ID   RL2_RHOPA               Reviewed;         278 AA.
AC   P60403;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
DE   AltName: Full=RRP-L2;
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=RPA3247;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=15473684; DOI=10.1021/pr049940z;
RA   Strader M.B., VerBerkmoes N.C., Tabb D.L., Connelly H.M., Barton J.W.,
RA   Bruce B.D., Pelletier D.A., Davison B.H., Hettich R.L., Larimer F.W.,
RA   Hurst G.B.;
RT   "Characterization of the 70S ribosome from Rhodopseudomonas palustris using
RT   an integrated 'top-down' and 'bottom-up' mass spectrometric approach.";
RL   J. Proteome Res. 3:965-978(2004).
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   -!- MISCELLANEOUS: The initiator methionine may be removed.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR   EMBL; BX572603; CAE28688.1; -; Genomic_DNA.
DR   RefSeq; WP_011158792.1; NC_005296.1.
DR   AlphaFoldDB; P60403; -.
DR   SMR; P60403; -.
DR   IntAct; P60403; 1.
DR   STRING; 258594.RPA3247; -.
DR   PRIDE; P60403; -.
DR   EnsemblBacteria; CAE28688; CAE28688; RPA3247.
DR   GeneID; 66894333; -.
DR   KEGG; rpa:RPA3247; -.
DR   eggNOG; COG0090; Bacteria.
DR   HOGENOM; CLU_036235_2_1_5; -.
DR   OMA; SCIELRP; -.
DR   PhylomeDB; P60403; -.
DR   BioCyc; RPAL258594:TX73_RS16565-MON; -.
DR   Proteomes; UP000001426; 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: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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..278
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129606"
FT   REGION          222..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  30644 MW;  1FF246657A6E3282 CRC64;
     MALKTFNPTT PGQRQLVMVD RSALYKGKPV KRLTEGKNSN GGRNNTGRIT VRFRGGGHKQ
     AYRLVDFKRT KVDVPAKVER LEYDPNRTAF IALIKYEDGE QAYILAPQRL AVGDTVIAGA
     YVDVKPGNVM PLGNMPIGTI VHNVELKIGK GGQLARSAGT YAQIVGRDHD YVILRMNSGE
     QRLIHGRCIA AIGAVSNPDH MNISIGKAGR KRWLGRRPHN RGVVMNPIDH PHGGGEGRTS
     GGRHPVTPWG KPTKGKKTRS NKSTDKFILI SRHKRKKK