RL2_LEIXX
ID RL2_LEIXX Reviewed; 279 AA.
AC Q6ACZ8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=Lxx20300;
OS Leifsonia xyli subsp. xyli (strain CTCB07).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=281090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTCB07;
RX PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT subsp. xyli.";
RL Mol. Plant Microbe Interact. 17:827-836(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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; AE016822; AAT89746.1; -; Genomic_DNA.
DR RefSeq; WP_011186732.1; NC_006087.1.
DR AlphaFoldDB; Q6ACZ8; -.
DR SMR; Q6ACZ8; -.
DR STRING; 281090.Lxx20300; -.
DR EnsemblBacteria; AAT89746; AAT89746; Lxx20300.
DR KEGG; lxx:Lxx20300; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_11; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000001306; 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..279
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000237201"
FT REGION 29..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 30287 MW; 21C5E3B09C4A01B2 CRC64;
MAIRNYKPTT PGRRGSSVAD FAEITRSNPE KSLLRPLSKS GGRNNQGRIT TRHIGGGHKR
QYRVIDFRRN DKDGVNAKVA HIEYDPNRTA RIALLHFLDG TKRYILAPAG LKQGNIVESG
AGADIKPGNN LPLCNIPTGT VVHAIELKPG GGAKLARSAG SSVRLVAKDG PYAQLRLPSG
EVRNVDARCR ATIGEVGNAE QSNINWGKAG RMRWKGVRPT VRGVAMNPID HPHGGGEGKT
SGGRHPVSPW GQKEGRTRHP NKESDKLIVR RRNAGKKRK