ID RL3_ECOLI Reviewed; 209 AA.
AC P60438; P02386; Q2M6Y5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 01-MAY-2013, entry version 103.
DE RecName: Full=50S ribosomal protein L3;
GN Name=rplC; OrderedLocusNames=b3320, JW3282;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE, AND METHYLATION AT GLN-150.
RC STRAIN=MRE-600;
RX PubMed=365579; DOI=10.1016/0014-5793(78)80423-2;
RA Muranova T.A., Muranov A.V., Markova L.F., Ovchinnikov Y.A.;
RT "The primary structure of ribosomal protein L3 from Escherichia coli
RT 70 S ribosomes.";
RL FEBS Lett. 96:301-305(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3892488; DOI=10.1093/nar/13.12.4521;
RA Zurawski G., Zurawski S.M.;
RT "Structure of the Escherichia coli S10 ribosomal protein operon.";
RL Nucleic Acids Res. 13:4521-4526(1985).
RN [3]
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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
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
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX PubMed=7037196; DOI=10.1016/0092-8674(81)90303-2;
RA Olins P.O., Nomura M.;
RT "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide
RT sequence at the start of the operon.";
RL Cell 26:205-211(1981).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded
RT in the genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP IDENTIFICATION AS AN ASSEMBLY INITIATOR PROTEIN.
RX PubMed=6760192; DOI=10.1073/pnas.79.23.7238;
RA Nowotny V., Nierhaus K.H.;
RT "Initiator proteins for the assembly of the 50S subunit from
RT Escherichia coli ribosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7238-7242(1982).
RN [8]
RP ASSEMBLY MAP OF THE 50S SUBUNIT.
RC STRAIN=K12;
RX PubMed=3298242;
RA Herold M., Nierhaus K.H.;
RT "Incorporation of six additional proteins to complete the assembly map
RT of the 50 S subunit from Escherichia coli ribosomes.";
RL J. Biol. Chem. 262:8826-8833(1987).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP MASS SPECTROMETRY.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [11]
RP METHYLATION BY PRMB.
RC STRAIN=K12;
RX PubMed=11847124; DOI=10.1093/emboj/21.4.769;
RA Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M.,
RA Buckingham R.H.;
RT "The hemK gene in Escherichia coli encodes the N(5)-glutamine
RT methyltransferase that modifies peptide release factors.";
RL EMBO J. 21:769-778(2002).
RN [12]
RP SUCCINYLATION AT LYS-38.
RC STRAIN=K12;
RX PubMed=21151122; DOI=10.1038/nchembio.495;
RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
RT "Identification of lysine succinylation as a new post-translational
RT modification.";
RL Nat. Chem. Biol. 7:58-63(2011).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
RC STRAIN=MRE-600;
RX PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6;
RA Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
RA Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S.,
RA Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using
RT real-space refinement.";
RL Cell 113:789-801(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP STRUCTURES.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W.,
RA Vila-Sanjurjo A., Holton J.M., Cate J.H.D.;
RT "Structures of the bacterial ribosome at 3.5 A resolution.";
RL Science 310:827-834(2005).
CC -!- FUNCTION: One of two assembly inititator proteins, it binds
CC directly near the 3'-end of the 23S rRNA, where it nucleates
CC assembly of the 50S subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19.
CC -!- PTM: Methylated by PrmB (By similarity).
CC -!- MASS SPECTROMETRY: Mass=22257.2; Method=MALDI; Range=1-209;
CC Source=PubMed:10094780;
CC -!- SIMILARITY: Belongs to the ribosomal protein L3P family.
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DR EMBL; X02613; CAA26460.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58117.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76345.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77971.1; -; Genomic_DNA.
DR EMBL; V00344; CAA23634.1; -; Genomic_DNA.
DR PIR; A02757; R5EC3.
DR RefSeq; NP_417779.1; NC_000913.2.
DR RefSeq; YP_492112.1; NC_007779.1.
DR PDB; 1ML5; EM; 14.00 A; e=2-209.
DR PDB; 1P85; EM; 12.30 A; B=1-209.
DR PDB; 1P86; EM; 11.50 A; B=1-209.
DR PDB; 1VS6; X-ray; 3.46 A; D=1-209.
DR PDB; 1VS8; X-ray; 3.46 A; D=1-209.
DR PDB; 1VT2; X-ray; 3.30 A; D=1-209.
DR PDB; 2AW4; X-ray; 3.46 A; D=1-209.
DR PDB; 2AWB; X-ray; 3.46 A; D=1-209.
DR PDB; 2GYA; EM; 15.00 A; B=1-209.
DR PDB; 2GYC; EM; 15.00 A; B=1-209.
DR PDB; 2I2T; X-ray; 3.22 A; D=1-209.
DR PDB; 2I2V; X-ray; 3.22 A; D=1-209.
DR PDB; 2J28; EM; 8.00 A; D=1-209.
DR PDB; 2QAM; X-ray; 3.21 A; D=1-209.
DR PDB; 2QAO; X-ray; 3.21 A; D=1-209.
DR PDB; 2QBA; X-ray; 3.54 A; D=1-209.
DR PDB; 2QBC; X-ray; 3.54 A; D=1-209.
DR PDB; 2QBE; X-ray; 3.30 A; D=1-209.
DR PDB; 2QBG; X-ray; 3.30 A; D=1-209.
DR PDB; 2QBI; X-ray; 4.00 A; D=1-209.
DR PDB; 2QBK; X-ray; 4.00 A; D=1-209.
DR PDB; 2QOV; X-ray; 3.93 A; D=1-209.
DR PDB; 2QOX; X-ray; 3.93 A; D=1-209.
DR PDB; 2QOZ; X-ray; 3.50 A; D=1-209.
DR PDB; 2QP1; X-ray; 3.50 A; D=1-209.
DR PDB; 2RDO; EM; 9.10 A; D=1-209.
DR PDB; 2VHM; X-ray; 3.74 A; D=1-209.
DR PDB; 2VHN; X-ray; 3.74 A; D=1-209.
DR PDB; 2WWQ; EM; 5.80 A; D=1-209.
DR PDB; 2Z4L; X-ray; 4.45 A; D=1-209.
DR PDB; 2Z4N; X-ray; 4.45 A; D=1-209.
DR PDB; 3BBX; EM; 10.00 A; D=1-209.
DR PDB; 3DF2; X-ray; 3.50 A; D=1-209.
DR PDB; 3DF4; X-ray; 3.50 A; D=1-209.
DR PDB; 3E1B; EM; -; Y=1-209.
DR PDB; 3E1D; EM; -; Y=1-209.
DR PDB; 3FIK; EM; 6.70 A; D=1-209.
DR PDB; 3I1N; X-ray; 3.19 A; D=1-209.
DR PDB; 3I1P; X-ray; 3.19 A; D=1-209.
DR PDB; 3I1R; X-ray; 3.81 A; D=1-209.
DR PDB; 3I1T; X-ray; 3.81 A; D=1-209.
DR PDB; 3I20; X-ray; 3.71 A; D=1-209.
DR PDB; 3I22; X-ray; 3.71 A; D=1-209.
DR PDB; 3IZT; EM; -; E=1-209.
DR PDB; 3IZU; EM; -; E=1-209.
DR PDB; 3J01; EM; -; D=1-209.
DR PDB; 3J0T; EM; 12.10 A; E=1-209.
DR PDB; 3J0W; EM; 14.70 A; E=1-209.
DR PDB; 3J0Y; EM; 13.50 A; E=1-209.
DR PDB; 3J11; EM; 13.10 A; E=1-209.
DR PDB; 3J12; EM; 11.50 A; E=1-209.
DR PDB; 3J14; EM; 11.50 A; E=1-209.
DR PDB; 3J19; EM; 8.30 A; D=1-209.
DR PDB; 3KCR; EM; -; D=1-209.
DR PDB; 3OAS; X-ray; 3.25 A; D=1-209.
DR PDB; 3OAT; X-ray; 3.25 A; D=1-209.
DR PDB; 3OFC; X-ray; 3.19 A; D=1-209.
DR PDB; 3OFD; X-ray; 3.19 A; D=1-209.
DR PDB; 3OFQ; X-ray; 3.10 A; D=1-209.
DR PDB; 3OFR; X-ray; 3.10 A; D=1-209.
DR PDB; 3OFZ; X-ray; 3.29 A; D=1-209.
DR PDB; 3OG0; X-ray; 3.29 A; D=1-209.
DR PDB; 3ORB; X-ray; 3.30 A; D=1-209.
DR PDB; 3R8S; X-ray; 3.00 A; D=1-209.
DR PDB; 3R8T; X-ray; 3.00 A; D=1-209.
DR PDB; 3SGF; X-ray; 3.20 A; D=1-209.
DR PDB; 3UOS; X-ray; 3.70 A; D=1-209.
DR PDB; 4GAR; X-ray; 3.30 A; D=1-209.
DR PDB; 4GAU; X-ray; 3.30 A; D=1-209.
DR PDBsum; 1ML5; -.
DR PDBsum; 1P85; -.
DR PDBsum; 1P86; -.
DR PDBsum; 1VS6; -.
DR PDBsum; 1VS8; -.
DR PDBsum; 1VT2; -.
DR PDBsum; 2AW4; -.
DR PDBsum; 2AWB; -.
DR PDBsum; 2GYA; -.
DR PDBsum; 2GYC; -.
DR PDBsum; 2I2T; -.
DR PDBsum; 2I2V; -.
DR PDBsum; 2J28; -.
DR PDBsum; 2QAM; -.
DR PDBsum; 2QAO; -.
DR PDBsum; 2QBA; -.
DR PDBsum; 2QBC; -.
DR PDBsum; 2QBE; -.
DR PDBsum; 2QBG; -.
DR PDBsum; 2QBI; -.
DR PDBsum; 2QBK; -.
DR PDBsum; 2QOV; -.
DR PDBsum; 2QOX; -.
DR PDBsum; 2QOZ; -.
DR PDBsum; 2QP1; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 2VHM; -.
DR PDBsum; 2VHN; -.
DR PDBsum; 2WWQ; -.
DR PDBsum; 2Z4L; -.
DR PDBsum; 2Z4N; -.
DR PDBsum; 3BBX; -.
DR PDBsum; 3DF2; -.
DR PDBsum; 3DF4; -.
DR PDBsum; 3E1B; -.
DR PDBsum; 3E1D; -.
DR PDBsum; 3FIK; -.
DR PDBsum; 3I1N; -.
DR PDBsum; 3I1P; -.
DR PDBsum; 3I1R; -.
DR PDBsum; 3I1T; -.
DR PDBsum; 3I20; -.
DR PDBsum; 3I22; -.
DR PDBsum; 3IZT; -.
DR PDBsum; 3IZU; -.
DR PDBsum; 3J01; -.
DR PDBsum; 3J0T; -.
DR PDBsum; 3J0W; -.
DR PDBsum; 3J0Y; -.
DR PDBsum; 3J11; -.
DR PDBsum; 3J12; -.
DR PDBsum; 3J14; -.
DR PDBsum; 3J19; -.
DR PDBsum; 3KCR; -.
DR PDBsum; 3OAS; -.
DR PDBsum; 3OAT; -.
DR PDBsum; 3OFC; -.
DR PDBsum; 3OFD; -.
DR PDBsum; 3OFQ; -.
DR PDBsum; 3OFR; -.
DR PDBsum; 3OFZ; -.
DR PDBsum; 3OG0; -.
DR PDBsum; 3ORB; -.
DR PDBsum; 3R8S; -.
DR PDBsum; 3R8T; -.
DR PDBsum; 3SGF; -.
DR PDBsum; 3UOS; -.
DR PDBsum; 4GAR; -.
DR PDBsum; 4GAU; -.
DR ProteinModelPortal; P60438; -.
DR SMR; P60438; 1-209.
DR IntAct; P60438; 144.
DR MINT; MINT-1302843; -.
DR STRING; 511145.b3320; -.
DR PaxDb; P60438; -.
DR PRIDE; P60438; -.
DR EnsemblBacteria; AAC76345; AAC76345; b3320.
DR EnsemblBacteria; BAE77971; BAE77971; BAE77971.
DR GeneID; 12932298; -.
DR GeneID; 947817; -.
DR KEGG; ecj:Y75_p3856; -.
DR KEGG; eco:b3320; -.
DR PATRIC; 32122072; VBIEscCol129921_3413.
DR EchoBASE; EB0859; -.
DR EcoGene; EG10866; rplC.
DR eggNOG; COG0087; -.
DR HOGENOM; HOG000100368; -.
DR KO; K02906; -.
DR OMA; KGMRMAG; -.
DR ProtClustDB; PRK00001; -.
DR BioCyc; EcoCyc:EG10866-MONOMER; -.
DR BioCyc; ECOL316407:JW3282-MONOMER; -.
DR EvolutionaryTrace; P60438; -.
DR Genevestigator; P60438; -.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:HAMAP.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1; -.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1 209 50S ribosomal protein L3.
FT /FTId=PRO_0000077098.
FT MOD_RES 38 38 N6-succinyllysine.
FT MOD_RES 150 150 N5-methylglutamine.
FT STRAND 4 15
FT TURN 17 19
FT STRAND 21 28
FT STRAND 32 38
FT HELIX 40 43
FT STRAND 47 53
FT HELIX 57 59
FT HELIX 62 71
FT STRAND 77 83
FT TURN 91 93
FT HELIX 98 102
FT STRAND 103 105
FT STRAND 106 112
FT STRAND 115 118
FT HELIX 121 125
FT STRAND 132 135
FT STRAND 136 138
FT STRAND 140 142
FT TURN 150 152
FT HELIX 155 157
FT STRAND 162 164
FT STRAND 166 181
FT HELIX 182 184
FT STRAND 186 191
FT STRAND 194 196
FT STRAND 200 205
SQ SEQUENCE 209 AA; 22244 MW; EA8E10EDD2C0A8FD CRC64;
MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV TTGAKKANRV
TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL FADVKKVDVT GTSKGKGFAG
TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ TPGKVFKGKK MAGQMGNERV TVQSLDVVRV
DAERNLLLVK GAVPGATGSD LIVKPAVKA
//
