RL1_STAHJ
ID RL1_STAHJ Reviewed; 231 AA.
AC Q4L3J7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=SH2471;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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; AP006716; BAE05780.1; -; Genomic_DNA.
DR RefSeq; WP_011276724.1; NC_007168.1.
DR AlphaFoldDB; Q4L3J7; -.
DR SMR; Q4L3J7; -.
DR STRING; 279808.SH2471; -.
DR EnsemblBacteria; BAE05780; BAE05780; SH2471.
DR GeneID; 58061510; -.
DR KEGG; sha:SH2471; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_9; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 1671455at2; -.
DR Proteomes; UP000000543; 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 Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT CHAIN 1..231
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125739"
SQ SEQUENCE 231 AA; 24983 MW; 6E4E7BFB58DA3E76 CRC64;
MAKKGKKYQE AANKVDRTKH YSVEEAISLA KETSIANFDA SVEVAFRLGI DTRKNDQQIR
GAVVLPNGTG KSQRVLVFAK GDKITEAEEA GADYVGESEY VQKIQQGWFD FDVVVATPDM
MGEVGKLGRV LGPKGLMPNP KTGTVTMDVK KAVEEIKAGK VEYRAEKAGI VHASIGKVSF
SDEKLVENFK TLQDVLAKAK PSSAKGTYFK SVAVTTTMGP GVKIDTSSFK L