RL1_AQUAE
ID RL1_AQUAE Reviewed; 242 AA.
AC O67759;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=aq_1935;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC the ribosome, and is involved in E site tRNA release.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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:0000255|HAMAP-Rule:MF_01318}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01318}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; AE000657; AAC07725.1; -; Genomic_DNA.
DR PIR; C70466; C70466.
DR RefSeq; NP_214328.1; NC_000918.1.
DR RefSeq; WP_010881264.1; NC_000918.1.
DR PDB; 3QOY; X-ray; 2.10 A; A=1-242.
DR PDBsum; 3QOY; -.
DR AlphaFoldDB; O67759; -.
DR SMR; O67759; -.
DR STRING; 224324.aq_1935; -.
DR EnsemblBacteria; AAC07725; AAC07725; aq_1935.
DR KEGG; aae:aq_1935; -.
DR PATRIC; fig|224324.8.peg.1498; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_0; -.
DR InParanoid; O67759; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 1671455at2; -.
DR Proteomes; UP000000798; 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_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..242
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125605"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3QOY"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:3QOY"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3QOY"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:3QOY"
SQ SEQUENCE 242 AA; 26908 MW; C9A9EB8ED36C4E67 CRC64;
MARRGKKYIE ASKLVDRNKR YTLEEAVDLL KKMEEVLQRR FDETVELAMR LNVDPRYADQ
MVRGSVVLPH GLGKPIKVVV FAEGEYAKKA EEAGADYVGG DELINKILKE EWTDFDVAIA
TPEMMPKVAK LGRILGPRGL MPSPKTGTVT TNVEQAIKDA KRGRVEFKVD KAGNVHMPVG
KISFEKEKLI DNLYAAIDAV VRAKPPGAKG QYIKNMAVSL TMSPSVKLDI NEVLKKLQEK
AA
