RL1_SULAC
ID RL1_SULAC Reviewed; 221 AA.
AC P35024; Q4J8V1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, 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=Saci_1458;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7966335; DOI=10.1006/jmbi.1994.1723;
RA Ramirez C., Shimmin L.C., Leggatt P., Matheson A.T.;
RT "Structure and transcription of the L11-L1-L10-L12 ribosomal protein gene
RT operon from the extreme thermophilic archaeon Sulfolobus acidocaldarius.";
RL J. Mol. Biol. 244:242-249(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2497941; DOI=10.1139/m89-036;
RA Ramirez C., Shimmin L.C., Newton C.H., Matheson A.T., Dennis P.P.;
RT "Structure and evolution of the L11, L1, L10, and L12 equivalent ribosomal
RT proteins in eubacteria, archaebacteria, and eucaryotes.";
RL Can. J. Microbiol. 35:234-244(1989).
RN [3]
RP ERRATUM OF PUBMED:2497941.
RA Ramirez C., Shimmin L.C., Newton C.H., Matheson A.T., Dennis P.P.;
RL Can. J. Microbiol. 35:975-975(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 5-220 IN COMPLEX WITH A
RP T.THERMOPHILUS RRNA FRAGMENT.
RX PubMed=12514741; DOI=10.1038/nsb886;
RA Nikulin A., Eliseikina I., Tishchenko S., Nevskaya N., Davydova N.,
RA Platonova O., Piendl W., Selmer M., Liljas A., Drygin D., Zimmermann R.,
RA Garber M.B., Nikonov S.;
RT "Structure of the L1 protuberance in the ribosome.";
RL Nat. Struct. Biol. 10:104-108(2003).
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:12514741}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- CAUTION: Was originally thought to originate from S.solfataricus strain
CC P1, but the culture was contaminated with S.acidocaldarius.
CC {ECO:0000305|PubMed:2497941}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY80779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59038; CAA41763.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80779.1; ALT_INIT; Genomic_DNA.
DR PIR; S53649; S53649.
DR PDB; 1MZP; X-ray; 2.65 A; A=5-220.
DR PDB; 4V49; X-ray; 8.70 A; 5=5-220.
DR PDB; 4V4A; X-ray; 9.50 A; 5=5-220.
DR PDB; 4V4G; X-ray; 11.50 A; 7=5-220.
DR PDBsum; 1MZP; -.
DR PDBsum; 4V49; -.
DR PDBsum; 4V4A; -.
DR PDBsum; 4V4G; -.
DR AlphaFoldDB; P35024; -.
DR SMR; P35024; -.
DR STRING; 330779.Saci_1458; -.
DR EnsemblBacteria; AAY80779; AAY80779; Saci_1458.
DR KEGG; sai:Saci_1458; -.
DR PATRIC; fig|330779.12.peg.1402; -.
DR eggNOG; arCOG04289; Archaea.
DR HOGENOM; CLU_062853_4_0_2; -.
DR EvolutionaryTrace; P35024; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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: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..221
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125812"
FT CONFLICT 73
FT /note="F -> S (in Ref. 1; CAA41763 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="N -> K (in Ref. 1; CAA41763 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="R -> I (in Ref. 1; CAA41763 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> I (in Ref. 1; CAA41763 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:1MZP"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1MZP"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:1MZP"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:1MZP"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1MZP"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:1MZP"
SQ SEQUENCE 221 AA; 24935 MW; 47A26B9251F89F2F CRC64;
MKKVLADKES LIEALKLALS TEYNVKRNFT QSVEIILTFK GIDMKKGDLK LREIVPLPKQ
PSKAKRVLVV PSFEQLEYAK KASPNVVITR EELQKLQGQK RPVKKLARQN EWFLINQESM
ALAGRILGPA LGPRGKFPTP LPNTADISEY INRFKRSVLV KTKDQPQVQV FIGTEDMKPE
DLAENAIAVL NAIENKAKVE TNLRNIYVKT TMGKAVKVKR A
