RL1_METJA
ID RL1_METJA Reviewed; 219 AA.
AC P54050;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=MJ0510;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP BINDING TO ENDOGENOUS 23S RRNA, AND BINDING TO METHANOCOCCUS VANNIELII L1
RP MRNA.
RX PubMed=9746351; DOI=10.1046/j.1432-1327.1998.2560097.x;
RA Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W.;
RT "Interaction of ribosomal L1 proteins from mesophilic and thermophilic
RT Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA.";
RL Eur. J. Biochem. 256:97-105(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10801481; DOI=10.1016/s0969-2126(00)00116-7;
RA Nevskaya N., Tischenko S., Fedorov R., Al-Karadaghi S., Liljas A.,
RA Kraft A., Piendl W., Garber M.B., Nikonov S.;
RT "Archaeal ribosomal protein L1: the structure provides new insights into
RT RNA binding of the L1 protein family.";
RL Structure 8:363-371(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=12037305; DOI=10.1107/s0907444902006157;
RA Nevskaya N., Tishchenko S., Paveliev M., Smolinskaya Y., Fedorov R.,
RA Piendl W., Nakamura Y., Toyoda T., Garber M.B., Nikonov S.;
RT "Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus.
RT Functionally important structural invariants on the L1 surface.";
RL Acta Crystallogr. D 58:1023-1029(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH AN ENDOGENOUS L1 MRNA
RP FRAGMENT.
RX PubMed=15659579; DOI=10.1093/nar/gki194;
RA Nevskaya N., Tishchenko S., Gabdoulkhakov A., Nikonova E., Nikonov O.,
RA Nikulin A., Platonova O., Garber M.B., Nikonov S., Piendl W.;
RT "Ribosomal protein L1 recognizes the same specific structural motif in its
RT target sites on the autoregulatory mRNA and 23S rRNA.";
RL Nucleic Acids Res. 33:478-485(2005).
CC -!- FUNCTION: Probably involved in E site tRNA release (By similarity).
CC Binds directly to 23S rRNA. {ECO:0000250}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of its operon by binding to its mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01318, ECO:0000269|PubMed:15659579}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98500.1; ALT_INIT; Genomic_DNA.
DR PIR; F64363; F64363.
DR RefSeq; WP_064496520.1; NC_000909.1.
DR PDB; 1CJS; X-ray; 2.30 A; A=1-219.
DR PDB; 1I2A; X-ray; 1.85 A; A=1-219.
DR PDB; 1U63; X-ray; 3.40 A; A/C=1-219.
DR PDB; 4LQ4; X-ray; 1.75 A; A=1-211.
DR PDBsum; 1CJS; -.
DR PDBsum; 1I2A; -.
DR PDBsum; 1U63; -.
DR PDBsum; 4LQ4; -.
DR AlphaFoldDB; P54050; -.
DR SMR; P54050; -.
DR STRING; 243232.MJ_0510; -.
DR EnsemblBacteria; AAB98500; AAB98500; MJ_0510.
DR GeneID; 1451372; -.
DR KEGG; mja:MJ_0510; -.
DR eggNOG; arCOG04289; Archaea.
DR HOGENOM; CLU_062853_4_0_2; -.
DR InParanoid; P54050; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 70269at2157; -.
DR PhylomeDB; P54050; -.
DR EvolutionaryTrace; P54050; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_A; Ribosomal_L1_A; 1.
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; IPR023669; Ribosomal_L1_arc.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repressor; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW tRNA-binding.
FT CHAIN 1..219
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125798"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:4LQ4"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:4LQ4"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:4LQ4"
SQ SEQUENCE 219 AA; 24793 MW; BEFF3E31B693F9EA CRC64;
MDREALLQAV KEARELAKPR NFTQSFEFIA TLKEIDMRKP ENRIKTEVVL PHGRGKEAKI
AVIGTGDLAK QAEELGLTVI RKEEIEELGK NKRKLRKIAK AHDFFIAQAD LMPLIGRYMG
VILGPRGKMP KPVPANANIK PLVERLKKTV VINTRDKPYF QVLVGNEKMT DEQIVDNIEA
VLNVVAKKYE KGLYHIKDAY VKLTMGPAVK VKKEKAKKK
