ID   RL1_GEOSE               Reviewed;         233 AA.
AC   P04447;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-233.
RX   PubMed=4018095; DOI=10.1111/j.1432-1033.1985.tb09049.x;
RA   Kimura M., Kimura J., Ashman K.;
RT   "The complete primary structure of ribosomal proteins L1, L14, L15, L23,
RT   L24 and L29 from Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 150:491-497(1985).
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   PIR; A02755; R5BS1.
DR   AlphaFoldDB; P04447; -.
DR   SMR; P04447; -.
DR   PRIDE; P04447; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Repressor; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4018095"
FT   CHAIN           2..233
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_0000125615"
SQ   SEQUENCE   233 AA;  24971 MW;  D7B93B9F148668DE CRC64;
     MPKRGKKYLE ALKLVDRSKA YPIAEAIELV KKTNVAKFDA TVEVAFRLGV DPKKADQQIR
     GAVVLPHGTG KVARVLVFAK GEKAKEAEAA GADYVGDTEY INKIQQGWFD FDVVVATPDM
     MGEVGKLGRI LGPKGLMPDP KTGTVTFDVA KAVQEIKAGK VEYRVDKAGN IHVPIGKVSF
     DNEKLAENFA AVYEALIKAK PAAAKGTYVK NVTITSTMGP GIKVDPTTVA VAQ