RL1_DEIRA
ID RL1_DEIRA Reviewed; 233 AA.
AC Q9RSS8;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=50S ribosomal protein L1;
GN Name=rplA; OrderedLocusNames=DR_2045;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP STRUCTURE OF THE 50S SUBUNIT.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=11733066; DOI=10.1016/s0092-8674(01)00546-3;
RA Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I.,
RA Bartels H., Franceschi F., Yonath A.;
RT "High resolution structure of the large ribosomal subunit from a mesophilic
RT eubacterium.";
RL Cell 107:679-688(2001).
CC -!- FUNCTION: Binds directly to 23S rRNA. Forms the L1 stalk. Unlike the
CC case in the Thermus thermophilus 70S ribosome, this protein is not seen
CC to block the exit path of the E site tRNA. It is clear that the protein
CC in the structure is flexible however, so this is probably due to its
CC position in these crystals.
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 {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF11592.1; -; Genomic_DNA.
DR PIR; F75323; F75323.
DR RefSeq; NP_295768.1; NC_001263.1.
DR RefSeq; WP_010888677.1; NZ_CP015081.1.
DR PDB; 5DM6; X-ray; 2.90 A; 0=6-229.
DR PDB; 5DM7; X-ray; 3.00 A; 0=6-229.
DR PDBsum; 5DM6; -.
DR PDBsum; 5DM7; -.
DR AlphaFoldDB; Q9RSS8; -.
DR SMR; Q9RSS8; -.
DR STRING; 243230.DR_2045; -.
DR EnsemblBacteria; AAF11592; AAF11592; DR_2045.
DR KEGG; dra:DR_2045; -.
DR PATRIC; fig|243230.17.peg.2272; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_0; -.
DR InParanoid; Q9RSS8; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 1671455at2; -.
DR Proteomes; UP000002524; Chromosome I.
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_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; Reference proteome; Repressor; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW tRNA-binding.
FT CHAIN 1..233
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125651"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 85..91
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5DM6"
SQ SEQUENCE 233 AA; 24360 MW; 477D83811EE1A5FC CRC64;
MPKHGKRYRA LEGKVDRNKQ YSIDEAAALV KELATAKFDE TVEVHFRLGI DPRKSDQNVR
GTVALPHGTG RSVRVAVITK GENVQAAEAA GADVVGSDEL IERIAGGFMD FDAVVATPDM
MAQIGQKLAR LLGPRGLLPN PKSGTVGADV AGMVRGLKAG RIEFRNDKTG VVHAPIGKAS
FESGNLSANY QALISALEGA KPGTAKGVFL RSAYLTTTMG PSIPLALGGA ALA
