ID RL19_ECOLI Reviewed; 115 AA.
AC P0A7K6; P02420;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 01-MAY-2013, entry version 85.
DE RecName: Full=50S ribosomal protein L19;
GN Name=rplS; OrderedLocusNames=b2606, JW2587;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
RC STRAIN=K12;
RX PubMed=6357787;
RA Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.;
RT "The nucleotide sequence of an Escherichia coli operon containing
RT genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16
RT and L19 and a 21-K polypeptide.";
RL EMBO J. 2:899-905(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
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 PROTEIN SEQUENCE OF 2-115.
RX PubMed=339951; DOI=10.1021/bi00596a021;
RA Brosius J., Arfsten U.;
RT "Primary structure of protein L19 from the large subunit of
RT Escherichia coli ribosomes.";
RL Biochemistry 17:508-516(1978).
RN [6]
RP CROSS-LINKING TO L14.
RX PubMed=2665813; DOI=10.1021/bi00435a071;
RA Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.;
RT "Comparative cross-linking study on the 50S ribosomal subunit from
RT Escherichia coli.";
RL Biochemistry 28:4099-4105(1989).
RN [7]
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 [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND INTERSUBUNIT
RP BRIDGE FORMATION.
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 [9]
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: This protein is located at the 30S-50S ribosomal subunit
CC interface. In the 70S ribosome (PubMed:12809609) it has been
CC modeled to make two contacts with the 16S rRNA of the 30S subunit
CC forming part of bridges B6 and B8. In the 3.5 A resolved
CC structures (PubMed:16272117) L14 and L19 interact and together
CC make contact with the 16S rRNA. The protein conformation is quite
CC different between the 50S and 70S structures, which may be
CC necessary for translocation.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts L14
CC (PubMed:2665813 and PubMed:16272117). Forms two bridges to the 30S
CC subunit in the 70S ribosome, contacting the 16S rRNA.
CC -!- INTERACTION:
CC P0A761:nanE; NbExp=1; IntAct=EBI-543891, EBI-561432;
CC -!- INDUCTION: Part of the rpsP-rimM-trmD-rplS operon.
CC -!- MASS SPECTROMETRY: Mass=13001.7; Method=MALDI; Range=2-115;
CC Source=PubMed:10094780;
CC -!- SIMILARITY: Belongs to the ribosomal protein L19P family.
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DR EMBL; X01818; CAA25960.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75655.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16491.1; -; Genomic_DNA.
DR PIR; S07951; R5EC19.
DR RefSeq; NP_417097.1; NC_000913.2.
DR RefSeq; YP_490829.1; NC_007779.1.
DR PDB; 1P85; EM; 12.30 A; N=2-115.
DR PDB; 1P86; EM; 11.50 A; N=2-115.
DR PDB; 1VS6; X-ray; 3.46 A; P=2-114.
DR PDB; 1VS8; X-ray; 3.46 A; P=1-115.
DR PDB; 1VT2; X-ray; 3.30 A; P=1-115.
DR PDB; 2AW4; X-ray; 3.46 A; P=2-115.
DR PDB; 2AWB; X-ray; 3.46 A; P=2-115.
DR PDB; 2GYA; EM; 15.00 A; N=2-114.
DR PDB; 2GYC; EM; 15.00 A; N=2-115.
DR PDB; 2I2T; X-ray; 3.22 A; P=2-114.
DR PDB; 2I2V; X-ray; 3.22 A; P=2-114.
DR PDB; 2J28; EM; 8.00 A; P=2-115.
DR PDB; 2QAM; X-ray; 3.21 A; P=2-115.
DR PDB; 2QAO; X-ray; 3.21 A; P=2-115.
DR PDB; 2QBA; X-ray; 3.54 A; P=2-115.
DR PDB; 2QBC; X-ray; 3.54 A; P=2-115.
DR PDB; 2QBE; X-ray; 3.30 A; P=2-115.
DR PDB; 2QBG; X-ray; 3.30 A; P=2-115.
DR PDB; 2QBI; X-ray; 4.00 A; P=2-115.
DR PDB; 2QBK; X-ray; 4.00 A; P=2-115.
DR PDB; 2QOV; X-ray; 3.93 A; P=2-115.
DR PDB; 2QOX; X-ray; 3.93 A; P=2-115.
DR PDB; 2QOZ; X-ray; 3.50 A; P=2-115.
DR PDB; 2QP1; X-ray; 3.50 A; P=2-115.
DR PDB; 2RDO; EM; 9.10 A; P=2-115.
DR PDB; 2VHM; X-ray; 3.74 A; P=2-115.
DR PDB; 2VHN; X-ray; 3.74 A; P=2-115.
DR PDB; 2WWQ; EM; 5.80 A; P=2-115.
DR PDB; 2Z4L; X-ray; 4.45 A; P=2-115.
DR PDB; 2Z4N; X-ray; 4.45 A; P=2-115.
DR PDB; 3BBX; EM; 10.00 A; P=2-115.
DR PDB; 3DF2; X-ray; 3.50 A; P=2-114.
DR PDB; 3DF4; X-ray; 3.50 A; P=2-114.
DR PDB; 3E1B; EM; -; I=1-115.
DR PDB; 3E1D; EM; -; I=1-115.
DR PDB; 3FIK; EM; 6.70 A; P=2-115.
DR PDB; 3I1N; X-ray; 3.19 A; P=1-115.
DR PDB; 3I1P; X-ray; 3.19 A; P=1-115.
DR PDB; 3I1R; X-ray; 3.81 A; P=1-115.
DR PDB; 3I1T; X-ray; 3.81 A; P=1-115.
DR PDB; 3I20; X-ray; 3.71 A; P=1-115.
DR PDB; 3I22; X-ray; 3.71 A; P=1-115.
DR PDB; 3IZT; EM; -; Q=1-115.
DR PDB; 3IZU; EM; -; Q=1-115.
DR PDB; 3J01; EM; -; P=2-115.
DR PDB; 3J0T; EM; 12.10 A; R=2-114.
DR PDB; 3J0W; EM; 14.70 A; R=2-114.
DR PDB; 3J0Y; EM; 13.50 A; R=2-114.
DR PDB; 3J11; EM; 13.10 A; R=2-114.
DR PDB; 3J12; EM; 11.50 A; R=2-114.
DR PDB; 3J14; EM; 11.50 A; R=2-114.
DR PDB; 3J19; EM; 8.30 A; P=2-115.
DR PDB; 3KCR; EM; -; P=1-115.
DR PDB; 3OAS; X-ray; 3.25 A; P=2-115.
DR PDB; 3OAT; X-ray; 3.25 A; P=2-115.
DR PDB; 3OFC; X-ray; 3.19 A; P=2-115.
DR PDB; 3OFD; X-ray; 3.19 A; P=2-115.
DR PDB; 3OFQ; X-ray; 3.10 A; P=2-115.
DR PDB; 3OFR; X-ray; 3.10 A; P=2-115.
DR PDB; 3OFZ; X-ray; 3.29 A; P=2-115.
DR PDB; 3OG0; X-ray; 3.29 A; P=2-115.
DR PDB; 3ORB; X-ray; 3.30 A; P=1-115.
DR PDB; 3R8S; X-ray; 3.00 A; P=2-115.
DR PDB; 3R8T; X-ray; 3.00 A; P=2-115.
DR PDB; 3SGF; X-ray; 3.20 A; T=1-115.
DR PDB; 3UOS; X-ray; 3.70 A; T=1-115.
DR PDB; 4GAR; X-ray; 3.30 A; P=1-115.
DR PDB; 4GAU; X-ray; 3.30 A; P=1-115.
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; P0A7K6; -.
DR SMR; P0A7K6; 2-115.
DR DIP; DIP-35793N; -.
DR IntAct; P0A7K6; 100.
DR MINT; MINT-1245288; -.
DR STRING; 511145.b2606; -.
DR PhosSite; P0810432; -.
DR PaxDb; P0A7K6; -.
DR PRIDE; P0A7K6; -.
DR EnsemblBacteria; AAC75655; AAC75655; b2606.
DR EnsemblBacteria; BAA16491; BAA16491; BAA16491.
DR GeneID; 12931612; -.
DR GeneID; 947096; -.
DR KEGG; ecj:Y75_p2554; -.
DR KEGG; eco:b2606; -.
DR PATRIC; 32120611; VBIEscCol129921_2704.
DR EchoBASE; EB0873; -.
DR EcoGene; EG10880; rplS.
DR eggNOG; COG0335; -.
DR HOGENOM; HOG000016264; -.
DR KO; K02884; -.
DR OMA; TLKVHVR; -.
DR ProtClustDB; PRK05338; -.
DR BioCyc; EcoCyc:EG10880-MONOMER; -.
DR BioCyc; ECOL316407:JW2587-MONOMER; -.
DR EvolutionaryTrace; P0A7K6; -.
DR Genevestigator; P0A7K6; -.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR HAMAP; MF_00402; Ribosomal_L19; 1; -.
DR InterPro; IPR001857; Ribosomal_L19.
DR InterPro; IPR018257; Ribosomal_L19_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like.
DR PANTHER; PTHR15680; PTHR15680; 1.
DR Pfam; PF01245; Ribosomal_L19; 1.
DR PIRSF; PIRSF002191; Ribosomal_L19; 1.
DR PRINTS; PR00061; RIBOSOMALL19.
DR SUPFAM; SSF50104; Transl_SH3_like; 1.
DR TIGRFAMs; TIGR01024; rplS_bact; 1.
DR PROSITE; PS01015; RIBOSOMAL_L19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 115 50S ribosomal protein L19.
FT /FTId=PRO_0000163451.
FT HELIX 4 9
FT HELIX 10 12
FT STRAND 25 34
FT STRAND 37 51
FT HELIX 54 56
FT STRAND 58 65
FT STRAND 68 75
FT STRAND 76 78
FT STRAND 81 88
FT STRAND 93 95
FT HELIX 98 100
FT TURN 101 103
FT HELIX 105 108
SQ SEQUENCE 115 AA; 13133 MW; 7BD9F2EFB9DDB06B CRC64;
MSNIIKQLEQ EQMKQDVPSF RPGDTVEVKV WVVEGSKKRL QAFEGVVIAI RNRGLHSAFT
VRKISNGEGV ERVFQTHSPV VDSISVKRRG AVRKAKLYYL RERTGKAARI KERLN
//
