RL1_ECOLI
ID RL1_ECOLI Reviewed; 234 AA.
AC P0A7L0; P02384; Q2M8S0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=50S ribosomal protein L1;
DE AltName: Full=Large ribosomal subunit protein uL1 {ECO:0000303|PubMed:24524803};
GN Name=rplA; OrderedLocusNames=b3984, JW3947;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=377281; DOI=10.1073/pnas.76.4.1697;
RA Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.;
RT "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the
RT gene for RNA polymerase subunit beta in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-234.
RC STRAIN=K;
RX PubMed=365581; DOI=10.1016/0014-5793(78)80426-8;
RA Brauer D., Oechsner I.;
RT "The primary structure of protein L1 from the large ribosomal subunit of
RT Escherichia coli.";
RL FEBS Lett. 96:317-321(1978).
RN [6]
RP ERRATUM OF PUBMED:365581.
RA Brauer D., Oechsner I.;
RL FEBS Lett. 98:411-411(1979).
RN [7]
RP PROTEIN SEQUENCE OF 2-13.
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 in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 199-203, AND CROSS-LINKING TO RRNA.
RC STRAIN=MRE-600;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [9]
RP ASSEMBLY MAP OF THE 50S SUBUNIT.
RC STRAIN=K12;
RX PubMed=3298242; DOI=10.1016/s0021-9258(18)47489-3;
RA Herold M., Nierhaus K.H.;
RT "Incorporation of six additional proteins to complete the assembly map of
RT the 50 S subunit from Escherichia coli ribosomes.";
RL J. Biol. Chem. 262:8826-8833(1987).
RN [10]
RP MECHANISM OF TRANSLATION REGULATION.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=3104883; DOI=10.1093/nar/15.7.3085;
RA Thomas M.S., Nomura M.;
RT "Translational regulation of the L11 ribosomal protein operon of
RT Escherichia coli: mutations that define the target site for repression by
RT L1.";
RL Nucleic Acids Res. 15:3085-3096(1987).
RN [11]
RP CROSS-LINKING TO THE TRNA CENTRAL FOLD.
RC STRAIN=MRE-600;
RX PubMed=8524654; DOI=10.1093/nar/23.22.4635;
RA Osswald M., Doering T., Brimacombe R.;
RT "The ribosomal neighbourhood of the central fold of tRNA: cross-links from
RT position 47 of tRNA located at the A, P or E site.";
RL Nucleic Acids Res. 23:4635-4641(1995).
RN [12]
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., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
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 [14]
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 [15]
RP 3D-STRUCTURE MODELING.
RC STRAIN=MRE-600;
RX PubMed=10756104; DOI=10.1006/jmbi.2000.3635;
RA Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J.,
RA Goerlach M., van Heel M., Brimacombe R.;
RT "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S
RT ribosomal subunit based on a cryo-electron microscopic reconstruction at
RT 7.5 A resolution.";
RL J. Mol. Biol. 298:35-59(2000).
RN [16]
RP SUCCINYLATION AT LYS-105; LYS-154; LYS-186 AND LYS-197.
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 [17]
RP 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES IMPLYING THE INVOLVEMENT OF
RP THE L1 STALK IN TRANSLOCATION OF TRNAS FROM THE P TO E SITE.
RX PubMed=12859903; DOI=10.1016/s0092-8674(03)00476-8;
RA Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.;
RT "Locking and unlocking of ribosomal motions.";
RL Cell 114:123-134(2003).
RN [18]
RP LOCALIZATION IN THE 3.5 ANGSTROM RIBOSOMAL STRUCTURES AND DISCUSSION OF ITS
RP MOVEMENT.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A.,
RA 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 [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 50S RIBOSOMAL SUBUNIT
RP IN COMPLEX WITH OBGE AND GMP-PNP.
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., Zhang Y.,
RA 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).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds very close
CC to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often
CC not seen in high-resolution crystal structures, but can be seen in
CC cryo_EM and 3D reconstruction models. These indicate that the distal
CC end of the stalk moves by approximately 20 angstroms (PubMed:12859903,
CC PubMed:16272117). This stalk movement is thought to be coupled to
CC movement of deacylated tRNA into and out of the E site, and thus to
CC participate in tRNA translocation (PubMed:12859903, PubMed:16272117).
CC Contacts the P and E site tRNAs. {ECO:0000269|PubMed:12859903,
CC ECO:0000269|PubMed:16272117}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of the L11 operon by binding to its mRNA.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Cross-links to the P and E
CC site tRNAs.
CC -!- INTERACTION:
CC P0A7L0; P0ABQ0: coaBC; NbExp=2; IntAct=EBI-543771, EBI-548929;
CC P0A7L0; P0A978: cspG; NbExp=3; IntAct=EBI-543771, EBI-547581;
CC P0A7L0; P0ABS5: dnaG; NbExp=2; IntAct=EBI-543771, EBI-549259;
CC P0A7L0; P06710: dnaX; NbExp=2; IntAct=EBI-543771, EBI-549140;
CC P0A7L0; P0A738: moaC; NbExp=2; IntAct=EBI-543771, EBI-554314;
CC P0A7L0; P0A8M3: thrS; NbExp=3; IntAct=EBI-543771, EBI-551254;
CC -!- MASS SPECTROMETRY: Mass=24598.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
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DR EMBL; V00339; CAA23622.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43082.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76958.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77336.1; -; Genomic_DNA.
DR PIR; S12573; R5EC1.
DR RefSeq; NP_418411.1; NC_000913.3.
DR RefSeq; WP_001096684.1; NZ_STEB01000045.1.
DR PDB; 1EG0; EM; 11.50 A; N=1-229.
DR PDB; 1ML5; EM; 14.00 A; c=2-229.
DR PDB; 2RDO; EM; 9.10 A; 9=2-234.
DR PDB; 3J46; EM; 10.10 A; 5=1-234.
DR PDB; 3J5S; EM; 7.50 A; F=1-234.
DR PDB; 3J8G; EM; 5.00 A; 5=1-234.
DR PDB; 3J9Z; EM; 3.60 A; LC=1-234.
DR PDB; 3JA1; EM; 3.60 A; LC=1-234.
DR PDB; 3JCD; EM; 3.70 A; 5=1-234.
DR PDB; 3JCE; EM; 3.20 A; 5=1-234.
DR PDB; 487D; EM; 7.50 A; H=29-201.
DR PDB; 4CSU; EM; 5.50 A; 5=1-234.
DR PDB; 4U1U; X-ray; 2.95 A; B5=2-229.
DR PDB; 4U1V; X-ray; 3.00 A; B5=2-229.
DR PDB; 4U20; X-ray; 2.90 A; B5=2-229.
DR PDB; 4U24; X-ray; 2.90 A; B5=2-229.
DR PDB; 4U25; X-ray; 2.90 A; B5=2-229.
DR PDB; 4U26; X-ray; 2.80 A; B5=2-229.
DR PDB; 4U27; X-ray; 2.80 A; B5=2-229.
DR PDB; 4V4V; EM; 15.00 A; B2=6-227.
DR PDB; 4V4W; EM; 15.00 A; B2=6-227.
DR PDB; 4V5H; EM; 5.80 A; B5=1-234.
DR PDB; 4V65; EM; 9.00 A; BZ=5-220.
DR PDB; 4V66; EM; 9.00 A; BZ=5-220.
DR PDB; 4V69; EM; 6.70 A; B5=1-234.
DR PDB; 4V6K; EM; 8.25 A; AC=1-234.
DR PDB; 4V6L; EM; 13.20 A; BC=1-234.
DR PDB; 4V6M; EM; 7.10 A; B5=1-234.
DR PDB; 4V6N; EM; 12.10 A; AC=1-234.
DR PDB; 4V6O; EM; 14.70 A; BC=1-234.
DR PDB; 4V6P; EM; 13.50 A; BC=1-234.
DR PDB; 4V6Q; EM; 11.50 A; BC=1-234.
DR PDB; 4V6R; EM; 11.50 A; BC=1-234.
DR PDB; 4V6S; EM; 13.10 A; AC=1-234.
DR PDB; 4V6V; EM; 9.80 A; BC=1-234.
DR PDB; 4V6Y; EM; 12.00 A; B5=1-234.
DR PDB; 4V6Z; EM; 12.00 A; B5=1-234.
DR PDB; 4V70; EM; 17.00 A; B5=1-234.
DR PDB; 4V71; EM; 20.00 A; B5=1-234.
DR PDB; 4V72; EM; 13.00 A; B5=1-234.
DR PDB; 4V73; EM; 15.00 A; B5=1-234.
DR PDB; 4V74; EM; 17.00 A; B5=1-234.
DR PDB; 4V75; EM; 12.00 A; B5=1-234.
DR PDB; 4V76; EM; 17.00 A; B5=1-234.
DR PDB; 4V77; EM; 17.00 A; B5=1-234.
DR PDB; 4V78; EM; 20.00 A; B5=1-234.
DR PDB; 4V79; EM; 15.00 A; B5=1-234.
DR PDB; 4V7A; EM; 9.00 A; B5=1-234.
DR PDB; 4V7C; EM; 7.60 A; BC=2-234.
DR PDB; 4V7D; EM; 7.60 A; AC=2-234.
DR PDB; 4V7I; EM; 9.60 A; A5=1-234.
DR PDB; 4WOI; X-ray; 3.00 A; B5=2-229.
DR PDB; 5ADY; EM; 4.50 A; 5=1-234.
DR PDB; 5U9F; EM; 3.20 A; 03=1-234.
DR PDB; 5U9G; EM; 3.20 A; 03=1-234.
DR PDB; 5UYK; EM; 3.90 A; 03=3-225.
DR PDB; 5UYL; EM; 3.60 A; 03=1-234.
DR PDB; 5UYM; EM; 3.20 A; 03=3-225.
DR PDB; 5UYN; EM; 4.00 A; 03=3-225.
DR PDB; 5UYP; EM; 3.90 A; 03=3-225.
DR PDB; 5UYQ; EM; 3.80 A; 03=3-225.
DR PDB; 6BU8; EM; 3.50 A; 03=3-225.
DR PDB; 6ENJ; EM; 3.70 A; 7=6-229.
DR PDB; 6ENU; EM; 3.10 A; 7=6-229.
DR PDB; 6OFX; EM; 3.30 A; a=3-225.
DR PDB; 6OG7; EM; 3.30 A; a=3-225.
DR PDB; 6WD6; EM; 3.70 A; a=3-225.
DR PDB; 6WDB; EM; 4.00 A; a=3-225.
DR PDB; 6WDC; EM; 4.20 A; a=3-225.
DR PDB; 6WDD; EM; 3.20 A; a=3-225.
DR PDB; 6WDE; EM; 3.00 A; a=3-225.
DR PDB; 6WDF; EM; 3.30 A; a=3-225.
DR PDB; 6WDG; EM; 3.30 A; a=3-225.
DR PDB; 6WDH; EM; 4.30 A; a=3-225.
DR PDB; 6WDI; EM; 4.00 A; a=3-225.
DR PDB; 6WDJ; EM; 3.70 A; a=3-225.
DR PDB; 6WDK; EM; 3.60 A; a=3-225.
DR PDB; 6WDL; EM; 3.70 A; a=3-225.
DR PDB; 6WDM; EM; 3.60 A; a=3-225.
DR PDB; 6WNT; EM; 3.10 A; a=3-225.
DR PDB; 6WNV; EM; 3.50 A; a=3-225.
DR PDB; 6WNW; EM; 3.20 A; a=3-225.
DR PDB; 7JSZ; EM; 3.70 A; a=1-234.
DR PDB; 7K50; EM; 3.40 A; a=3-225.
DR PDB; 7K51; EM; 3.50 A; a=3-225.
DR PDB; 7K52; EM; 3.40 A; a=3-225.
DR PDB; 7K53; EM; 3.20 A; a=3-225.
DR PDB; 7K54; EM; 3.20 A; a=3-225.
DR PDB; 7K55; EM; 3.30 A; a=3-225.
DR PDB; 7LV0; EM; 3.20 A; a=3-225.
DR PDB; 7QG8; EM; 3.97 A; C=3-225.
DR PDB; 7QGH; EM; 4.48 A; C=3-225.
DR PDB; 7SS9; EM; 3.90 A; a=1-234.
DR PDB; 7SSD; EM; 3.30 A; a=1-234.
DR PDB; 7SSL; EM; 3.80 A; a=3-225.
DR PDB; 7SSO; EM; 3.20 A; a=3-225.
DR PDB; 7SSW; EM; 3.80 A; a=3-225.
DR PDB; 7ST2; EM; 2.90 A; a=1-234.
DR PDB; 7ST7; EM; 3.20 A; a=3-225.
DR PDBsum; 1EG0; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3J46; -.
DR PDBsum; 3J5S; -.
DR PDBsum; 3J8G; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR PDBsum; 487D; -.
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; 4V4V; -.
DR PDBsum; 4V4W; -.
DR PDBsum; 4V5H; -.
DR PDBsum; 4V65; -.
DR PDBsum; 4V66; -.
DR PDBsum; 4V69; -.
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; 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; 4V7C; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V7I; -.
DR PDBsum; 4WOI; -.
DR PDBsum; 5ADY; -.
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 PDBsum; 6BU8; -.
DR PDBsum; 6ENJ; -.
DR PDBsum; 6ENU; -.
DR PDBsum; 6OFX; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6WD6; -.
DR PDBsum; 6WDB; -.
DR PDBsum; 6WDC; -.
DR PDBsum; 6WDD; -.
DR PDBsum; 6WDE; -.
DR PDBsum; 6WDF; -.
DR PDBsum; 6WDG; -.
DR PDBsum; 6WDH; -.
DR PDBsum; 6WDI; -.
DR PDBsum; 6WDJ; -.
DR PDBsum; 6WDK; -.
DR PDBsum; 6WDL; -.
DR PDBsum; 6WDM; -.
DR PDBsum; 6WNT; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7K50; -.
DR PDBsum; 7K51; -.
DR PDBsum; 7K52; -.
DR PDBsum; 7K53; -.
DR PDBsum; 7K54; -.
DR PDBsum; 7K55; -.
DR PDBsum; 7LV0; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
DR PDBsum; 7SS9; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7SSW; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P0A7L0; -.
DR SMR; P0A7L0; -.
DR BioGRID; 4259509; 105.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35746N; -.
DR IntAct; P0A7L0; 141.
DR STRING; 511145.b3984; -.
DR MoonProt; P0A7L0; -.
DR SWISS-2DPAGE; P0A7L0; -.
DR jPOST; P0A7L0; -.
DR PaxDb; P0A7L0; -.
DR PRIDE; P0A7L0; -.
DR EnsemblBacteria; AAC76958; AAC76958; b3984.
DR EnsemblBacteria; BAE77336; BAE77336; BAE77336.
DR GeneID; 66672105; -.
DR GeneID; 948483; -.
DR KEGG; ecj:JW3947; -.
DR KEGG; eco:b3984; -.
DR PATRIC; fig|1411691.4.peg.2728; -.
DR EchoBASE; EB0857; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_6; -.
DR InParanoid; P0A7L0; -.
DR OMA; GWTDVDV; -.
DR PhylomeDB; P0A7L0; -.
DR BioCyc; EcoCyc:EG10864-MON; -.
DR BioCyc; MetaCyc:EG10864-MON; -.
DR EvolutionaryTrace; P0A7L0; -.
DR PRO; PR:P0A7L0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:CAFA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:CAFA.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR InterPro; IPR005878; Ribosom_L1_bac-type.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR TIGRFAMs; TIGR01169; rplA_bact; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome; Repressor;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:365581,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..234
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125654"
FT MOD_RES 105
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 154
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 186
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 197
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT CONFLICT 12
FT /note="R -> I (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:6WNT"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6WNT"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 167..177
FT /evidence="ECO:0007829|PDB:6WNT"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:6WNT"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6WNT"
SQ SEQUENCE 234 AA; 24730 MW; D751704B34748D53 CRC64;
MAKLTKRMRV IREKVDATKQ YDINEAIALL KELATAKFVE SVDVAVNLGI DARKSDQNVR
GATVLPHGTG RSVRVAVFTQ GANAEAAKAA GAELVGMEDL ADQIKKGEMN FDVVIASPDA
MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA EAVKNAKAGQ VRYRNDKNGI IHTTIGKVDF
DADKLKENLE ALLVALKKAK PTQAKGVYIK KVSISTTMGA GVAVDQAGLS ASVN
