ID   RL2_XYLFA               Reviewed;         275 AA.
AC   Q9PE73;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=XF_1155;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(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; AE003849; AAF83965.1; -; Genomic_DNA.
DR   PIR; C82717; C82717.
DR   RefSeq; WP_010893671.1; NC_002488.3.
DR   AlphaFoldDB; Q9PE73; -.
DR   SMR; Q9PE73; -.
DR   STRING; 160492.XF_1155; -.
DR   EnsemblBacteria; AAF83965; AAF83965; XF_1155.
DR   KEGG; xfa:XF_1155; -.
DR   eggNOG; COG0090; Bacteria.
DR   HOGENOM; CLU_036235_2_1_6; -.
DR   OMA; SCIELRP; -.
DR   Proteomes; UP000000812; 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   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..275
FT                   /note="50S ribosomal protein L2"
FT                   /id="PRO_0000129655"
FT   REGION          226..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   275 AA;  30061 MW;  F215E62EEB9582E9 CRC64;
     MPLIKFKPTS PGRRSAARVV TPNIHKGSPH AALLEPQSKT GGRNHHGRIT VRHIGGGCKQ
     RYRVIDFKRD KEAIPARVER IEYDPNRTAH IALLCYVDGE RCYIIAPKGL KEGDKIISGP
     NVPIKLGNSL PLRNIPVGTT VHAVELKPSK GAQMARSAGS SVQLVAREGV YATLRLRSGE
     MRRVLAECRA TIGEVGNEEH NLRKLGKAGA KRWLGVRPTV RGAAMNPVDH PHGGGEAKSG
     QGNPHPVTPW GVPTKGYKTR KNKRTQQFII RGRRG