RL1_MALP2
ID RL1_MALP2 Reviewed; 336 AA.
AC Q8EX24;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=50S ribosomal protein L1;
GN Name=rplA; OrderedLocusNames=MYPE260;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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 (By similarity).
CC {ECO:0000250}.
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:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
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DR EMBL; BA000026; BAC43816.1; -; Genomic_DNA.
DR RefSeq; WP_011076852.1; NC_004432.1.
DR AlphaFoldDB; Q8EX24; -.
DR SMR; Q8EX24; -.
DR STRING; 272633.26453484; -.
DR PRIDE; Q8EX24; -.
DR EnsemblBacteria; BAC43816; BAC43816; BAC43816.
DR KEGG; mpe:MYPE260; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_825898_0_0_14; -.
DR OrthoDB; 1671455at2; -.
DR Proteomes; UP000002522; 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; 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 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..336
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125692"
FT REGION 1..231
FT /note="50S ribosomal protein L1"
FT REGION 232..336
FT /note="Unknown"
FT REGION 267..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 36892 MW; 10E913C25033CDA8 CRC64;
MANQKKVTNK TPKKPSVNFD RTKFYTIEEA VNLAKQTSNA KFLSSIDIAI KLNLDTSKSD
QQLRGTVSLP YFFGKEKRIL VLDKGLTQKD AKSLGVNHAG DSELIAEISK GWLDFDLIIT
TPKMMPELSK LGKILGTRGL MPNPKNGNVT TDLPKTIAEF KKGINQYRTD SYGNIHMVVG
KANADTAKIV ENINFLLSFI AAKRLTSVKG IFIEKVNLSS TMGPGIRVLV NKTAVVKKTA
KGKVIADDSA KGENKKPAYL IQRVKYAQKK KPSKHPENPP VITEAKKKKV KKILKKAKPA
KKAAVAKKPV VVNKKTATKK SPAKKGDVKK AKTSKK
