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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
 
 
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