RL2_BARBK
ID RL2_BARBK Reviewed; 277 AA.
AC A1USL7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB1 {ECO:0000255|HAMAP-Rule:MF_01320};
GN OrderedLocusNames=BARBAKC583_0669;
GN and
GN Name=rplB2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN OrderedLocusNames=BARBAKC583_0701;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000524; ABM44750.1; -; Genomic_DNA.
DR EMBL; CP000524; ABM45337.1; -; Genomic_DNA.
DR RefSeq; WP_005766902.1; NC_008783.1.
DR AlphaFoldDB; A1USL7; -.
DR SMR; A1USL7; -.
DR STRING; 360095.BARBAKC583_0669; -.
DR EnsemblBacteria; ABM44750; ABM44750; BARBAKC583_0701.
DR EnsemblBacteria; ABM45337; ABM45337; BARBAKC583_0669.
DR KEGG; bbk:BARBAKC583_0669; -.
DR KEGG; bbk:BARBAKC583_0701; -.
DR PATRIC; fig|360095.6.peg.680; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_5; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000000643; 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_0000309872"
FT REGION 222..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 30246 MW; DC11730B3DA2BE5B CRC64;
MALKHFNPTT SGQRQLVIVD RSGLYKGKPV KTLTEGLLSK GGRNNSGKIT ARFQGGRHKR
SYRFIDFKRL KLDVSAKVER LEYDPNRTAF IALIRYEDGQ LSYILAPQRL DVGDTVVAGL
SVDVKPGNAM PLGNMPVGAI VHNVEMKPGK GGQIARSAGA YAQLVGRDQG MAILRLNSGE
QRLVSSNCFA TVGAVSNPDH GNINDGKAGR SRWRGKRPHV RGVAMNPVDH PHGGGEGRTS
GGRHPVSPWG KPTKGKRTRS NKATDKFIMR SRHQRKK