77213.1
PIRⁱ	S01915 Q9EC15
NCBI Reference Sequences More...RefSeqⁱ	NP_417636.1, NC_000913.3 WP_001040205.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76201; AAC76201; b3167 BAE77213; BAE77213; BAE77213
GeneIDⁱ	947685
KEGGⁱ	ecj:JW3136 eco:b3167
PATRICⁱ	fig\|1411691.4.peg.3563

Protein	Similar proteins		Species	Score	Length	Source
P0A7G2	Ribosome-binding factor A		ECO24		133	UniRef100_A7ZS64
Ribosome-binding factor A		ECO45		133
Ribosome-binding factor A		ECO55		133
Ribosome-binding factor A		ECO57		133
Ribosome-binding factor A		ECO5E		133
+192

Protein	Similar proteins		Species	Score	Length	Source
P0A7G2	Ribosome-binding factor A		ECO24		133	UniRef90_A7ZS64
Ribosome-binding factor A		ECO45		133
Ribosome-binding factor A		ECO55		133
Ribosome-binding factor A		ECO57		133
Ribosome-binding factor A		ECO5E		133
+278

Protein	Similar proteins		Species	Score	Length	Source
P0A7G2	Ribosome-binding factor A		VIBCB		135	UniRef50_A7MZI4
Ribosome-binding factor A		ERWT9		137
Ribosome-binding factor A		PHOLL		136
Ribosome-binding factor A		PASMU		132
Ribosome-binding factor A		VIBVU		131
+769

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X13270 Genomic DNA Translation: CAA31634.1 X13775 Genomic DNA Translation: CAA32020.1 U18997 Genomic DNA Translation: AAA57970.1 U00096 Genomic DNA Translation: AAC76201.1 AP009048 Genomic DNA Translation: BAE77213.1
PIRⁱ	S01915 Q9EC15
RefSeqⁱ	NP_417636.1, NC_000913.3 WP_001040205.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1KKG	NMR	-	A	1-108	[»]
ProteinModelPortalⁱ	P0A7G2
SMRⁱ	P0A7G2
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262435, 190 interactors
IntActⁱ	P0A7G2, 2 interactors
STRINGⁱ	316385.ECDH10B_3341

2D gel databases

SWISS-2DPAGEⁱ	P0A7G2

SWISS-2DPAGEⁱ

P0A7G2

Proteomic databases

PaxDbⁱ	P0A7G2
PRIDEⁱ	P0A7G2

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76201; AAC76201; b3167 BAE77213; BAE77213; BAE77213
GeneIDⁱ	947685
KEGGⁱ	ecj:JW3136 eco:b3167
PATRICⁱ	fig\|1411691.4.peg.3563

Organism-specific databases

EchoBASEⁱ	EB1165
EcoGeneⁱ	EG11178 rbfA

Phylogenomic databases

eggNOGⁱ	ENOG4105KG7 Bacteria COG0858 LUCA
HOGENOMⁱ	HOG000218325
InParanoidⁱ	P0A7G2
KOⁱ	K02834
PhylomeDBⁱ	P0A7G2

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11178-MONOMER

BioCycⁱ

EcoCyc:EG11178-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0A7G2
Protein Ontology More...PROⁱ	PR:P0A7G2

Family and domain databases

Gene3Dⁱ	3.30.300.20, 1 hit
HAMAPⁱ	MF_00003 RbfA, 1 hit
InterProⁱ	View protein in InterPro IPR015946 KH_dom-like_a/b IPR000238 RbfA IPR023799 RbfA_dom_sf IPR020053 Ribosome-bd_factorA_CS
PANTHERⁱ	PTHR33515 PTHR33515, 1 hit
Pfamⁱ	View protein in Pfam PF02033 RBFA, 1 hit
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD007327 Rib_bd_factA, 1 hit
SUPFAMⁱ	SSF89919 SSF89919, 1 hit
TIGRFAMsⁱ	TIGR00082 rbfA, 1 hit
PROSITEⁱ	View protein in PROSITE PS01319 RBFA, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RBFA_ECOLI
Accessionⁱ	P0A7G2Primary (citable) accession number: P0A7G2 Secondary accession number(s): P09170, Q2M943
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 107 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P0A7G2 (RBFA_ECOLI)

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30S ribosome-binding factor

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ