RBFA_ECOLI
ID RBFA_ECOLI Reviewed; 133 AA.
AC P0A7G2; P09170; Q2M943;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=30S ribosome-binding factor {ECO:0000303|PubMed:7535280};
DE AltName: Full=Protein P15B {ECO:0000303|PubMed:2849753};
DE AltName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003, ECO:0000303|PubMed:9422595};
DE Short=RbfA {ECO:0000303|PubMed:7535280};
GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003, ECO:0000303|PubMed:7535280};
GN Synonyms=P15B {ECO:0000303|PubMed:2849753}, yhbB;
GN OrderedLocusNames=b3167, JW3136;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND OPERON.
RC STRAIN=K12;
RX PubMed=2849753; DOI=10.1093/nar/16.22.10803;
RA Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B.;
RT "The existence of two genes between infB and rpsO in the Escherichia coli
RT genome: DNA sequencing and S1 nuclease mapping.";
RL Nucleic Acids Res. 16:10803-10816(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Tonella L., Hochstrasser D.F.;
RL Submitted (SEP-1996) to UniProtKB.
RN [5]
RP IDENTIFICATION, FUNCTION IN SUPPRESSION OF AN RRNA COLD-SENSITIVE MUTATION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CSH142;
RX PubMed=7535280; DOI=10.1101/gad.9.5.626;
RA Dammel C.S., Noller H.F.;
RT "Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of
RT a novel ribosome-binding factor, RbfA.";
RL Genes Dev. 9:626-637(1995).
RN [6]
RP FUNCTION, INDUCTION BY COLD-SHOCK, AND DISRUPTION PHENOTYPE.
RC STRAIN=CSH142;
RX PubMed=8898389; DOI=10.1111/j.1365-2958.1996.tb02582.x;
RA Jones P.G., Inouye M.;
RT "RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose
RT absence triggers the cold-shock response.";
RL Mol. Microbiol. 21:1207-1218(1996).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MW100;
RX PubMed=9422595; DOI=10.1128/jb.180.1.73-82.1998;
RA Bylund G.O., Wipemo L.C., Lundberg L.A., Wikstroem P.M.;
RT "RimM and RbfA are essential for efficient processing of 16S rRNA in
RT Escherichia coli.";
RL J. Bacteriol. 180:73-82(1998).
RN [8]
RP DISRUPTION PHENOTYPE, AND SUPPRESSION BY ERA.
RC STRAIN=K12 / ATCC 35607 / JM83, and K12 / MC4100;
RX PubMed=12753192; DOI=10.1046/j.1365-2958.2003.03475.x;
RA Inoue K., Alsina J., Chen J., Inouye M.;
RT "Suppression of defective ribosome assembly in a rbfA deletion mutant by
RT overexpression of Era, an essential GTPase in Escherichia coli.";
RL Mol. Microbiol. 48:1005-1016(2003).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 109-MET--ASP-133.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12963368; DOI=10.1016/s0022-2836(03)00953-7;
RA Xia B., Ke H., Shinde U., Inouye M.;
RT "The role of RbfA in 16S rRNA processing and cell growth at low temperature
RT in Escherichia coli.";
RL J. Mol. Biol. 332:575-584(2003).
RN [10]
RP FUNCTION.
RC STRAIN=K12 / ATCC 35607 / JM83, and K12 / MC4100;
RX PubMed=16825789; DOI=10.1159/000092818;
RA Inoue K., Chen J., Tan Q., Inouye M.;
RT "Era and RbfA have overlapping function in ribosome biogenesis in
RT Escherichia coli.";
RL J. Mol. Microbiol. Biotechnol. 11:41-52(2006).
RN [11]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-10; PRO-30;
RP GLY-77; GLY-84; ASP-100; 111-ASN--ASP-133; ASP-120 AND 122-GLU--ASP-133.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=21102555; DOI=10.1038/emboj.2010.291;
RA Goto S., Kato S., Kimura T., Muto A., Himeno H.;
RT "RsgA releases RbfA from 30S ribosome during a late stage of ribosome
RT biosynthesis.";
RL EMBO J. 30:104-114(2011).
RN [12]
RP RELEASE FROM THE 30S RIBOSOMAL SUBUNIT.
RX PubMed=25904134; DOI=10.1261/rna.049171.114;
RA Jeganathan A., Razi A., Thurlow B., Ortega J.;
RT "The C-terminal helix in the YjeQ zinc-finger domain catalyzes the release
RT of RbfA during 30S ribosome subunit assembly.";
RL RNA 21:1203-1216(2015).
RN [13] {ECO:0007744|PDB:1KKG}
RP STRUCTURE BY NMR OF 1-108, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP 109-MET--ASP-133.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12628255; DOI=10.1016/s0022-2836(03)00061-5;
RA Huang Y.J., Swapna G.V., Rajan P.K., Ke H., Xia B., Shukla K., Inouye M.,
RA Montelione G.T.;
RT "Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock
RT adaptation protein from Escherichia coli.";
RL J. Mol. Biol. 327:521-536(2003).
CC -!- FUNCTION: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ)
CC that assist in the late maturation steps of the functional core of the
CC 30S subunit. Essential for efficient processing of pre-16S rRNA
CC (PubMed:9422595, PubMed:12963368, PubMed:12628255). Probably part of
CC the 30S subunit prior to or during the final step in the processing of
CC 16S free 30S ribosomal subunits. Probably interacts with the 5'-
CC terminal helix region of 16S rRNA (PubMed:7535280). Has affinity for
CC free ribosomal 30S subunits but not for 70S ribosomes (PubMed:7535280,
CC PubMed:12963368). Overexpression suppresses a cold-sensitive C23U 16S
CC rRNA mutation (PubMed:7535280). Overexpression decreases the lag time
CC following cold-shock by about half, leading to faster adaptation and
CC increased protein synthesis (PubMed:8898389). Overexpression also
CC partially suppresses a rimM deletion mutant and partially rescues its
CC 16S rRNA processing deficiency (PubMed:9422595). Its function overlaps
CC that of Era in ribosome biogenesis (PubMed:16825789). A number of RbfA
CC mutants suppress RsgA/YjeQ deletions, in all cases less RbfA is bound
CC to the 30S ribosome (PubMed:21102555). Released from 30S ribosomes by
CC RsgA; stimulates the ribosome-associated GTPase activity of RsgA
CC (PubMed:21102555). {ECO:0000269|PubMed:12628255,
CC ECO:0000269|PubMed:12963368, ECO:0000269|PubMed:16825789,
CC ECO:0000269|PubMed:21102555, ECO:0000269|PubMed:7535280,
CC ECO:0000269|PubMed:8898389, ECO:0000269|PubMed:9422595}.
CC -!- SUBUNIT: Monomer (PubMed:12628255). Binds 30S but not 50S or 70S
CC ribosomes (PubMed:7535280, PubMed:12963368, PubMed:25904134). Binds
CC equally well to mature and immature 30S ribosomes, but is more stably
CC associated with immature 30S ribosomes (PubMed:21102555).
CC {ECO:0000269|PubMed:12628255, ECO:0000269|PubMed:21102555}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003,
CC ECO:0000269|PubMed:12963368, ECO:0000269|PubMed:7535280}. Note=About
CC 1/3 associates with free 30S ribosomal subunits at 37 degrees Celsius,
CC 6 hours after a 15 degrees Celsius cold-shock about 4-fold more protein
CC is associated with 30S ribosomes (PubMed:7535280, PubMed:12963368).
CC {ECO:0000269|PubMed:12963368, ECO:0000269|PubMed:7535280}.
CC -!- INDUCTION: Fairly strongly expressed in maxicells, part of the metY
CC operon that extends to pnp (at protein level) (PubMed:2849753). Induced
CC by cold shock (42 to 15 degrees Celsius) (at protein level)
CC (PubMed:8898389). {ECO:0000269|PubMed:2849753,
CC ECO:0000269|PubMed:8898389}.
CC -!- DOMAIN: The C-terminus (residues 109-133) is required for stable
CC association with the 30S ribosomal subunit in vitro.
CC {ECO:0000269|PubMed:12963368}.
CC -!- DISRUPTION PHENOTYPE: Severe growth defect at 26 and 30 degrees
CC Celsius, with poor growth at 37 and 42 degrees; has decreased amounts
CC of 70S ribosomes and polysomes and increased amounts of 30S and 50S
CC subunits (PubMed:7535280). Results in a constitutive induction of the
CC cold-shock response; increased cold-shock and ribosomal protein
CC synthesis continues in the presence of general translation inhibition
CC (PubMed:8898389). Less efficient processing of 5' end of 16S rRNA,
CC increased levels of precursor 17S rRNA; effect is more pronounced in
CC cold-shocked cells (PubMed:9422595, PubMed:12963368). Both phenotypes
CC are partially suppressed by overexpression of Era and completely
CC suppressed by overexpression of Era-delta 'Ala-40-Gly-49' mutation
CC (PubMed:12753192). Double rbfA-rsgA deletion mutants have the same
CC phenotype as single mutants (PubMed:21102555).
CC {ECO:0000269|PubMed:12753192, ECO:0000269|PubMed:12963368,
CC ECO:0000269|PubMed:21102555, ECO:0000269|PubMed:7535280,
CC ECO:0000269|PubMed:8898389, ECO:0000269|PubMed:9422595}.
CC -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000255|HAMAP-
CC Rule:MF_00003}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X13270; CAA31634.1; -; Genomic_DNA.
DR EMBL; X13775; CAA32020.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57970.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76201.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77213.1; -; Genomic_DNA.
DR PIR; S01915; Q9EC15.
DR RefSeq; NP_417636.1; NC_000913.3.
DR RefSeq; WP_001040205.1; NZ_STEB01000012.1.
DR PDB; 1KKG; NMR; -; A=1-108.
DR PDB; 7AFL; EM; 4.20 A; V=1-133.
DR PDB; 7AFQ; NMR; -; V=1-133.
DR PDB; 7BOG; EM; 2.75 A; V=1-133.
DR PDB; 7BOH; EM; 2.82 A; V=1-133.
DR PDB; 7NAV; EM; 4.80 A; V=1-133.
DR PDBsum; 1KKG; -.
DR PDBsum; 7AFL; -.
DR PDBsum; 7AFQ; -.
DR PDBsum; 7BOG; -.
DR PDBsum; 7BOH; -.
DR PDBsum; 7NAV; -.
DR AlphaFoldDB; P0A7G2; -.
DR SMR; P0A7G2; -.
DR BioGRID; 4262435; 190.
DR IntAct; P0A7G2; 2.
DR STRING; 511145.b3167; -.
DR SWISS-2DPAGE; P0A7G2; -.
DR jPOST; P0A7G2; -.
DR PaxDb; P0A7G2; -.
DR PRIDE; P0A7G2; -.
DR EnsemblBacteria; AAC76201; AAC76201; b3167.
DR EnsemblBacteria; BAE77213; BAE77213; BAE77213.
DR GeneID; 67414895; -.
DR GeneID; 947685; -.
DR KEGG; ecj:JW3136; -.
DR KEGG; eco:b3167; -.
DR PATRIC; fig|1411691.4.peg.3563; -.
DR EchoBASE; EB1165; -.
DR eggNOG; COG0858; Bacteria.
DR HOGENOM; CLU_089475_5_0_6; -.
DR InParanoid; P0A7G2; -.
DR OMA; GDLQHCK; -.
DR PhylomeDB; P0A7G2; -.
DR BioCyc; EcoCyc:EG11178-MON; -.
DR EvolutionaryTrace; P0A7G2; -.
DR PRO; PR:P0A7G2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:EcoliWiki.
DR GO; GO:0009409; P:response to cold; IMP:EcoCyc.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:EcoCyc.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_00003; RbfA; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR000238; RbfA.
DR InterPro; IPR023799; RbfA_dom_sf.
DR InterPro; IPR020053; Ribosome-bd_factorA_CS.
DR PANTHER; PTHR33515; PTHR33515; 1.
DR Pfam; PF02033; RBFA; 1.
DR SUPFAM; SSF89919; SSF89919; 1.
DR TIGRFAMs; TIGR00082; rbfA; 1.
DR PROSITE; PS01319; RBFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribosome biogenesis; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..133
FT /note="30S ribosome-binding factor"
FT /id="PRO_0000102658"
FT REGION 109..133
FT /note="Required for stable 30S ribosomal association in
FT vitro"
FT /evidence="ECO:0000269|PubMed:12963368"
FT MUTAGEN 10
FT /note="R->H: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 30
FT /note="P->L: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 77
FT /note="G->D: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 84
FT /note="G->E: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 100
FT /note="D->G: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 109..133
FT /note="Missing: Complements small colony and slow growth
FT phenotype of the deletion mutant at 15 degrees Celsius,
FT growth is not quite wild-type. Restores pre-16S rRNA
FT processing but does not suppress cold-sensitive C23U 16S
FT rRNA mutation."
FT /evidence="ECO:0000269|PubMed:12628255,
FT ECO:0000269|PubMed:12963368"
FT MUTAGEN 112..133
FT /note="LVTSVVKHDEERRVNPDDSKED->GDQRGQT: Suppresses growth
FT defects and restores maturation of the 30S subunit of an
FT rsgA deletion. Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 120
FT /note="D->N: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 122..133
FT /note="Missing: Suppresses growth defects and restores
FT maturation of the 30S subunit of an rsgA deletion.
FT Decreased affinity for 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:21102555"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1KKG"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:7BOG"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1KKG"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1KKG"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:7BOG"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:1KKG"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7BOG"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1KKG"
FT HELIX 62..87
FT /evidence="ECO:0007829|PDB:7BOG"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7BOG"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1KKG"
SQ SEQUENCE 133 AA; 15154 MW; C8EE4FBFD8C01F08 CRC64;
MAKEFGRPQR VAQEMQKEIA LILQREIKDP RLGMMTTVSG VEMSRDLAYA KVYVTFLNDK
DEDAVKAGIK ALQEASGFIR SLLGKAMRLR IVPELTFFYD NSLVEGMRMS NLVTSVVKHD
EERRVNPDDS KED
