RL2_AQUPY
ID RL2_AQUPY Reviewed; 295 AA.
AC Q9ZI47;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
GN Synonyms=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320};
OS Aquifex pyrophilus.
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=2714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX PubMed=10795828; DOI=10.1007/s002399910040;
RA Bocchetta M., Gribaldo S., Sanangelantoni A.M., Cammarano P.;
RT "Phylogenetic depth of the bacterial genera Aquifex and Thermotoga inferred
RT from analysis of ribosomal protein, elongation factor, and RNA polymerase
RT subunit sequences.";
RL J. Mol. Evol. 50:366-380(2000).
CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; AF040100; AAD08788.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZI47; -.
DR SMR; Q9ZI47; -.
DR PRIDE; Q9ZI47; -.
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:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..295
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129523"
FT REGION 243..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 295 AA; 33313 MW; 70CBCC5EB100C105 CRC64;
MGVRKLKPVT NGTRHAVLYD FEEIEKLVRK GKELVLVKKN KVEPEKSLLK WWHRAKGRSR
QRGNITARHR GGGHKKLYRI IDFERDKSLV PAKVVSIEYD PFRSARICLL HYADGEKRYI
IWPEGLKVGD TVMSISWEDA EAGKPLPEIK PGNAMPLKYI PEGTIIHNIE FMPGKGGQIA
RAAGTWAQVL GRSTKKGYVL VRMPSGEVRM IHERCMATIG RVGLAEHELV NVGKAGRARW
LGWRPHTRGT AMNPVDHPHG GGEGRTRGKH PESPWDGRRR DTRREGVRST PISLS