RL2_GEOSE
ID RL2_GEOSE Reviewed; 276 AA.
AC P04257; O82995;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
DE Short=BstL2;
DE AltName: Full=L3;
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kimura M.;
RT "Nucleotide sequence of the genes encoding the ribosomal proteins L23 and
RT L2 from the Bacillus stearothermophilus ribosome.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-276.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=2222862; DOI=10.1515/bchm3.1990.371.2.631;
RA Kroemer W.J., Hatakeyama T., Kimura M.;
RT "Nucleotide sequences of Bacillus stearothermophilus ribosomal protein
RT genes: part of the ribosomal S10 operon.";
RL Biol. Chem. Hoppe-Seyler 371:631-636(1990).
RN [3]
RP PROTEIN SEQUENCE OF 2-276.
RX PubMed=3908098; DOI=10.1111/j.1432-1033.1985.tb09299.x;
RA Kimura M., Kimura J., Watanabe K.;
RT "The primary structure of ribosomal protein L2 from Bacillus
RT stearothermophilus.";
RL Eur. J. Biochem. 153:289-297(1985).
RN [4]
RP PROTEIN SEQUENCE OF 239-247, AND CROSS-LINKING TO RRNA.
RC STRAIN=799;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 61-202.
RX PubMed=10075918; DOI=10.1093/emboj/18.6.1459;
RA Nakagawa A., Nakashima T., Taniguchi M., Hosaka H., Kimura M., Tanaka I.;
RT "The three-dimensional structure of the RNA-binding domain of ribosomal
RT protein L2; a protein at the peptidyl transferase center of the ribosome.";
RL EMBO J. 18:1459-1467(1999).
RN [6]
RP 3D-STRUCTURE MODELING OF 62-197 ONTO THE H.MARISMORTUI 50S RIBOSOME.
RX PubMed=10476961; DOI=10.1038/23641;
RA Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.;
RT "Placement of protein and RNA structures into a 5 A-resolution map of the
RT 50S ribosomal subunit.";
RL Nature 400:841-847(1999).
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; AB015722; BAA31210.1; -; Genomic_DNA.
DR EMBL; X54994; CAA38737.1; -; Genomic_DNA.
DR PIR; A02759; R5BS2F.
DR PDB; 1ML5; EM; 14.00 A; d=61-233.
DR PDB; 1RL2; X-ray; 2.30 A; A/B=61-197.
DR PDB; 4V4R; X-ray; 5.90 A; D=61-197.
DR PDB; 4V4S; X-ray; 6.76 A; D=61-197.
DR PDB; 4V4T; X-ray; 6.46 A; D=61-197.
DR PDBsum; 1ML5; -.
DR PDBsum; 1RL2; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR AlphaFoldDB; P04257; -.
DR SMR; P04257; -.
DR EvolutionaryTrace; P04257; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3908098"
FT CHAIN 2..276
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129528"
FT REGION 224..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40
FT /note="R -> K (in Ref. 1; BAA31210)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="A -> R (in Ref. 1; BAA31210)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="Q -> L (in Ref. 1; BAA31210)"
FT /evidence="ECO:0000305"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1RL2"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1RL2"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1RL2"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1RL2"
SQ SEQUENCE 276 AA; 30331 MW; 871DBC74317C3AAD CRC64;
MAIKKYKPTS NGRRGMTVLD FSEITTDQPE KSLLAPLKKR AGRNNQGKIT VRHQGGGHKR
QYRIIDFKRD KDGIPGRVAT IEYDPNRSAN IALINYADGE KRYIIAPKNL KVGMEIMSGP
DADIKIGNAL PLENIPVGTL VHNIELKPGR GGQLVRAAGT SAQVLGKEGK YVIVRLASGE
VRMILGKCRA TVGEVGNEQH ELVNIGKAGR ARWLGIRPTV RGSVMNPVDH PHGGGEGKAP
IGRKSPMTPW GKPTLGYKTR KKKNKSDKFI IRRRKK
