RSGA_ECOLI
ID RSGA_ECOLI Reviewed; 350 AA.
AC P39286; Q2M6E1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000303|PubMed:15466596};
GN Synonyms=engC, yjeQ; OrderedLocusNames=b4161, JW4122;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 IDENTIFICATION.
RX PubMed=9743119; DOI=10.1038/nbt0998-851;
RA Arigoni F., Talabot F., Peitsch M.C., Edgerton M.D., Meldrum E., Allet E.,
RA Fish R., Jamotte T., Curchod M.-L., Loferer H.;
RT "A genome-based approach for the identification of essential bacterial
RT genes.";
RL Nat. Biotechnol. 16:851-856(1998).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP MUTAGENESIS OF LYS-220 AND SER-221, AND GDP-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12220175; DOI=10.1021/bi020355q;
RA Daigle D.M., Rossi L., Berghuis A.M., Aravind L., Koonin E.V., Brown E.D.;
RT "YjeQ, an essential, conserved, uncharacterized protein from Escherichia
RT coli, is an unusual GTPase with circularly permuted G-motifs and marked
RT burst kinetics.";
RL Biochemistry 41:11109-11117(2002).
RN [6]
RP FUNCTION, ASSOCIATION WITH 30S RIBOSOMAL SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 1-MET--ARG-20 AND SER-221.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14973029; DOI=10.1128/jb.186.5.1381-1387.2004;
RA Daigle D.M., Brown E.D.;
RT "Studies of the interaction of Escherichia coli YjeQ with the ribosome in
RT vitro.";
RL J. Bacteriol. 186:1381-1387(2004).
RN [7]
RP FUNCTION, ASSOCIATION WITH 30S RIBOSOMAL SUBUNIT, DISRUPTION PHENOTYPE, AND
RP EFFECT OF ANTIBIOTICS ON GTPASE.
RC STRAIN=K12;
RX PubMed=15466596; DOI=10.1093/nar/gkh861;
RA Himeno H., Hanawa-Suetsugu K., Kimura T., Takagi K., Sugiyama W.,
RA Shirata S., Mikami T., Odagiri F., Osanai Y., Watanabe D., Goto S.,
RA Kalachnyuk L., Ushida C., Muto A.;
RT "A novel GTPase activated by the small subunit of ribosome.";
RL Nucleic Acids Res. 32:5303-5309(2004).
RN [8]
RP FUNCTION, AND EFFECT OF ANTIBIOTICS ON GTPASE ACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15828870; DOI=10.1042/bj20041873;
RA Campbell T.L., Daigle D.M., Brown E.D.;
RT "Characterization of the Bacillus subtilis GTPase YloQ and its role in
RT ribosome function.";
RL Biochem. J. 389:843-852(2005).
RN [9]
RP FUNCTION, AND GENETIC INTERACTION.
RC STRAIN=K12;
RX PubMed=18223068; DOI=10.1128/jb.01744-07;
RA Campbell T.L., Brown E.D.;
RT "Genetic interaction screens with ordered overexpression and deletion clone
RT sets implicate the Escherichia coli GTPase YjeQ in late ribosome
RT biogenesis.";
RL J. Bacteriol. 190:2537-2545(2008).
RN [10]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-250.
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 [11]
RP FUNCTION, STRUCTURE BY ELECTRON MICROSCOPY (11.6 ANGSTROMS), AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=EB334;
RX PubMed=21303937; DOI=10.1261/rna.2509811;
RA Jomaa A., Stewart G., Martin-Benito J., Zielke R., Campbell T.L.,
RA Maddock J.R., Brown E.D., Ortega J.;
RT "Understanding ribosome assembly: the structure of in vivo assembled
RT immature 30S subunits revealed by cryo-electron microscopy.";
RL RNA 17:697-709(2011).
RN [12]
RP FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 298-LYS--ARG-300 AND 320-LYS--ASP-350.
RC STRAIN=K12 / MG1655 / ATCC 47076;
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]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=27382067; DOI=10.1093/nar/gkw613;
RA Thurlow B., Davis J.H., Leong V., Moraes T.F., Williamson J.R., Ortega J.;
RT "Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly
RT intermediates of the 30S subunit.";
RL Nucleic Acids Res. 44:9918-9932(2016).
RN [14] {ECO:0007744|PDB:2YKR}
RP STRUCTURE BY ELECTRON MICROSCOPY (9.80 ANGSTROMS) IN GMP-PNP-BOUND FORM ON
RP THE 30S RIBOSOME, SUBUNIT, AND RRNA-BINDING.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=21788480; DOI=10.1073/pnas.1104645108;
RA Guo Q., Yuan Y., Xu Y., Feng B., Liu L., Chen K., Sun M., Yang Z., Lei J.,
RA Gao N.;
RT "Structural basis for the function of a small GTPase RsgA on the 30S
RT ribosomal subunit maturation revealed by cryoelectron microscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13100-13105(2011).
RN [15] {ECO:0007744|PDB:4A2I}
RP STRUCTURE BY ELECTRON MICROSCOPY (16.50 ANGSTROMS) OF 35-337 IN
RP GMP-PNP-BOUND FORM ON THE 30S RIBOSOME, SUBUNIT, AND RRNA-BINDING.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=21960487; DOI=10.1261/rna.2922311;
RA Jomaa A., Stewart G., Mears J.A., Kireeva I., Brown E.D., Ortega J.;
RT "Cryo-electron microscopy structure of the 30S subunit in complex with the
RT YjeQ biogenesis factor.";
RL RNA 17:2026-2038(2011).
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 ribosomal subunit (PubMed:18223068, PubMed:21102555,
CC PubMed:21303937, PubMed:25904134, PubMed:27382067). Binds the 30S
CC subunit contacting the head, platform, and rRNA helix 44, which may
CC assist the last maturation stages (PubMed:21788480, PubMed:21960487).
CC Removes RbfA from mature, but not immature 30S ribosomes in a GTP-
CC dependent manner; 95% removal in the presence of GTP, 90% removal in
CC GMP-PNP and 65% removal in the presence of GDP (PubMed:21102555,
CC PubMed:25904134). Circulary permuted GTPase that catalyzes rapid
CC hydrolysis of GTP with a slow catalytic turnover (PubMed:12220175).
CC Dispensible for viability, but important for overall fitness. The
CC intrinsic GTPase activity is stimulated by the presence of 30S (160-
CC fold increase in kcat) or 70S (96-fold increase in kcat) ribosomes
CC (PubMed:14973029). Mature 30S ribosomes stimulate intrinsic GTPase more
CC than do immature 30S ribosomes (PubMed:25904134). Ribosome-associated
CC GTPase activity is stimulated by RbfA (PubMed:21102555). The GTPase is
CC inhibited by aminoglycoside antibiotics such as neomycin and paromycin
CC (PubMed:15466596) streptomycin and spectinomycin (PubMed:15828870).
CC This inhibition is not due to competition for binding sites on the 30S
CC or 70S ribosome (PubMed:15828870). {ECO:0000269|PubMed:12220175,
CC ECO:0000269|PubMed:14973029, ECO:0000269|PubMed:15466596,
CC ECO:0000269|PubMed:15828870, ECO:0000269|PubMed:21102555,
CC ECO:0000269|PubMed:25904134, ECO:0000305|PubMed:18223068,
CC ECO:0000305|PubMed:27382067}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01820};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for GTP {ECO:0000269|PubMed:12220175};
CC KM=1.0 mM for dATP {ECO:0000269|PubMed:12220175};
CC KM=1.2 mM for ATP {ECO:0000269|PubMed:12220175};
CC KM=1.3 mM for ITP {ECO:0000269|PubMed:12220175};
CC KM=1.6 mM for dGTP {ECO:0000269|PubMed:12220175};
CC KM=2.4 mM for CTP {ECO:0000269|PubMed:12220175};
CC Note=Measured in the absence of 30S ribosomes, kcat is 8.1 h(-1) for
CC GTP, 5.2 for dATP, 3.5 for ATP, 4.5 for ITP, 7.1 for dGTP, 2.1 for
CC CTP. {ECO:0000269|PubMed:12220175};
CC -!- SUBUNIT: Monomer (Probable). All of the protein is associated with
CC ribosomes; the ratio is substoichiometric at 1:200 RsgA/ribosome
CC (PubMed:14973029). Association is tightest with the 30S subunit in the
CC presence of the non-hydrolyzable GTP analog GMP-PNP (PubMed:14973029,
CC PubMed:15466596). 2 cryoelectron microscopy (cryo-EM) structures in
CC complex with 30S ribosomes have been resolved; the protein is
CC determined to bind to different but partially overlapping regions of
CC the 30S ribosomal subunit (PubMed:21788480, PubMed:21960487). One cryo-
CC EM study suggests it contacts ribosomal proteins S3, S12 and S13 as
CC well as 16S rRNA (PubMed:21788480). Another cryo-EM study shows it to
CC bind 16S rRNA, no ribosomal proteins, and to cover the sites of
CC intersubunit bridges B2a, B3 and B7a (PubMed:21960487). Has a
CC significant preference for mature versus immature 30S ribosomes in the
CC presence of GMP-PNP (PubMed:21102555, PubMed:27382067). Another study
CC shows it binds equally well to mature and immature 30S ribosomal
CC subunits in the presence of GMP-PNP (PubMed:25904134).
CC {ECO:0000269|PubMed:14973029, ECO:0000269|PubMed:15466596,
CC ECO:0000269|PubMed:21102555, ECO:0000269|PubMed:21788480,
CC ECO:0000269|PubMed:21960487, ECO:0000269|PubMed:25904134,
CC ECO:0000269|PubMed:27382067, ECO:0000305|PubMed:12220175}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820,
CC ECO:0000269|PubMed:14973029}. Note=Associates with 30S ribosomes
CC (PubMed:14973029). {ECO:0000269|PubMed:14973029}.
CC -!- DOMAIN: Has 3 domains; an N-terminal OB-like domain (about residues 1-
CC 100), a central, circularly permutated GTPase module (residues 104-270)
CC and the C-terminal zinc-finger domain (residues 280 to 350)
CC (PubMed:25904134). The C-terminal domain has 2 regions; the zinc-
CC binding domain (residues 287-319) is required for binding to 30S
CC ribosomes while the extreme C-terminus (residues 320-350) helps remove
CC RbfA from the mature 30S subunit. {ECO:0000305|PubMed:25904134}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth rate, reduced 70S ribosomes,
CC accumulation of 17S rRNA (the precursor of 16S rRNA) (PubMed:15466596,
CC PubMed:21303937, PubMed:25904134, PubMed:27382067). Ribosomal proteins
CC S2 and S21 not found in 30S subunits, decreased S3 and RbfA in 30S
CC subunits, distortion of rRNA helix 44 near the decoding center
CC (PubMed:21303937, PubMed:27382067). The phenotype is partially
CC suppressed by overexpression of a number of genes involved in ribosome
CC function, including infB, era and ksgA (PubMed:15466596). Double rbfA-
CC rsgA deletion mutants have the same phenotype as single mutants
CC (PubMed:21102555). Single rgsA deletion is suppressed by a number of
CC mutants in RbfA but not by wild-type RbfA; in all the RbfA mutants less
CC RbfA is found bound to the 30S ribosome (PubMed:21102555).
CC {ECO:0000269|PubMed:15466596, ECO:0000269|PubMed:21102555,
CC ECO:0000269|PubMed:21303937, ECO:0000269|PubMed:25904134,
CC ECO:0000269|PubMed:27382067}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- CAUTION: Was initially characterized with a propeptide of 20 residues;
CC this is now thought to be the result of in vitro proteolysis when the
CC protein is overexpressed (PubMed:12220175, PubMed:14973029).
CC {ECO:0000305|PubMed:12220175, ECO:0000305|PubMed:14973029}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97060.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97060.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77121.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78165.1; -; Genomic_DNA.
DR PIR; S56389; S56389.
DR RefSeq; NP_418585.4; NC_000913.3.
DR RefSeq; WP_000041964.1; NZ_LN832404.1.
DR PDB; 2YKR; EM; 9.80 A; W=1-350.
DR PDB; 4A2I; EM; 16.50 A; V=35-337.
DR PDB; 5NO2; EM; 5.16 A; Z=34-346.
DR PDB; 5NO3; EM; 5.16 A; Z=34-346.
DR PDB; 5NO4; EM; 5.16 A; Z=34-346.
DR PDB; 5UZ4; EM; 5.80 A; Z=6-339.
DR PDB; 7BOI; EM; 2.98 A; W=1-350.
DR PDB; 7NAR; EM; 3.00 A; W=1-350.
DR PDBsum; 2YKR; -.
DR PDBsum; 4A2I; -.
DR PDBsum; 5NO2; -.
DR PDBsum; 5NO3; -.
DR PDBsum; 5NO4; -.
DR PDBsum; 5UZ4; -.
DR PDBsum; 7BOI; -.
DR PDBsum; 7NAR; -.
DR AlphaFoldDB; P39286; -.
DR SMR; P39286; -.
DR BioGRID; 4261080; 609.
DR DIP; DIP-12581N; -.
DR IntAct; P39286; 33.
DR MINT; P39286; -.
DR STRING; 511145.b4161; -.
DR jPOST; P39286; -.
DR PaxDb; P39286; -.
DR PRIDE; P39286; -.
DR EnsemblBacteria; AAC77121; AAC77121; b4161.
DR EnsemblBacteria; BAE78165; BAE78165; BAE78165.
DR GeneID; 58390199; -.
DR GeneID; 948674; -.
DR KEGG; ecj:JW4122; -.
DR KEGG; eco:b4161; -.
DR PATRIC; fig|1411691.4.peg.2537; -.
DR EchoBASE; EB2372; -.
DR eggNOG; COG1162; Bacteria.
DR HOGENOM; CLU_033617_2_0_6; -.
DR InParanoid; P39286; -.
DR OMA; CLVAAYD; -.
DR PhylomeDB; P39286; -.
DR BioCyc; EcoCyc:G7841-MON; -.
DR BioCyc; MetaCyc:G7841-MON; -.
DR SABIO-RK; P39286; -.
DR EvolutionaryTrace; P39286; -.
DR PRO; PR:P39286; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0019003; F:GDP binding; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:EcoCyc.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:EcoCyc.
DR CDD; cd01854; YjeQ_EngC; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01820; GTPase_RsgA; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR InterPro; IPR010914; RsgA_GTPase_dom.
DR PANTHER; PTHR32120; PTHR32120; 1.
DR Pfam; PF03193; RsgA_GTPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00157; TIGR00157; 1.
DR PROSITE; PS50936; ENGC_GTPASE; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..350
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000008149"
FT DOMAIN 104..273
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..113
FT /note="Necessary for association with the ribosome and for
FT stimulation of GTPase activity by 30S ribosomes"
FT /evidence="ECO:0000269|PubMed:14973029"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..20
FT /note="Necessary for GMP-PNP-dependent association with the
FT 30S ribosomal subunit"
FT /evidence="ECO:0000269|PubMed:14973029,
FT ECO:0000305|PubMed:12220175, ECO:0000305|PubMed:21788480"
FT REGION 287..319
FT /note="Required for binding to mature and immature 30S
FT ribosomes"
FT /evidence="ECO:0000269|PubMed:25904134"
FT REGION 320..350
FT /note="Required to remove RbfA from mature 30S ribosomes"
FT /evidence="ECO:0000269|PubMed:25904134"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 214..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT MUTAGEN 1..20
FT /note="Missing: Loss of GMP-PNP-dependent association with
FT 30S ribosomal subunit, increased association with 50S and
FT 70S ribosomes."
FT /evidence="ECO:0000269|PubMed:14973029"
FT MUTAGEN 220
FT /note="K->A: Reduction in GTPase activity, 38% of wild-type
FT kcat for GTP. Strong reduction, 5.2% of wild-type kcat for
FT GTP; when associated with A-221."
FT /evidence="ECO:0000269|PubMed:12220175"
FT MUTAGEN 221
FT /note="S->A: Reduction in GTPase activity, 22% of wild-type
FT kcat for GTP. GTPase activity not stimulated by 30S
FT ribosomes (PubMed:14973029). Strong reduction, 5.2% of
FT wild-type kcat for GTP; when associated with A-220."
FT /evidence="ECO:0000269|PubMed:12220175,
FT ECO:0000269|PubMed:14973029"
FT MUTAGEN 250
FT /note="T->A: Loss of GTPase activity, does not dissociate
FT RbfA."
FT /evidence="ECO:0000269|PubMed:21102555"
FT MUTAGEN 298..300
FT /note="KYR->AYA: About 2-fold decreased binding to mature
FT and immature 30S ribosomes, GTPase activity stimulated by
FT ribosomes."
FT /evidence="ECO:0000269|PubMed:25904134"
FT MUTAGEN 320..350
FT /note="Missing: Slightly increased specific binding to
FT mature and immature 30S ribosomes, GTPase activity not
FT stimulated by ribosomes. No longer removes RbfA from mature
FT 30S ribosomes, increases RbfA-binding about 5-fold. Does
FT not complement a deletion mutant in vivo, fewer 70S
FT ribosomes, slower growth than deletion mutant."
FT /evidence="ECO:0000269|PubMed:25904134"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:7BOI"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:7BOI"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:7BOI"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:7BOI"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7BOI"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7BOI"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:7BOI"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:7BOI"
SQ SEQUENCE 350 AA; 39193 MW; DEB14E36D2F0F378 CRC64;
MSKNKLSKGQ QRRVNANHQR RLKTSKEKPD YDDNLFGEPD EGIVISRFGM HADVESADGD
VHRCNIRRTI RSLVTGDRVV WRPGKPAAEG VNVKGIVEAV HERTSVLTRP DFYDGVKPIA
ANIDQIVIVS AILPELSLNI IDRYLVACET LQIEPIIVLN KIDLLDDEGM AFVNEQMDIY
RNIGYRVLMV SSHTQDGLKP LEEALTGRIS IFAGQSGVGK SSLLNALLGL QKEILTNDIS
DNSGLGQHTT TAARLYHFPH GGDVIDSPGV REFGLWHLEP EQITQGFVEF HDYLGLCKYR
DCKHDTDPGC AIREAVEEGK IAETRFENYH RILESMAQVK TRKNFSDTDD
