RL1_METVS
ID RL1_METVS Reviewed; 213 AA.
AC P15824; A6URP8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
DE AltName: Full=Ribosomal protein ML6;
GN Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=Mevan_1273;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2107529; DOI=10.1093/nar/18.4.719;
RA Baier G., Piendl W., Redl B., Stoeffler G.;
RT "Structure, organization and evolution of the L1 equivalent ribosomal
RT protein gene of the archaebacterium Methanococcus vannielii.";
RL Nucleic Acids Res. 18:719-724(1990).
RN [2]
RP SEQUENCE REVISION.
RA Piendl W.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP AUTOGENOUS TRANSLATIONAL REPRESSOR.
RX PubMed=8288536; DOI=10.1128/jb.176.2.409-418.1994;
RA Hanner M., Mayer C., Koehrer C., Golderer G., Groebner P., Piendl W.;
RT "Autogenous translational regulation of the ribosomal MvaL1 operon in the
RT archaebacterium Methanococcus vannielii.";
RL J. Bacteriol. 176:409-418(1994).
RN [5]
RP BINDING TO ENDOGENOUS 23S RRNA AND TO 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).
RN [6]
RP MECHANISM OF TRANSLATION REGULATION, AND BINDING TO 23S RRNA.
RX PubMed=9484899; DOI=10.1046/j.1365-2958.1998.00693.x;
RA Mayer C., Koehrer C., Groebner P., Piendl W.;
RT "MvaL1 autoregulates the synthesis of the three ribosomal proteins encoded
RT on the MvaL1 operon of the archaeon Methanococcus vannielii by inhibiting
RT its own translation before or at the formation of the first peptide bond.";
RL Mol. Microbiol. 27:455-468(1998).
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 the L1 operon by binding to its mRNA. Thus
CC it also controls transcription of L10 and L12 by translational
CC coupling. Unlike the case in E.coli, where the site is in the
CC untranslated mRNA leader, this site is within the L1 protein's
CC structural gene.
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; X16023; CAA34156.1; -; Genomic_DNA.
DR EMBL; CP000742; ABR55170.1; -; Genomic_DNA.
DR PIR; S08390; R5MX1.
DR RefSeq; WP_012066085.1; NC_009634.1.
DR AlphaFoldDB; P15824; -.
DR SMR; P15824; -.
DR STRING; 406327.Mevan_1273; -.
DR EnsemblBacteria; ABR55170; ABR55170; Mevan_1273.
DR GeneID; 5324661; -.
DR KEGG; mvn:Mevan_1273; -.
DR eggNOG; arCOG04289; Archaea.
DR HOGENOM; CLU_062853_4_0_2; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 70269at2157; -.
DR Proteomes; UP000001107; 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 Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT CHAIN 1..213
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125804"
FT CONFLICT 40
FT /note="P -> H (in Ref. 1; CAA34156)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..133
FT /note="QPV -> TPL (in Ref. 1; CAA34156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23074 MW; 7B47BAC8AB82A101 CRC64;
MDSAQIQKAV KEARTLAKPR NFTQSVDLIV NLKELDLTRP ENRLKEQIVL PSGKGKDTKI
AVIAKGDLAA QAAEMGLTVI RQEELEELGK NKKAAKRIAN EHGFFIAQAD MMPLVGKSLG
PVLGPRGKMP QPVPGNANLA PLVARFKKTV AINTRDKSLF QVYIGTEAMS DEEIAANAEA
ILNVVAKKYE KGLYHVKSAF TKLTMGAAAP ISK
