RNG_ECOLI
ID RNG_ECOLI Reviewed; 489 AA.
AC P0A9J0; P25537; P76677; Q2M8W7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ribonuclease G {ECO:0000303|PubMed:10329633, ECO:0000303|PubMed:10362534};
DE Short=RNase G {ECO:0000303|PubMed:10329633, ECO:0000303|PubMed:10362534};
DE EC=3.1.26.-;
DE AltName: Full=Cytoplasmic axial filament protein {ECO:0000303|PubMed:8300545};
DE Short=CafA protein {ECO:0000303|PubMed:8300545};
GN Name=rng {ECO:0000303|PubMed:10329633, ECO:0000303|PubMed:10362534};
GN Synonyms=cafA {ECO:0000303|PubMed:8300545},
GN orfF {ECO:0000303|PubMed:1937035}, yhdF; OrderedLocusNames=b3247, JW3216;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1937035; DOI=10.1016/0378-1119(91)90578-y;
RA Wachi M., Doi M., Ueda T., Ueki M., Tsuritani K., Nagai K., Matsuhashi M.;
RT "Sequence of the downstream flanking region of the shape-determining genes
RT mreBCD of Escherichia coli.";
RL Gene 106:135-136(1991).
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 2-11, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=8300545; DOI=10.1128/jb.176.3.917-922.1994;
RA Okada Y., Wachi M., Hirata A., Suzuki K., Nagai K., Matsuhashi M.;
RT "Cytoplasmic axial filaments in Escherichia coli cells: possible function
RT in the mechanism of chromosome segregation and cell division.";
RL J. Bacteriol. 176:917-922(1994).
RN [5]
RP PROTEIN SEQUENCE OF 2-7 AND 315-320, AND SUBUNIT.
RX PubMed=14622423; DOI=10.1046/j.1365-2958.2003.03775.x;
RA Briant D.J., Hankins J.S., Cook M.A., Mackie G.A.;
RT "The quaternary structure of RNase G from Escherichia coli.";
RL Mol. Microbiol. 50:1381-1390(2003).
RN [6]
RP FUNCTION IN 16S RRNA MATURATION, DISRUPTION PHENOTYPE, AND DOMAIN.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10362534; DOI=10.1006/bbrc.1999.0806;
RA Wachi M., Umitsuki G., Shimizu M., Takada A., Nagai K.;
RT "Escherichia coli cafA gene encodes a novel RNase, designated as RNase G,
RT involved in processing of the 5' end of 16S rRNA.";
RL Biochem. Biophys. Res. Commun. 259:483-488(1999).
RN [7]
RP FUNCTION IN 16S RRNA MATURATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=10329633; DOI=10.1093/emboj/18.10.2878;
RA Li Z., Pandit S., Deutscher M.P.;
RT "RNase G (CafA protein) and RNase E are both required for the 5' maturation
RT of 16S ribosomal RNA.";
RL EMBO J. 18:2878-2885(1999).
RN [8]
RP FUNCTION AS AN ENDONUCLEASE, AND SUBSTRATE SPECIFICITY.
RX PubMed=10762247; DOI=10.1128/jb.182.9.2468-2475.2000;
RA Jiang X., Diwa A., Belasco J.G.;
RT "Regions of RNase E important for 5'-end-dependent RNA cleavage and
RT autoregulated synthesis.";
RL J. Bacteriol. 182:2468-2475(2000).
RN [9]
RP FUNCTION AS AN ENDONUCLEASE, AND SUBSTRATE SPECIFICITY.
RX PubMed=10722715; DOI=10.1074/jbc.275.12.8726;
RA Tock M.R., Walsh A.P., Carroll G., McDowall K.J.;
RT "The CafA protein required for the 5'-maturation of 16 S rRNA is a 5'-end-
RT dependent ribonuclease that has context-dependent broad sequence
RT specificity.";
RL J. Biol. Chem. 275:8726-8732(2000).
RN [10]
RP FUNCTION IN MRNA STABILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=11380618; DOI=10.1046/j.1365-2443.2001.00430.x;
RA Umitsuki G., Wachi M., Takada A., Hikichi T., Nagai K.;
RT "Involvement of RNase G in in vivo mRNA metabolism in Escherichia coli.";
RL Genes Cells 6:403-410(2001).
RN [11]
RP FUNCTION IN MRNA STABILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=12450135; DOI=10.1271/bbb.66.2216;
RA Kaga N., Umitsuki G., Nagai K., Wachi M.;
RT "RNase G-dependent degradation of the eno mRNA encoding a glycolysis enzyme
RT enolase in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 66:2216-2220(2002).
RN [12]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=15197283; DOI=10.1073/pnas.0401382101;
RA Jiang X., Belasco J.G.;
RT "Catalytic activation of multimeric RNase E and RNase G by 5'-
RT monophosphorylated RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9211-9216(2004).
RN [13]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF VAL-131; ARG-171; THR-172; ASP-304 AND ASP-347.
RX PubMed=18078441; DOI=10.1111/j.1365-2958.2007.06028.x;
RA Jourdan S.S., McDowall K.J.;
RT "Sensing of 5' monophosphate by Escherichia coli RNase G can significantly
RT enhance association with RNA and stimulate the decay of functional mRNA
RT transcripts in vivo.";
RL Mol. Microbiol. 67:102-115(2008).
RN [14]
RP FUNCTION IN 16S RRNA MATURATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=20176963; DOI=10.1073/pnas.0912305107;
RA Roy-Chaudhuri B., Kirthi N., Culver G.M.;
RT "Appropriate maturation and folding of 16S rRNA during 30S subunit
RT biogenesis are critical for translational fidelity.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4567-4572(2010).
RN [15]
RP FUNCTION IN 23S RRNA MATURATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21717341; DOI=10.1007/s12275-011-1198-7;
RA Song W.S., Lee M., Lee K.;
RT "RNase G participates in processing of the 5'-end of 23S ribosomal RNA.";
RL J. Microbiol. 49:508-511(2011).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=22509045; DOI=10.1073/pnas.1120181109;
RA Murashko O.N., Kaberdin V.R., Lin-Chao S.;
RT "Membrane binding of Escherichia coli RNase E catalytic domain stabilizes
RT protein structure and increases RNA substrate affinity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7019-7024(2012).
RN [17]
RP FUNCTION IN 16S RRNA MATURATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076, and N3433;
RX PubMed=24489121; DOI=10.1093/nar/gku093;
RA Song W., Kim Y.H., Sim S.H., Hwang S., Lee J.H., Lee Y., Bae J., Hwang J.,
RA Lee K.;
RT "Antibiotic stress-induced modulation of the endoribonucleolytic activity
RT of RNase III and RNase G confers resistance to aminoglycoside antibiotics
RT in Escherichia coli.";
RL Nucleic Acids Res. 42:4669-4681(2014).
RN [18]
RP SUBSTRATE SPECIFICITY.
RX PubMed=26694614; DOI=10.1074/jbc.m115.702555;
RA Richards J., Belasco J.G.;
RT "Distinct Requirements for 5'-Monophosphate-assisted RNA Cleavage by
RT Escherichia coli RNase E and RNase G.";
RL J. Biol. Chem. 291:5038-5048(2016).
RN [19]
RP ERRATUM OF PUBMED:26694614.
RX PubMed=27664066; DOI=10.1074/jbc.a115.702555;
RA Richards J., Belasco J.G.;
RT "Distinct requirements for 5'-monophosphate-assisted RNA cleavage by
RT Escherichia coli RNase E and RNase G.";
RL J. Biol. Chem. 291:20825-20825(2016).
RN [20]
RP FUNCTION IN TRNA(PRO) 3' PROCESSING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=27288443; DOI=10.1093/nar/gkw517;
RA Mohanty B.K., Petree J.R., Kushner S.R.;
RT "Endonucleolytic cleavages by RNase E generate the mature 3' termini of the
RT three proline tRNAs in Escherichia coli.";
RL Nucleic Acids Res. 44:6350-6362(2016).
RN [21]
RP FUNCTION IN 16S RRNA PRECURSOR PROCESSING, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=32343306; DOI=10.1093/nar/gkaa260;
RA Jain C.;
RT "RNase AM, a 5' to 3' exonuclease, matures the 5' end of all three
RT ribosomal RNAs in E. coli.";
RL Nucleic Acids Res. 48:5616-5623(2020).
RN [22]
RP PRELIMINARY CRYSTALLIZATION.
RX PubMed=19478437; DOI=10.1107/s1744309109015802;
RA Fang P., Wang J., Li X., Guo M., Xing L., Cao X., Zhu Y., Gao Y., Niu L.,
RA Teng M.;
RT "Crystallization and preliminary X-ray analysis of Escherichia coli RNase
RT G.";
RL Acta Crystallogr. F 65:586-588(2009).
CC -!- FUNCTION: An endonuclease that acts in the processing of the 5'-end of
CC precursors of 16S rRNA, generates a precursor with 3 extra nucleotides
CC at its 5'-end (which is matured by Rnm) (PubMed:10329633,
CC PubMed:10362534, PubMed:10722715, PubMed:20176963, PubMed:24489121,
CC PubMed:26694614, PubMed:32343306). It prefers 5'-monophosphorylated
CC over 5'-OH or 5'-triphosphorylated substrates and cleaves single-
CC stranded sites rich in A and U residues; contributes to RNA turnover
CC (PubMed:10722715, PubMed:11380618, PubMed:12450135, PubMed:18078441,
CC PubMed:21717341, PubMed:10762247). 5'-monophosphate-assisted cleavage
CC requires at least 2 and preferably 3 or more unpaired 5'-terminal
CC nucleotides for cleavage. The optimal spacing between the 5' end and
CC the scissile phosphate appears to be 6 nucleotides. Any sequence of
CC unpaired nucleotides at the 5'-end is tolerated (PubMed:26694614).
CC Processes the 5'-end precursors of 23S rRNA (PubMed:21717341).
CC Participates in processing of tRNA(Pro) (proK and proM)
CC (PubMed:27288443). Also involved in metabolism of some mRNAs
CC (PubMed:11380618, PubMed:12450135, PubMed:18078441). Cells
CC overproducing this protein form chains of cell with cytoplasmic axial
CC filaments (PubMed:8300545). Could be involved in chromosome segregation
CC and cell division. It may be one of the components of the cytoplasmic
CC axial filaments bundles, or merely regulate the formation of this
CC structure (Probable). {ECO:0000269|PubMed:10329633,
CC ECO:0000269|PubMed:10362534, ECO:0000269|PubMed:10722715,
CC ECO:0000269|PubMed:10762247, ECO:0000269|PubMed:11380618,
CC ECO:0000269|PubMed:12450135, ECO:0000269|PubMed:18078441,
CC ECO:0000269|PubMed:20176963, ECO:0000269|PubMed:21717341,
CC ECO:0000269|PubMed:24489121, ECO:0000269|PubMed:26694614,
CC ECO:0000269|PubMed:27288443, ECO:0000269|PubMed:32343306,
CC ECO:0000269|PubMed:8300545, ECO:0000305|PubMed:8300545}.
CC -!- FUNCTION: Confers adaptive resistance to aminoglycoside antibiotics
CC through modulation of 16S rRNA processing.
CC {ECO:0000269|PubMed:24489121}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC -!- ACTIVITY REGULATION: The presence of a 5'-monophosphate on substrate
CC RNA accelerates its cleavage by catalytically activating the enzyme
CC (PubMed:15197283). In contrast, another group has shown that the enzyme
CC has a higher affinity for 5'-monophosphorylated substrate, which
CC enhances substrate binding in vitro and the decay of RNA in vivo
CC (PubMed:18078441). {ECO:0000269|PubMed:15197283,
CC ECO:0000269|PubMed:18078441}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 uM for 5'-phosphorylated 14 base fluorogenic substrate
CC {ECO:0000269|PubMed:15197283};
CC KM=0.33 uM for 5'-OH 14 base fluorogenic substrate
CC {ECO:0000269|PubMed:15197283};
CC KM=0.12 uM for 5'-phosphorylated 13 base fluorogenic substrate
CC {ECO:0000269|PubMed:18078441};
CC KM=21 uM for 5'-OH 13 base fluorogenic substrate
CC {ECO:0000269|PubMed:18078441};
CC Note=kcat is 2.1 min(-1) for 14-base 5'-PO(4) substrate and 0.096
CC min(-1) for 5-OH substrate (PubMed:15197283). kcat is 3.0 min(-1) for
CC 13-base 5'-PO(4) substrate and 1.2 min(-1) for 5-OH substrate
CC (PubMed:18078441). {ECO:0000269|PubMed:15197283,
CC ECO:0000269|PubMed:18078441};
CC -!- SUBUNIT: Homodimer, in equilibrium with possible higher multimers.
CC {ECO:0000305|PubMed:14622423, ECO:0000305|PubMed:15197283,
CC ECO:0000305|PubMed:18078441}.
CC -!- INTERACTION:
CC P0A9J0; P0A7V8: rpsD; NbExp=2; IntAct=EBI-545964, EBI-543939;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22509045,
CC ECO:0000305|PubMed:14622423}. Cell inner membrane
CC {ECO:0000269|PubMed:22509045}; Peripheral membrane protein
CC {ECO:0000305|PubMed:22509045}. Cytoplasm, cytoskeleton
CC {ECO:0000303|PubMed:8300545}. Note=Possible cytoskeletal location is
CC upon overproduction. {ECO:0000303|PubMed:8300545}.
CC -!- INDUCTION: Its mRNA is degraded by RNase III (rnc); in the presence of
CC aminoglycoside antibiotics levels of rng mRNA decrease, leading to
CC longer precursor 16S rRNA in the ribosome, which prevents antibiotic-
CC binding and thus increases resistance to aminoglycosides.
CC {ECO:0000269|PubMed:24489121}.
CC -!- DISRUPTION PHENOTYPE: Slow processing of the 17S rRNA precursor to 16S
CC rRNA, with significant accumulation of a 16.3S rRNA precursor with 66
CC extra nucleotides at its 5' end (PubMed:10329633, PubMed:10362534,
CC PubMed:20176963, PubMed:32343306). Ribosomes with the precursor 16S
CC rRNA show decreased translational fidelity and an increased sensitivity
CC to aminoglycoside antibiotics neomycin and paromomycin
CC (PubMed:20176963). In contrast another group, using independently
CC generated rng deletions in 2 different strains, showed decreased
CC sensitivity to aminoglycoside antibiotics kanamycin, neomycin,
CC paromomycin and streptomycin (PubMed:24489121). A double rne-rng
CC mutated strain no longer processes the 17S rRNA precursor
CC (PubMed:10329633, PubMed:10362534). Significant accumulation of AdhE
CC and enolase, greatly increased stability of adhE and eno mRNA
CC (PubMed:11380618, PubMed:12450135). Accumulation of a 23S rRNA
CC precursor (PubMed:21717341). {ECO:0000269|PubMed:10329633,
CC ECO:0000269|PubMed:10362534, ECO:0000269|PubMed:11380618,
CC ECO:0000269|PubMed:12450135, ECO:0000269|PubMed:20176963,
CC ECO:0000269|PubMed:21717341, ECO:0000269|PubMed:24489121,
CC ECO:0000269|PubMed:32343306}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X57166; CAA40457.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58050.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76279.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77289.1; -; Genomic_DNA.
DR PIR; A65117; A65117.
DR RefSeq; NP_417713.2; NC_000913.3.
DR RefSeq; WP_000123197.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P0A9J0; -.
DR SMR; P0A9J0; -.
DR BioGRID; 4262071; 231.
DR BioGRID; 852056; 1.
DR DIP; DIP-48098N; -.
DR IntAct; P0A9J0; 20.
DR STRING; 511145.b3247; -.
DR jPOST; P0A9J0; -.
DR PaxDb; P0A9J0; -.
DR PRIDE; P0A9J0; -.
DR EnsemblBacteria; AAC76279; AAC76279; b3247.
DR EnsemblBacteria; BAE77289; BAE77289; BAE77289.
DR GeneID; 67415922; -.
DR GeneID; 947744; -.
DR KEGG; ecj:JW3216; -.
DR KEGG; eco:b3247; -.
DR PATRIC; fig|1411691.4.peg.3482; -.
DR EchoBASE; EB1276; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_6; -.
DR InParanoid; P0A9J0; -.
DR OMA; TKGPRIS; -.
DR PhylomeDB; P0A9J0; -.
DR BioCyc; EcoCyc:EG11299-MON; -.
DR BioCyc; MetaCyc:EG11299-MON; -.
DR BRENDA; 3.1.26.3; 2165.
DR PRO; PR:P0A9J0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR GO; GO:0008996; F:ribonuclease G activity; IDA:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IDA:EcoCyc.
DR GO; GO:0006364; P:rRNA processing; IMP:EcoliWiki.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR30001; PTHR30001; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00757; RNaseEG; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Endonuclease; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Nuclease; Reference proteome;
KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14622423,
FT ECO:0000269|PubMed:8300545"
FT CHAIN 2..489
FT /note="Ribonuclease G"
FT /id="PRO_0000097383"
FT DOMAIN 39..128
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 244..489
FT /note="Required for function, when replaced by
FT GVHSRDDKQAGALHRTPADFRSL in mutant BUMMER, cells accumulate
FT 16.3S rRNA precursor"
FT /evidence="ECO:0000269|PubMed:10362534"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513,
FT ECO:0000305|PubMed:18078441"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513,
FT ECO:0000305|PubMed:18078441"
FT MUTAGEN 131
FT /note="V->A: 3.9-fold reduced activity on 5'-PO(4)
FT substrate, 1.9-fold reduced activity on 5'-OH substrate.
FT Has wild-type 16S rRNA in vivo."
FT /evidence="ECO:0000269|PubMed:18078441"
FT MUTAGEN 171
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18078441"
FT MUTAGEN 171
FT /note="R->K: 34-fold reduced activity on 5'-PO(4)
FT substrate, 2.4-fold reduced activity on 5'-OH substrate.
FT Binds 5'-PO(4) substrate 65-fold less well than wild-type,
FT kcat is nearly wild-type. Has wild-type 16S rRNA in vivo."
FT /evidence="ECO:0000269|PubMed:18078441"
FT MUTAGEN 172
FT /note="T->V: 82-fold reduced activity on 5'-PO(4)
FT substrate, 4.9-fold reduced activity on 5'-OH substrate."
FT /evidence="ECO:0000269|PubMed:18078441"
FT MUTAGEN 304
FT /note="D->N: Loss of activity. Accumulates about 50% 16.3S
FT rRNA, 50% wild-type 16SrRNA in vivo."
FT /evidence="ECO:0000269|PubMed:18078441"
FT MUTAGEN 347
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18078441"
SQ SEQUENCE 489 AA; 55364 MW; 9517B3367C455C99 CRC64;
MTAELLVNVT PSETRVAYID GGILQEIHIE REARRGIVGN IYKGRVSRVL PGMQAAFVDI
GLDKAAFLHA SDIMPHTECV AGEEQKQFTV RDISELVRQG QDLMVQVVKD PLGTKGARLT
TDITLPSRYL VFMPGASHVG VSQRIESESE RERLKKVVAE YCDEQGGFII RTAAEGVGEA
ELASDAAYLK RVWTKVMERK KRPQTRYQLY GELALAQRVL RDFADAELDR IRVDSRLTYE
ALLEFTSEYI PEMTSKLEHY TGRQPIFDLF DVENEIQRAL ERKVELKSGG YLIIDQTEAM
TTVDINTGAF VGHRNLDDTI FNTNIEATQA IARQLRLRNL GGIIIIDFID MNNEDHRRRV
LHSLEQALSK DRVKTSVNGF SALGLVEMTR KRTRESIEHV LCNECPTCHG RGTVKTVETV
CYEIMREIVR VHHAYDSDRF LVYASPAVAE ALKGEESHSL AEVEIFVGKQ VKVQIEPLYN
QEQFDVVMM
