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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   01-APR-2015, entry version 119.
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 277:1453-1462(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.
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 initiator 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. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=22257.2; Method=MALDI; Range=1-209;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- SIMILARITY: Belongs to the ribosomal protein L3P family.
CC       {ECO:0000305}.
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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_000913.3.
DR   RefSeq; YP_492112.1; NC_007779.1.
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; 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; 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; 4WWW; X-ray; 3.10 A; RD/YD=1-209.
DR   PDBsum; 1ML5; -.
DR   PDBsum; 2J28; -.
DR   PDBsum; 2RDO; -.
DR   PDBsum; 3BBX; -.
DR   PDBsum; 3J5L; -.
DR   PDBsum; 3J7Z; -.
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; 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; 4WWW; -.
DR   ProteinModelPortal; P60438; -.
DR   SMR; P60438; 1-209.
DR   DIP; DIP-10744N; -.
DR   IntAct; P60438; 144.
DR   MINT; MINT-1302843; -.
DR   STRING; 511145.b3320; -.
DR   ChEMBL; CHEMBL2363135; -.
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   InParanoid; P60438; -.
DR   KO; K02906; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; EOG6WDSMH; -.
DR   PhylomeDB; P60438; -.
DR   BioCyc; EcoCyc:EG10866-MONOMER; -.
DR   BioCyc; ECOL316407:JW3282-MONOMER; -.
DR   EvolutionaryTrace; P60438; -.
DR   PRO; PR:P60438; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   Genevestigator; P60438; -.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:EcoCyc.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-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_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:4U26}.
FT   TURN         17     19       {ECO:0000244|PDB:4U24}.
FT   STRAND       21     28       {ECO:0000244|PDB:4U26}.
FT   STRAND       32     38       {ECO:0000244|PDB:4U26}.
FT   TURN         40     43       {ECO:0000244|PDB:4U26}.
FT   STRAND       47     53       {ECO:0000244|PDB:4U26}.
FT   HELIX        57     59       {ECO:0000244|PDB:4U26}.
FT   HELIX        62     71       {ECO:0000244|PDB:4U26}.
FT   STRAND       77     83       {ECO:0000244|PDB:4U26}.
FT   TURN         91     93       {ECO:0000244|PDB:4V9O}.
FT   HELIX        98    101       {ECO:0000244|PDB:4U26}.
FT   TURN        102    104       {ECO:0000244|PDB:4U24}.
FT   STRAND      106    112       {ECO:0000244|PDB:4U26}.
FT   STRAND      115    119       {ECO:0000244|PDB:4U26}.
FT   HELIX       121    125       {ECO:0000244|PDB:4U26}.
FT   STRAND      132    135       {ECO:0000244|PDB:4V7U}.
FT   STRAND      136    138       {ECO:0000244|PDB:4V4Q}.
FT   STRAND      140    142       {ECO:0000244|PDB:4U26}.
FT   TURN        150    152       {ECO:0000244|PDB:4U26}.
FT   HELIX       155    157       {ECO:0000244|PDB:4V4Q}.
FT   STRAND      163    181       {ECO:0000244|PDB:4U26}.
FT   HELIX       182    184       {ECO:0000244|PDB:4U26}.
FT   STRAND      186    191       {ECO:0000244|PDB:4U26}.
FT   STRAND      194    196       {ECO:0000244|PDB:4V7T}.
FT   STRAND      199    205       {ECO:0000244|PDB:4U26}.
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
//
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