RL1_CORU7
ID RL1_CORU7 Reviewed; 238 AA.
AC B1VEQ9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=cu0288;
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=504474;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109;
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
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; AM942444; CAQ04248.1; -; Genomic_DNA.
DR RefSeq; WP_012359549.1; NC_010545.1.
DR AlphaFoldDB; B1VEQ9; -.
DR SMR; B1VEQ9; -.
DR STRING; 504474.cu0288; -.
DR PRIDE; B1VEQ9; -.
DR EnsemblBacteria; CAQ04248; CAQ04248; cu0288.
DR GeneID; 60605093; -.
DR KEGG; cur:cu0288; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_11; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 1671455at2; -.
DR Proteomes; UP000001727; 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_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 3: Inferred from homology;
KW Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT CHAIN 1..238
FT /note="50S ribosomal protein L1"
FT /id="PRO_1000141383"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 25160 MW; 604860E6716B24B2 CRC64;
MSKVSKAYRE AAAKVDRDNK YTPLQAAKLA KATSSKNYDA TIDVAIRLGV DPRKADQLVR
GTVALPNGTG KDVRVVVFAE GPNATAAEEA GADFVGSAEL IEKIQGGWTD FDAAIATPDQ
MAKVGRVARV LGPRGLMPNP KTGTVTTDVA KAVSEIKGGK ISFRVDKASN LHALIGKASF
DEKKLAENYG ALIDELLRIK PSSSKGKYIK KVTLSSTNGP GVPVDETIQK NYADDAEA