ID   RL1_PHOPR               Reviewed;         233 AA.
AC   Q6LLV9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=PBPRA3435;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378674; CAG21719.1; -; Genomic_DNA.
DR   RefSeq; WP_011219960.1; NC_006370.1.
DR   AlphaFoldDB; Q6LLV9; -.
DR   SMR; Q6LLV9; -.
DR   STRING; 298386.PBPRA3435; -.
DR   EnsemblBacteria; CAG21719; CAG21719; PBPRA3435.
DR   KEGG; ppr:PBPRA3435; -.
DR   eggNOG; COG0081; Bacteria.
DR   HOGENOM; CLU_062853_0_0_6; -.
DR   OMA; GWTDVDV; -.
DR   OrthoDB; 1671455at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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..233
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_0000125707"
SQ   SEQUENCE   233 AA;  24693 MW;  11E58A647BD5AC0B CRC64;
     MAKITKRMRV IRDKVDATKS YDINEAVVLL KELATAKFVE SVDVAINLGI DARKSDQNVR
     GATVLPHGTG RDIRVAVFTQ GANAEAAKEA GADLIGMDDL ADQVKKGIMD FDVVIASPDA
     MRVVGQLGTI LGPRGLMPNP KVGTVTPNVA QAVKNAKAGQ VRYRNDKNGI IHTTIGKVDF
     DAAQLKENLE SLLVALKKSK PSSAKGIFIK KISISTTMGA GVSLDQGTLE ASI