RL1_SACS2
ID RL1_SACS2 Reviewed; 218 AA.
AC P96038;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Synonyms=rpl1Ab {ECO:0000255|HAMAP-Rule:MF_01318};
GN OrderedLocusNames=SSO0345;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9252104; DOI=10.1016/s0167-4838(97)00073-3;
RA Geiger M., Groebner P., Piendl W.;
RT "Nucleotide sequence of a gene cluster encoding NusG and the L11-L1-L10-L12
RT ribosomal proteins from the thermophilic archaeon Sulfolobus
RT solfataricus.";
RL Biochim. Biophys. Acta 1340:170-177(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP BINDING TO METHANOCOCCUS VANNIELII 23S RRNA AND TO M.VANNIELII L1 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).
CC -!- FUNCTION: Probably involved in E site tRNA release (By similarity).
CC Binds directly to 23S rRNA (Probable). {ECO:0000250, ECO:0000305}.
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.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; U85262; AAB99525.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40674.1; -; Genomic_DNA.
DR PIR; C90177; C90177.
DR RefSeq; WP_009990633.1; NC_002754.1.
DR AlphaFoldDB; P96038; -.
DR SMR; P96038; -.
DR STRING; 273057.SSO0345; -.
DR EnsemblBacteria; AAK40674; AAK40674; SSO0345.
DR GeneID; 44129315; -.
DR KEGG; sso:SSO0345; -.
DR PATRIC; fig|273057.12.peg.335; -.
DR eggNOG; arCOG04289; Archaea.
DR HOGENOM; CLU_062853_4_0_2; -.
DR InParanoid; P96038; -.
DR OMA; GWTDVDV; -.
DR PhylomeDB; P96038; -.
DR Proteomes; UP000001974; 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 Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT CHAIN 1..218
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125813"
SQ SEQUENCE 218 AA; 24527 MW; A74D93D2EBA80C3A CRC64;
MQIVDRSNLE ASLKLALSPE NNPKRNFVQS VEIIVTFKEV DMKKGDLKLR EIVVLPKPPE
KTKKVLVVPT IQQLEYAKKA EPNTILTKEE LQKLQGNKRA IKKIARQNDW FLIAPDSMAL
VGRILGPALG PRGKFPTPLP NTADISEYIL RFKRSTLVKT KDQPQTQVFI GTESQQIADL
AENALAVLNV IESKGYAQKV RNIYVKTTMG KVVKVELR