GenomeNet

Database: UniProt
Entry: P60438
LinkDB: P60438
Original site: P60438 
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   30-AUG-2017, entry version 141.
DE   RecName: Full=50S ribosomal protein L3;
DE   AltName: Full=Large ribosomal subunit protein uL3 {ECO:0000303|PubMed:24524803};
GN   Name=rplC; OrderedLocusNames=b3320, JW3282;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   PROTEIN SEQUENCE, SUBUNIT, 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 277:1453-1462(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, AND SUBUNIT.
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   NOMENCLATURE.
RX   PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA   Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA   Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA   Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA   Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA   Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT   "A new system for naming ribosomal proteins.";
RL   Curr. Opin. Struct. Biol. 24:165-169(2014).
RN   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
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   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP   STRUCTURES, AND SUBUNIT.
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).
RN   [16]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S
RP   RIBOSOMAL SUBUNIT, AND SUBUNIT.
RC   STRAIN=K12 / A19 / KC6;
RX   PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA   Bischoff L., Berninghausen O., Beckmann R.;
RT   "Molecular basis for the ribosome functioning as an L-tryptophan
RT   sensor.";
RL   Cell Rep. 9:469-475(2014).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 50S RIBOSOMAL
RP   SUBUNIT IN COMPLEX WITH OBGE AND GMP-PNP, AND SUBUNIT.
RX   PubMed=24844575; DOI=10.1371/journal.pbio.1001866;
RA   Feng B., Mandava C.S., Guo Q., Wang J., Cao W., Li N., Zhang Y.,
RA   Zhang Y., Wang Z., Wu J., Sanyal S., Lei J., Gao N.;
RT   "Structural and functional insights into the mode of action of a
RT   universally conserved Obg GTPase.";
RL   PLoS Biol. 12:E1001866-E1001866(2014).
RN   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27906160; DOI=10.1038/nature20822;
RA   Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT   "Mechanistic insights into the alternative translation termination by
RT   ArfA and RF2.";
RL   Nature 541:550-553(2017).
RN   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27906161; DOI=10.1038/nature20821;
RA   Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O.,
RA   Beckmann R., Wilson D.N.;
RT   "Structural basis for ArfA-RF2-mediated translation termination on
RT   mRNAs lacking stop codons.";
RL   Nature 541:546-549(2017).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=27934701; DOI=10.1126/science.aai9127;
RA   James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT   "Translational termination without a stop codon.";
RL   Science 354:1437-1440(2016).
RN   [21]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP   COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX   PubMed=28077875; DOI=10.1038/nature21053;
RA   Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA   Jin H.;
RT   "Structural basis of co-translational quality control by ArfA and RF2
RT   bound to ribosome.";
RL   Nature 541:554-557(2017).
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds
CC       directly near the 3'-end of the 23S rRNA, where it nucleates
CC       assembly of the 50S subunit. {ECO:0000269|PubMed:3298242,
CC       ECO:0000269|PubMed:6760192}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:365579,
CC       PubMed:10094780, PubMed:12809609, PubMed:16272117,
CC       PubMed:25310980, PubMed:24844575, PubMed:27934701,
CC       PubMed:27906160, PubMed:27906161). Forms a cluster with proteins
CC       L14 and L19. {ECO:0000269|PubMed:10094780,
CC       ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117,
CC       ECO:0000269|PubMed:24844575, ECO:0000269|PubMed:25310980,
CC       ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC       ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:365579}.
CC   -!- PTM: Methylated by PrmB. {ECO:0000269|PubMed:11847124}.
CC   -!- MASS SPECTROMETRY: Mass=22257.2; Method=MALDI; Range=1-209;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000305}.
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_000913.3.
DR   RefSeq; WP_000579833.1; NZ_LN832404.1.
DR   PDB; 1ML5; EM; 14.00 A; e=2-209.
DR   PDB; 2J28; EM; 8.00 A; D=1-209.
DR   PDB; 2RDO; EM; 9.10 A; D=1-209.
DR   PDB; 3BBX; EM; 10.00 A; D=1-209.
DR   PDB; 3J5L; EM; 6.60 A; D=1-209.
DR   PDB; 3J7Z; EM; 3.90 A; D=1-209.
DR   PDB; 3J8G; EM; 5.00 A; D=1-209.
DR   PDB; 3J9Y; EM; 3.90 A; D=1-209.
DR   PDB; 3J9Z; EM; 3.60 A; LX=1-209.
DR   PDB; 3JA1; EM; 3.60 A; LE=1-209.
DR   PDB; 3JBU; EM; 3.64 A; d=1-209.
DR   PDB; 3JBV; EM; 3.32 A; d=1-209.
DR   PDB; 3JCD; EM; 3.70 A; D=1-209.
DR   PDB; 3JCE; EM; 3.20 A; D=1-209.
DR   PDB; 3JCJ; EM; 3.70 A; C=1-209.
DR   PDB; 3JCN; EM; 4.60 A; D=1-209.
DR   PDB; 4CSU; EM; 5.50 A; D=1-209.
DR   PDB; 4U1U; X-ray; 2.95 A; BD/DD=1-209.
DR   PDB; 4U1V; X-ray; 3.00 A; BD/DD=1-209.
DR   PDB; 4U20; X-ray; 2.90 A; BD/DD=1-209.
DR   PDB; 4U24; X-ray; 2.90 A; BD/DD=1-209.
DR   PDB; 4U25; X-ray; 2.90 A; BD/DD=1-209.
DR   PDB; 4U26; X-ray; 2.80 A; BD/DD=1-209.
DR   PDB; 4U27; X-ray; 2.80 A; BD/DD=1-209.
DR   PDB; 4UY8; EM; 3.80 A; D=1-209.
DR   PDB; 4V47; EM; 12.30 A; AB=1-209.
DR   PDB; 4V48; EM; 11.50 A; AB=1-209.
DR   PDB; 4V4H; X-ray; 3.46 A; BD/DD=1-209.
DR   PDB; 4V4Q; X-ray; 3.46 A; BD/DD=1-209.
DR   PDB; 4V4V; EM; 15.00 A; BB=1-209.
DR   PDB; 4V4W; EM; 15.00 A; BB=1-209.
DR   PDB; 4V50; X-ray; 3.22 A; BD/DD=1-209.
DR   PDB; 4V52; X-ray; 3.21 A; BD/DD=1-209.
DR   PDB; 4V53; X-ray; 3.54 A; BD/DD=1-209.
DR   PDB; 4V54; X-ray; 3.30 A; BD/DD=1-209.
DR   PDB; 4V55; X-ray; 4.00 A; BD/DD=1-209.
DR   PDB; 4V56; X-ray; 3.93 A; BD/DD=1-209.
DR   PDB; 4V57; X-ray; 3.50 A; BD/DD=1-209.
DR   PDB; 4V5B; X-ray; 3.74 A; AD/CD=1-209.
DR   PDB; 4V5H; EM; 5.80 A; BD=1-209.
DR   PDB; 4V5Y; X-ray; 4.45 A; BD/DD=1-209.
DR   PDB; 4V64; X-ray; 3.50 A; BD/DD=1-209.
DR   PDB; 4V65; EM; 9.00 A; BY=1-209.
DR   PDB; 4V66; EM; 9.00 A; BY=1-209.
DR   PDB; 4V69; EM; 6.70 A; BD=1-209.
DR   PDB; 4V6C; X-ray; 3.19 A; BD/DD=1-209.
DR   PDB; 4V6D; X-ray; 3.81 A; BD/DD=1-209.
DR   PDB; 4V6E; X-ray; 3.71 A; BD/DD=1-209.
DR   PDB; 4V6K; EM; 8.25 A; AE=1-209.
DR   PDB; 4V6L; EM; 13.20 A; BE=1-209.
DR   PDB; 4V6M; EM; 7.10 A; BD=1-209.
DR   PDB; 4V6N; EM; 12.10 A; AE=1-209.
DR   PDB; 4V6O; EM; 14.70 A; BE=1-209.
DR   PDB; 4V6P; EM; 13.50 A; BE=1-209.
DR   PDB; 4V6Q; EM; 11.50 A; BE=1-209.
DR   PDB; 4V6R; EM; 11.50 A; BE=1-209.
DR   PDB; 4V6S; EM; 13.10 A; AE=1-209.
DR   PDB; 4V6T; EM; 8.30 A; BD=1-209.
DR   PDB; 4V6V; EM; 9.80 A; BE=1-209.
DR   PDB; 4V6Y; EM; 12.00 A; BD=1-209.
DR   PDB; 4V6Z; EM; 12.00 A; BD=1-209.
DR   PDB; 4V70; EM; 17.00 A; BD=1-209.
DR   PDB; 4V71; EM; 20.00 A; BD=1-209.
DR   PDB; 4V72; EM; 13.00 A; BD=1-209.
DR   PDB; 4V73; EM; 15.00 A; BD=1-209.
DR   PDB; 4V74; EM; 17.00 A; BD=1-209.
DR   PDB; 4V75; EM; 12.00 A; BD=1-209.
DR   PDB; 4V76; EM; 17.00 A; BD=1-209.
DR   PDB; 4V77; EM; 17.00 A; BD=1-209.
DR   PDB; 4V78; EM; 20.00 A; BD=1-209.
DR   PDB; 4V79; EM; 15.00 A; BD=1-209.
DR   PDB; 4V7A; EM; 9.00 A; BD=1-209.
DR   PDB; 4V7B; EM; 6.80 A; BD=1-209.
DR   PDB; 4V7C; EM; 7.60 A; BE=1-209.
DR   PDB; 4V7D; EM; 7.60 A; AE=1-209.
DR   PDB; 4V7I; EM; 9.60 A; AD=1-209.
DR   PDB; 4V7S; X-ray; 3.25 A; BD/DD=1-209.
DR   PDB; 4V7T; X-ray; 3.19 A; BD/DD=1-209.
DR   PDB; 4V7U; X-ray; 3.10 A; BD/DD=1-209.
DR   PDB; 4V7V; X-ray; 3.29 A; BD/DD=1-209.
DR   PDB; 4V85; X-ray; 3.20 A; D=1-209.
DR   PDB; 4V89; X-ray; 3.70 A; BD=1-209.
DR   PDB; 4V9C; X-ray; 3.30 A; BD/DD=1-209.
DR   PDB; 4V9D; X-ray; 3.00 A; CD/DD=1-209.
DR   PDB; 4V9O; X-ray; 2.90 A; AD/CD/ED/GD=1-209.
DR   PDB; 4V9P; X-ray; 2.90 A; AD/CD/ED/GD=1-209.
DR   PDB; 4WF1; X-ray; 3.09 A; BD/DD=1-209.
DR   PDB; 4WOI; X-ray; 3.00 A; BD/CD=1-209.
DR   PDB; 4WWW; X-ray; 3.10 A; RD/YD=1-209.
DR   PDB; 4YBB; X-ray; 2.10 A; CD/DD=1-209.
DR   PDB; 5ADY; EM; 4.50 A; D=1-209.
DR   PDB; 5AFI; EM; 2.90 A; D=1-209.
DR   PDB; 5AKA; EM; 5.70 A; D=1-209.
DR   PDB; 5GAD; EM; 3.70 A; D=1-209.
DR   PDB; 5GAE; EM; 3.33 A; D=1-209.
DR   PDB; 5GAF; EM; 4.30 A; D=1-209.
DR   PDB; 5GAG; EM; 3.80 A; D=1-209.
DR   PDB; 5GAH; EM; 3.80 A; D=1-209.
DR   PDB; 5H5U; EM; 3.00 A; D=1-209.
DR   PDB; 5IQR; EM; 3.00 A; C=1-209.
DR   PDB; 5IT8; X-ray; 3.12 A; CD/DD=1-209.
DR   PDB; 5J5B; X-ray; 2.80 A; CD/DD=1-209.
DR   PDB; 5J7L; X-ray; 3.00 A; CD/DD=1-209.
DR   PDB; 5J88; X-ray; 3.32 A; CD/DD=1-209.
DR   PDB; 5J8A; X-ray; 3.10 A; CD/DD=1-209.
DR   PDB; 5J91; X-ray; 2.96 A; CD/DD=1-209.
DR   PDB; 5JC9; X-ray; 3.03 A; CD/DD=1-209.
DR   PDB; 5JTE; EM; 3.60 A; BD=1-209.
DR   PDB; 5JU8; EM; 3.60 A; BD=1-209.
DR   PDB; 5KCR; EM; 3.60 A; 1E=1-209.
DR   PDB; 5KCS; EM; 3.90 A; 1E=1-209.
DR   PDB; 5KPS; EM; 3.90 A; C=1-209.
DR   PDB; 5KPV; EM; 4.10 A; B=1-209.
DR   PDB; 5KPW; EM; 3.90 A; B=1-209.
DR   PDB; 5KPX; EM; 3.90 A; B=1-209.
DR   PDB; 5L3P; EM; 3.70 A; E=1-209.
DR   PDB; 5LZA; EM; 3.60 A; D=1-209.
DR   PDB; 5LZB; EM; 5.30 A; D=1-209.
DR   PDB; 5LZC; EM; 4.80 A; D=1-209.
DR   PDB; 5LZD; EM; 3.40 A; D=1-209.
DR   PDB; 5LZE; EM; 3.50 A; D=1-209.
DR   PDB; 5LZF; EM; 4.60 A; D=1-209.
DR   PDB; 5MDV; EM; 2.97 A; C=1-209.
DR   PDB; 5MDW; EM; 3.06 A; C=1-209.
DR   PDB; 5MDY; EM; 3.35 A; C=1-209.
DR   PDB; 5MDZ; EM; 3.10 A; C=1-209.
DR   PDB; 5MGP; EM; 3.10 A; D=1-209.
DR   PDB; 5NCO; EM; 4.80 A; D=1-209.
DR   PDB; 5NP6; EM; 3.60 A; b=1-209.
DR   PDB; 5U4I; EM; 3.50 A; D=1-209.
DR   PDB; 5U9F; EM; 3.20 A; 05=1-209.
DR   PDB; 5U9G; EM; 3.20 A; 05=1-209.
DR   PDB; 5UYK; EM; 3.90 A; 05=1-209.
DR   PDB; 5UYL; EM; 3.60 A; 05=1-209.
DR   PDB; 5UYM; EM; 3.20 A; 05=1-209.
DR   PDB; 5UYN; EM; 4.00 A; 05=1-209.
DR   PDB; 5UYP; EM; 3.90 A; 05=1-209.
DR   PDB; 5UYQ; EM; 3.80 A; 05=1-209.
DR   PDBsum; 1ML5; -.
DR   PDBsum; 2J28; -.
DR   PDBsum; 2RDO; -.
DR   PDBsum; 3BBX; -.
DR   PDBsum; 3J5L; -.
DR   PDBsum; 3J7Z; -.
DR   PDBsum; 3J8G; -.
DR   PDBsum; 3J9Y; -.
DR   PDBsum; 3J9Z; -.
DR   PDBsum; 3JA1; -.
DR   PDBsum; 3JBU; -.
DR   PDBsum; 3JBV; -.
DR   PDBsum; 3JCD; -.
DR   PDBsum; 3JCE; -.
DR   PDBsum; 3JCJ; -.
DR   PDBsum; 3JCN; -.
DR   PDBsum; 4CSU; -.
DR   PDBsum; 4U1U; -.
DR   PDBsum; 4U1V; -.
DR   PDBsum; 4U20; -.
DR   PDBsum; 4U24; -.
DR   PDBsum; 4U25; -.
DR   PDBsum; 4U26; -.
DR   PDBsum; 4U27; -.
DR   PDBsum; 4UY8; -.
DR   PDBsum; 4V47; -.
DR   PDBsum; 4V48; -.
DR   PDBsum; 4V4H; -.
DR   PDBsum; 4V4Q; -.
DR   PDBsum; 4V4V; -.
DR   PDBsum; 4V4W; -.
DR   PDBsum; 4V50; -.
DR   PDBsum; 4V52; -.
DR   PDBsum; 4V53; -.
DR   PDBsum; 4V54; -.
DR   PDBsum; 4V55; -.
DR   PDBsum; 4V56; -.
DR   PDBsum; 4V57; -.
DR   PDBsum; 4V5B; -.
DR   PDBsum; 4V5H; -.
DR   PDBsum; 4V5Y; -.
DR   PDBsum; 4V64; -.
DR   PDBsum; 4V65; -.
DR   PDBsum; 4V66; -.
DR   PDBsum; 4V69; -.
DR   PDBsum; 4V6C; -.
DR   PDBsum; 4V6D; -.
DR   PDBsum; 4V6E; -.
DR   PDBsum; 4V6K; -.
DR   PDBsum; 4V6L; -.
DR   PDBsum; 4V6M; -.
DR   PDBsum; 4V6N; -.
DR   PDBsum; 4V6O; -.
DR   PDBsum; 4V6P; -.
DR   PDBsum; 4V6Q; -.
DR   PDBsum; 4V6R; -.
DR   PDBsum; 4V6S; -.
DR   PDBsum; 4V6T; -.
DR   PDBsum; 4V6V; -.
DR   PDBsum; 4V6Y; -.
DR   PDBsum; 4V6Z; -.
DR   PDBsum; 4V70; -.
DR   PDBsum; 4V71; -.
DR   PDBsum; 4V72; -.
DR   PDBsum; 4V73; -.
DR   PDBsum; 4V74; -.
DR   PDBsum; 4V75; -.
DR   PDBsum; 4V76; -.
DR   PDBsum; 4V77; -.
DR   PDBsum; 4V78; -.
DR   PDBsum; 4V79; -.
DR   PDBsum; 4V7A; -.
DR   PDBsum; 4V7B; -.
DR   PDBsum; 4V7C; -.
DR   PDBsum; 4V7D; -.
DR   PDBsum; 4V7I; -.
DR   PDBsum; 4V7S; -.
DR   PDBsum; 4V7T; -.
DR   PDBsum; 4V7U; -.
DR   PDBsum; 4V7V; -.
DR   PDBsum; 4V85; -.
DR   PDBsum; 4V89; -.
DR   PDBsum; 4V9C; -.
DR   PDBsum; 4V9D; -.
DR   PDBsum; 4V9O; -.
DR   PDBsum; 4V9P; -.
DR   PDBsum; 4WF1; -.
DR   PDBsum; 4WOI; -.
DR   PDBsum; 4WWW; -.
DR   PDBsum; 4YBB; -.
DR   PDBsum; 5ADY; -.
DR   PDBsum; 5AFI; -.
DR   PDBsum; 5AKA; -.
DR   PDBsum; 5GAD; -.
DR   PDBsum; 5GAE; -.
DR   PDBsum; 5GAF; -.
DR   PDBsum; 5GAG; -.
DR   PDBsum; 5GAH; -.
DR   PDBsum; 5H5U; -.
DR   PDBsum; 5IQR; -.
DR   PDBsum; 5IT8; -.
DR   PDBsum; 5J5B; -.
DR   PDBsum; 5J7L; -.
DR   PDBsum; 5J88; -.
DR   PDBsum; 5J8A; -.
DR   PDBsum; 5J91; -.
DR   PDBsum; 5JC9; -.
DR   PDBsum; 5JTE; -.
DR   PDBsum; 5JU8; -.
DR   PDBsum; 5KCR; -.
DR   PDBsum; 5KCS; -.
DR   PDBsum; 5KPS; -.
DR   PDBsum; 5KPV; -.
DR   PDBsum; 5KPW; -.
DR   PDBsum; 5KPX; -.
DR   PDBsum; 5L3P; -.
DR   PDBsum; 5LZA; -.
DR   PDBsum; 5LZB; -.
DR   PDBsum; 5LZC; -.
DR   PDBsum; 5LZD; -.
DR   PDBsum; 5LZE; -.
DR   PDBsum; 5LZF; -.
DR   PDBsum; 5MDV; -.
DR   PDBsum; 5MDW; -.
DR   PDBsum; 5MDY; -.
DR   PDBsum; 5MDZ; -.
DR   PDBsum; 5MGP; -.
DR   PDBsum; 5NCO; -.
DR   PDBsum; 5NP6; -.
DR   PDBsum; 5U4I; -.
DR   PDBsum; 5U9F; -.
DR   PDBsum; 5U9G; -.
DR   PDBsum; 5UYK; -.
DR   PDBsum; 5UYL; -.
DR   PDBsum; 5UYM; -.
DR   PDBsum; 5UYN; -.
DR   PDBsum; 5UYP; -.
DR   PDBsum; 5UYQ; -.
DR   ProteinModelPortal; P60438; -.
DR   SMR; P60438; -.
DR   DIP; DIP-10744N; -.
DR   IntAct; P60438; 144.
DR   MINT; MINT-1302843; -.
DR   STRING; 316385.ECDH10B_3495; -.
DR   PaxDb; P60438; -.
DR   PRIDE; P60438; -.
DR   EnsemblBacteria; AAC76345; AAC76345; b3320.
DR   EnsemblBacteria; BAE77971; BAE77971; BAE77971.
DR   GeneID; 947817; -.
DR   KEGG; ecj:JW3282; -.
DR   KEGG; eco:b3320; -.
DR   PATRIC; fig|1411691.4.peg.3411; -.
DR   EchoBASE; EB0859; -.
DR   EcoGene; EG10866; rplC.
DR   eggNOG; ENOG4105EEE; Bacteria.
DR   eggNOG; COG0087; LUCA.
DR   HOGENOM; HOG000100368; -.
DR   InParanoid; P60438; -.
DR   KO; K02906; -.
DR   PhylomeDB; P60438; -.
DR   BioCyc; EcoCyc:EG10866-MONOMER; -.
DR   BioCyc; MetaCyc:EG10866-MONOMER; -.
DR   EvolutionaryTrace; P60438; -.
DR   PRO; PR:P60438; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:CAFA.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IDA:CAFA.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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_B-barrel.
DR   PANTHER; PTHR11229; PTHR11229; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 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                                {ECO:0000269|PubMed:21151122}.
FT   MOD_RES     150    150       N5-methylglutamine.
FT                                {ECO:0000269|PubMed:365579}.
FT   STRAND        4     15       {ECO:0000244|PDB:5GAE}.
FT   STRAND       21     28       {ECO:0000244|PDB:5GAE}.
FT   STRAND       32     38       {ECO:0000244|PDB:5GAE}.
FT   TURN         40     42       {ECO:0000244|PDB:5GAE}.
FT   STRAND       43     45       {ECO:0000244|PDB:5GAE}.
FT   STRAND       47     51       {ECO:0000244|PDB:5GAE}.
FT   TURN         57     59       {ECO:0000244|PDB:5GAE}.
FT   HELIX        62     71       {ECO:0000244|PDB:5GAE}.
FT   STRAND       80     83       {ECO:0000244|PDB:5GAE}.
FT   HELIX        98    101       {ECO:0000244|PDB:5GAE}.
FT   STRAND      105    112       {ECO:0000244|PDB:5GAE}.
FT   STRAND      117    119       {ECO:0000244|PDB:5GAE}.
FT   HELIX       121    125       {ECO:0000244|PDB:5GAE}.
FT   STRAND      132    135       {ECO:0000244|PDB:5GAE}.
FT   STRAND      140    142       {ECO:0000244|PDB:5GAE}.
FT   STRAND      163    166       {ECO:0000244|PDB:5GAE}.
FT   STRAND      168    181       {ECO:0000244|PDB:5GAE}.
FT   TURN        182    185       {ECO:0000244|PDB:5GAE}.
FT   STRAND      186    191       {ECO:0000244|PDB:5GAE}.
FT   STRAND      200    205       {ECO:0000244|PDB:5GAE}.
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
//
DBGET integrated database retrieval system