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   04-NOV-2026, entry version 139.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000255|HAMAP-Rule:MF_01320};
DE   AltName: Full=50S ribosomal protein L2 {ECO:0000303|PubMed:9920395};
DE            Short=BL2 {ECO:0000303|PubMed:3908098};
DE            Short=BstL2 {ECO:0000303|PubMed:9920395};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320,
GN   ECO:0000303|PubMed:2222862};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae;
OC   Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], 23S RNA-BINDING, AND MUTAGENESIS OF
RP   PHE-67; 68-LYS-ARG-69; ARG-69; 71-LYS--ARG-77; ARG-87; TYR-96; TYR-103;
RP   147-LYS--ARG-156 AND ARG-156.
RC   STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX   PubMed=9920395; DOI=10.1016/s0167-4838(98)00230-1;
RA   Harada N., Maemura K., Yamasaki N., Kimura M.;
RT   "Identification by site-directed mutagenesis of amino acid residues in
RT   ribosomal protein L2 that are essential for binding to 23S ribosomal RNA.";
RL   Biochim. Biophys. Acta 1429:176-186(1998).
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, AND SUBUNIT.
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.
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: Component of the large ribosomal subunit. The ribosome is a
CC       large ribonucleoprotein complex responsible for the synthesis of
CC       proteins in the cell. {ECO:0000255|HAMAP-Rule:MF_01320}.
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
CC       (Probable). Makes several contacts with the 16S rRNA in the 70S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_01320,
CC       ECO:0000305|PubMed:10075918}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:3908098). Forms a
CC       bridge to the 30S subunit in the 70S ribosome. {ECO:0000255|HAMAP-
CC       Rule:MF_01320, ECO:0000269|PubMed:3908098}.
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; 4V42; X-ray; 5.50 A; BD=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   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:0002181; P:cytoplasmic translation; IEA:TreeGrafter.
DR   FunFam; 2.30.30.30:FF:000001; 50S ribosomal protein L2; 1.
DR   FunFam; 2.40.50.140:FF:000003; 50S ribosomal protein L2; 1.
DR   FunFam; 4.10.950.10:FF:000001; 50S ribosomal protein L2; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR   HAMAP; MF_01320_B; Ribosomal_uL2_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002171; Ribosomal_uL2.
DR   InterPro; IPR005880; Ribosomal_uL2_bact_org.
DR   InterPro; IPR022669; Ribosomal_uL2_C.
DR   InterPro; IPR022671; Ribosomal_uL2_CS.
DR   InterPro; IPR014726; Ribosomal_uL2_dom3.
DR   InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   NCBIfam; TIGR01171; rplB_bact; 1.
DR   PANTHER; PTHR13691:SF5; LARGE RIBOSOMAL SUBUNIT PROTEIN UL2M; 1.
DR   PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   Pfam; PF00181; Ribosomal_L2_N; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 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="Large ribosomal subunit protein uL2"
FT                   /id="PRO_0000129528"
FT   REGION          224..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..276
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         67
FT                   /note="F->A: Loss of 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         68..69
FT                   /note="KR->QQ: 10-fold reduction in 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         69
FT                   /note="R->Q: 5-fold reduction in 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         71..77
FT                   /note="KDGIPGR->QDGIPGQ: 5-fold reduction in 23S
FT                   rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         87
FT                   /note="R->Q: 10-fold reduction in 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         96
FT                   /note="Y->A: Near loss of 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         103
FT                   /note="Y->A: Near loss of 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         147..156
FT                   /note="KPGRGGQLVR->QPGQGGQLVQ: 10-fold reduction in 23S
FT                   rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
FT   MUTAGEN         156
FT                   /note="R->Q: 10-fold reduction in 23S rRNA-binding."
FT                   /evidence="ECO:0000269|PubMed:9920395"
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
//