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Protein

30S ribosome-binding factor

Gene

rbfA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoCyc
  • maturation of SSU-rRNA Source: EcoliWiki
  • response to cold Source: EcoCyc

Keywordsi

Biological processRibosome biogenesis, Stress response

Enzyme and pathway databases

BioCyciEcoCyc: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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11178. rbfA.

Subcellular locationi

  • Cytoplasm UniRule annotation2 Publications

  • 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

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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10R → H: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi30P → L: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi77G → D: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi84G → E: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi100D → G: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi109 – 133Missing : 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 BLAST25
Mutagenesisi112 – 133LVTSV…DSKED → GDQRGQT: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 PublicationAdd BLAST22
Mutagenesisi120D → N: Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 Publication1
Mutagenesisi122 – 133Missing : Suppresses growth defects and restores maturation of the 30S subunit of an rsgA deletion. Decreased affinity for 30S ribosomes. 1 PublicationAdd BLAST12

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001026582 – 13330S ribosome-binding factorAdd BLAST132

Proteomic databases

PaxDbiP0A7G2.
PRIDEiP0A7G2.

2D gel databases

SWISS-2DPAGEP0A7G2.

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

BioGridi4262435. 183 interactors.
IntActiP0A7G2. 2 interactors.
MINTiMINT-1265558.
STRINGi511145.b3167.

Structurei

Secondary structure

1133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Helixi8 – 22Combined sources15
Beta strandi25 – 29Combined sources5
Helixi30 – 32Combined sources3
Beta strandi41 – 44Combined sources4
Turni45 – 48Combined sources4
Beta strandi49 – 55Combined sources7
Helixi58 – 60Combined sources3
Helixi62 – 74Combined sources13
Helixi76 – 86Combined sources11
Beta strandi94 – 99Combined sources6
Beta strandi104 – 106Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKGNMR-A1-108[»]
ProteinModelPortaliP0A7G2.
SMRiP0A7G2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7G2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni109 – 133Required for stable 30S ribosomal association in vitro1 PublicationAdd BLAST25

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

eggNOGiENOG4105KG7. Bacteria.
COG0858. LUCA.
HOGENOMiHOG000218325.
InParanoidiP0A7G2.
KOiK02834.
OMAiVMPEIRF.
PhylomeDBiP0A7G2.

Family and domain databases

Gene3Di3.30.300.20. 1 hit.
HAMAPiMF_00003. RbfA. 1 hit.
InterProiView protein in InterPro
IPR015946. KH_dom-like_a/b.
IPR000238. Ribosome-bd_facA.
IPR023799. Ribosome-bd_facA_dom.
IPR020053. Ribosome-bd_factorA_CS.
PANTHERiPTHR33515. PTHR33515. 1 hit.
PfamiView protein in Pfam
PF02033. RBFA. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD007327. Rib_bd_factA. 1 hit.
SUPFAMiSSF89919. SSF89919. 1 hit.
TIGRFAMsiTIGR00082. rbfA. 1 hit.
PROSITEiView 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]FASTAAdd 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.
PIRiS01915. Q9EC15.
RefSeqiNP_417636.1. NC_000913.3.
WP_001040205.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76201; AAC76201; b3167.
BAE77213; BAE77213; BAE77213.
GeneIDi947685.
KEGGiecj:JW3136.
eco:b3167.
PATRICi32121752. VBIEscCol129921_3262.

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.
PIRiS01915. Q9EC15.
RefSeqiNP_417636.1. NC_000913.3.
WP_001040205.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKGNMR-A1-108[»]
ProteinModelPortaliP0A7G2.
SMRiP0A7G2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262435. 183 interactors.
IntActiP0A7G2. 2 interactors.
MINTiMINT-1265558.
STRINGi511145.b3167.

2D gel databases

SWISS-2DPAGEP0A7G2.

Proteomic databases

PaxDbiP0A7G2.
PRIDEiP0A7G2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76201; AAC76201; b3167.
BAE77213; BAE77213; BAE77213.
GeneIDi947685.
KEGGiecj:JW3136.
eco:b3167.
PATRICi32121752. VBIEscCol129921_3262.

Organism-specific databases

EchoBASEiEB1165.
EcoGeneiEG11178. rbfA.

Phylogenomic databases

eggNOGiENOG4105KG7. Bacteria.
COG0858. LUCA.
HOGENOMiHOG000218325.
InParanoidiP0A7G2.
KOiK02834.
OMAiVMPEIRF.
PhylomeDBiP0A7G2.

Enzyme and pathway databases

BioCyciEcoCyc:EG11178-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7G2.
PROiP0A7G2.

Family and domain databases

Gene3Di3.30.300.20. 1 hit.
HAMAPiMF_00003. RbfA. 1 hit.
InterProiView protein in InterPro
IPR015946. KH_dom-like_a/b.
IPR000238. Ribosome-bd_facA.
IPR023799. Ribosome-bd_facA_dom.
IPR020053. Ribosome-bd_factorA_CS.
PANTHERiPTHR33515. PTHR33515. 1 hit.
PfamiView protein in Pfam
PF02033. RBFA. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD007327. Rib_bd_factA. 1 hit.
SUPFAMiSSF89919. SSF89919. 1 hit.
TIGRFAMsiTIGR00082. rbfA. 1 hit.
PROSITEiView protein in PROSITE
PS01319. RBFA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRBFA_ECOLI
AccessioniPrimary (citable) accession number: P0A7G2
Secondary accession number(s): P09170, Q2M943
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 15, 2017
This is version 101 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.