RL2_BORBU
ID RL2_BORBU Reviewed; 277 AA.
AC P94270; O51434;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=BB_0481;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Perlee L., Qi H., Schwartz I.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; U78193; AAB36825.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66861.1; -; Genomic_DNA.
DR PIR; H70159; H70159.
DR RefSeq; NP_212615.1; NC_001318.1.
DR RefSeq; WP_002557072.1; NC_001318.1.
DR AlphaFoldDB; P94270; -.
DR SMR; P94270; -.
DR STRING; 224326.BB_0481; -.
DR PRIDE; P94270; -.
DR EnsemblBacteria; AAC66861; AAC66861; BB_0481.
DR GeneID; 56567916; -.
DR KEGG; bbu:BB_0481; -.
DR PATRIC; fig|224326.49.peg.872; -.
DR HOGENOM; CLU_036235_2_1_12; -.
DR OMA; SCIELRP; -.
DR Proteomes; UP000001807; 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..277
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129533"
FT REGION 32..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21
FT /note="F -> L (in Ref. 1; AAB36825)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="L -> K (in Ref. 1; AAB36825)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="S -> P (in Ref. 1; AAB36825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30591 MW; 6E668A2AC8CA5BEE CRC64;
MGIKTYKPKT SSLRYKTTLS FDDLSKGNDP LKSLTKGKKF KSGRDSSGRI SIRRRGGGHK
RKYRLIDFNR RDKFSIPARV ASIEYDPNRS ANIALLVYKD GEKRYIISPK GIKVGDVLES
GPNAPIKIGN ALPLENIPIG RTVHNIELNV GKGGQLIRSA GGYAMILASD GNYVTVKLSS
GEMRLIFKKC IATIGEIGNE DYANISIGKA GKSRWLGRRP KVRGVAMNPV DHPHGGGEGK
TSGGRHPVSP WGQPTKGYKT RKKKRYSDKF IIKRRNK